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USMLE - The Process Of Collagen Formation
http://www.usmlesuccess.net Understanding the process of collagen formation; essential USMLE Step 1 information. Don't forget to download your FREE USMLE Step 1 & Step 2 CK BIBLES at http://www.usmlesuccess.net/free-bible-download-page
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Integrin Binding Collagen - 3D model, Rate My Science
http://ratemyscience.com/ Publish and rate science
Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 50% of the whole-body protein content.
The tropocollagen or "collagen molecule" is a subunit of larger collagen aggregates such as fibrils. It is approximately 300 nm long and 1.5 nm in diameter, made up of three polypeptide stran
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Changes in Collagen Fibrils Damaged Suspensory Ligaments
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Type I Collagen Assembly
Type I Collagen Assembly
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Regional Changes in Collagen Fibril Diameter Distribution of Tendons
Perry Atangcho
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Collagen: Types and Synthesis Pathway
This video will cover the basics of the collagen types and the biochemical pathway of collagen synthesis.
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Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells
Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells. Andreas Herchenhan et al (2015), The Journal of Biological Chemistry http://dx.doi.org/10.1074/jbc.M115.641670
Lysyl oxidases (LOXs) are a family of copper- dependent oxido-deaminases that can modify the side-chain of lysyl residues in collagen and elastin, thereby leading to the spontaneous formation of non-
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Role of Decorin Core Protein in Collagen Organisation in Congenital Stromal Corneal Dystrophy (CSCD)
Role of Decorin Core Protein in Collagen Organisation in Congenital Stromal Corneal Dystrophy (CSCD). Christina S. Kamma-Lorger et al (2016), PLoS ONE http://dx.doi.org/10.1371/journal.pone.0147948
The role of Decorin in organising the extracellular matrix was examined in normal human corneas and in corneas from patients with Congenital Stromal Corneal Dystrophy (CSCD). In CSCD, corneal clouding
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I cut myself by accident and lost the tendons in 2 of my fingers permanantly
The common flexor tendon is a tendon that attaches to the medial epicondyle of the humerus (lower part of the bone of the upper arm that is near the elbow joint).
It serves as the upper attachment point for the superficial muscles of the front of the forearm: A tendon (or sinew) is a tough band of fibrous connective tissue that usually connects muscle to bone and is capable of withstanding tensio
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Periodontal Plus AB
PPAB is collagen fibril based formulation containing tetracycline hydrochloride (2 mg of tetracycline) in 25 mg of collagen fibrils. It has a dual mode of action, Via the active agent, Tetracycline, and the vehicle, high purity, bio compatible Type-I collagen which are used. This very unique features of PPAB enables the active agent as well as the vehicle to be able to work positively towards the
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Cell Motility and Mechanics in Three-Dimensional Collagen Matrices: Supplemental Video 1
A supplemental video from the 2010 review by Frederick Grinnell and W. Matthew Petroll, "Cell Motility and Mechanics in Three-Dimensional Collagen Matrices," from the Annual Review of Cell and Developmental Biology: http://www.annualreviews.org/doi/abs/10.1146/annurev.cellbio.042308.113318
Time-lapse video microscopy of cell migration shows that in addition to cells migrating out of the inner mat
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First full atomistic model of collagen microfibril
Collagen is the most abundant protein in humans, providing mechanical stability, elasticity, and strength to tissues such as bone, tendon, skin and cartilage. Collagen constitutes one-third of the human proteome, providing mechanical stability, elasticity, and strength to organisms and is the prime construction material in biology. Collagen is also the dominating material in the extracellular matr
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Golden Crocoduck nominees 2012 (Part 1)
Here are three nominees for the 2012 coveted Golden Crocoduck. Please don't ask how you can vote -- voting begins in October and details will be announced in a video at that time.
All three videos shown here can be found in the nominees' playlist on my channel.
2:45 Fake skeletons shown at http://michaelsheiser.com/PaleoBabble/2010/02/giant-paleobabble/
2:55 Fake skeleton from Worth 10
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internal structure of the human heart [ Medical videos ]
Structure of chordae tendineae in the left ventricle of the human heart
Abstract
The bicuspid (mitral) valve complex of the human heart consists of functional units which include the valve leaflets, chordae tendineae and the papillary muscles. The mechanical properties of these functional units depend to a large extent on the link between the muscle and the valve. This link is usually arranged in
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Application of Creme Egalisante by COLOSE
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fibrils, leading to skin regeneration. At the same time elasticity is improved and moisture content is increased, helping to smooth wrinkles on the face and neck. Our collagen cream also contains UVA & UVB Sun Filters.
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Atomic Force Microscopy - Fast scanning of collagen type I
Fast scanning of reconstituted type I collagen fibrillar layer. The video is a real-time screen recording of the AFM software for the JPK NanoWizard® ULTRA Speed AFM. The imaging in liquid starts with near 2.8 frames per second (fps) and shows the unaffected characteristic axial periodicity of 67 nm, by a subsequent zooming out of the original scanning area. The scanning was carried out with USC-
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Creme Egalisante by COLOSE
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fibrils, leading to skin regeneration. At the same time elasticity is improved and moisture content is increased, helping to smooth wrinkles on the face and neck. Our collagen cream also contains UVA & UVB Sun Filters.
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Collagen
Collagen /ˈkɒlədʒɨn/ is the main structural protein of the various connective tissues in animals. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin, and is also abundant in corneas, car
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What is Cartilage? what is cartilage made of
What is Cartilage?
What is Cartilage?,what is cartilage made of,what is cartilage function,what is cartilage for,what is cartilage and what does it doCartilage is an important structural component of the body. It is a firm tissue but is softer and much more flexible than bone.
Cartilage is a connective tissue found in many areas of the body including:
Joints between bones e.g. the elbows, knees
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Assembly of Type IV Collagen
The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds, and registers cognate alpha-chains for assembly of triple helical protomers that subsequently oligomeri
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Premier Dead Sea Collagen, Beta Carotene,and Seaweed Mask
Premier Dead Sea:
Collagen, Beta Carotene, and Seaweed Mask
=================================
http://bit.ly/1c8i5Es
The soluble form of collagen & Beta-carotene is the basis for the continual renewal of fibrils. These are dense chains of amino acids, which lie in the tissues forming a network of supporting elements to which the skin woes kits of elasticity. Moreover it increases the capacity of th
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What Is The Definition Of ADAMTS2 Medical Dictionary Free Online
what is the definition of ADAMTS2: A gene that encodes a metalloproteinase enzyme. This enzyme is responsible for processing type I, type II, and type V procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off of one end of the procollagen. The clipping step
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Anisotropic Collagen Fibrillogenesis within an accordion-like honeycomb scaffold
Visualization of the collagen fibril organization within the a pore of an accordion-like honeycomb scaffold, using fluorescence microscopy. (Jean and Engelmayr, Adv. Healh. Mater. 2012.)
USMLE - The Process Of Collagen Formation
http://www.usmlesuccess.net Understanding the process of collagen formation; essential USMLE Step 1 information. Don't forget to download your FREE USMLE Step...
http://www.usmlesuccess.net Understanding the process of collagen formation; essential USMLE Step 1 information. Don't forget to download your FREE USMLE Step 1 & Step 2 CK BIBLES at http://www.usmlesuccess.net/free-bible-download-page
wn.com/Usmle The Process Of Collagen Formation
http://www.usmlesuccess.net Understanding the process of collagen formation; essential USMLE Step 1 information. Don't forget to download your FREE USMLE Step 1 & Step 2 CK BIBLES at http://www.usmlesuccess.net/free-bible-download-page
- published: 22 Jul 2013
- views: 42752
Integrin Binding Collagen - 3D model, Rate My Science
http://ratemyscience.com/ Publish and rate science
Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making...
http://ratemyscience.com/ Publish and rate science
Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 50% of the whole-body protein content.
The tropocollagen or "collagen molecule" is a subunit of larger collagen aggregates such as fibrils. It is approximately 300 nm long and 1.5 nm in diameter, made up of three polypeptide strands (called alpha peptides), each possessing the conformation of a left-handed helix (its name is not to be confused with the commonly occurring alpha helix, a right-handed structure). These three left-handed helices are twisted together into a right-handed coiled coil, a triple helix or "super helix", a cooperative quaternary structure stabilized by numerous hydrogen bonds.
Design & production: Kosi Gramatikoff, PhD & Robert Liddington, PhD
wn.com/Integrin Binding Collagen 3D Model, Rate My Science
http://ratemyscience.com/ Publish and rate science
Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 50% of the whole-body protein content.
The tropocollagen or "collagen molecule" is a subunit of larger collagen aggregates such as fibrils. It is approximately 300 nm long and 1.5 nm in diameter, made up of three polypeptide strands (called alpha peptides), each possessing the conformation of a left-handed helix (its name is not to be confused with the commonly occurring alpha helix, a right-handed structure). These three left-handed helices are twisted together into a right-handed coiled coil, a triple helix or "super helix", a cooperative quaternary structure stabilized by numerous hydrogen bonds.
Design & production: Kosi Gramatikoff, PhD & Robert Liddington, PhD
- published: 03 Nov 2008
- views: 20003
Type I Collagen Assembly
Type I Collagen Assembly...
Type I Collagen Assembly
wn.com/Type I Collagen Assembly
Type I Collagen Assembly
- published: 05 Jul 2007
- views: 65583
Collagen: Types and Synthesis Pathway
This video will cover the basics of the collagen types and the biochemical pathway of collagen synthesis....
This video will cover the basics of the collagen types and the biochemical pathway of collagen synthesis.
wn.com/Collagen Types And Synthesis Pathway
This video will cover the basics of the collagen types and the biochemical pathway of collagen synthesis.
- published: 24 May 2013
- views: 26114
Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells
Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells. Andreas Herchenhan et al (2015), The Journal of Biological Chemistry ht...
Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells. Andreas Herchenhan et al (2015), The Journal of Biological Chemistry http://dx.doi.org/10.1074/jbc.M115.641670
Lysyl oxidases (LOXs) are a family of copper- dependent oxido-deaminases that can modify the side-chain of lysyl residues in collagen and elastin, thereby leading to the spontaneous formation of non-reducible aldehyde-derived inter-polypeptide chain cross-links. The consequences of LOX inhibition in producing lathyrism are well documented but the consequences on collagen fibril formation are less clear. Here we used β-aminoproprionitrile (BAPN) to inhibit LOX in tendon-like constructs (prepared from human tenocytes), which are an experimental model of cell- mediated collagen fibril formation. The improvement in structure and strength seen with time in control constructs was absent in constructs treated with BAPN. As expected, BAPN inhibited the formation of aldimine- derived cross-links in collagen and the constructs were mechanically weak. However, an unexpected finding was that BAPN- treatment led to structurally abnormal collagen fibrils with irregular profiles and widely dispersed diameters. Of special interest, the abnormal fibril profiles resembled those seen in some Ehlers-Danlos Syndrome (EDS) phenotypes. Importantly, the total collagen content developed normally, and there was no difference in COL1A1 gene expression. Collagen type V , decorin, fibromodulin and tenascin-X proteins were unaffected by the cross-link inhibition, suggesting that LOX regulates fibrillogenesis independently of these molecules. Collectively, the data show the importance of LOX on the mechanical development of early collagenous tissues, and that LOX is essential for correct collagen fibril shape formation.
wn.com/Lysyl Oxidase Activity Is Required For Ordered Collagen Fibrillogenesis By Tendon Cells
Lysyl Oxidase activity is required for ordered collagen fibrillogenesis by tendon cells. Andreas Herchenhan et al (2015), The Journal of Biological Chemistry http://dx.doi.org/10.1074/jbc.M115.641670
Lysyl oxidases (LOXs) are a family of copper- dependent oxido-deaminases that can modify the side-chain of lysyl residues in collagen and elastin, thereby leading to the spontaneous formation of non-reducible aldehyde-derived inter-polypeptide chain cross-links. The consequences of LOX inhibition in producing lathyrism are well documented but the consequences on collagen fibril formation are less clear. Here we used β-aminoproprionitrile (BAPN) to inhibit LOX in tendon-like constructs (prepared from human tenocytes), which are an experimental model of cell- mediated collagen fibril formation. The improvement in structure and strength seen with time in control constructs was absent in constructs treated with BAPN. As expected, BAPN inhibited the formation of aldimine- derived cross-links in collagen and the constructs were mechanically weak. However, an unexpected finding was that BAPN- treatment led to structurally abnormal collagen fibrils with irregular profiles and widely dispersed diameters. Of special interest, the abnormal fibril profiles resembled those seen in some Ehlers-Danlos Syndrome (EDS) phenotypes. Importantly, the total collagen content developed normally, and there was no difference in COL1A1 gene expression. Collagen type V , decorin, fibromodulin and tenascin-X proteins were unaffected by the cross-link inhibition, suggesting that LOX regulates fibrillogenesis independently of these molecules. Collectively, the data show the importance of LOX on the mechanical development of early collagenous tissues, and that LOX is essential for correct collagen fibril shape formation.
- published: 23 May 2015
- views: 110
Role of Decorin Core Protein in Collagen Organisation in Congenital Stromal Corneal Dystrophy (CSCD)
Role of Decorin Core Protein in Collagen Organisation in Congenital Stromal Corneal Dystrophy (CSCD). Christina S. Kamma-Lorger et al (2016), PLoS ONE http://dx...
Role of Decorin Core Protein in Collagen Organisation in Congenital Stromal Corneal Dystrophy (CSCD). Christina S. Kamma-Lorger et al (2016), PLoS ONE http://dx.doi.org/10.1371/journal.pone.0147948
The role of Decorin in organising the extracellular matrix was examined in normal human corneas and in corneas from patients with Congenital Stromal Corneal Dystrophy (CSCD). In CSCD, corneal clouding occurs due to a truncating mutation (c.967delT) in the decorin (DCN) gene. Normal human Decorin protein and the truncated one were reconstructed in silico using homology modelling techniques to explore structural changes in the diseased protein. Corneal CSCD specimens were also examined using 3-D electron tomography and Small Angle X-ray diffraction (SAXS), to image the collagen-proteoglycan arrangement and to quantify fibrillar diameters, respectively. Homology modelling showed that truncated Decorin had a different spatial geometry to the normal one, with the truncation removing a major part of the site that interacts with collagen, compromising its ability to bind effectively. Electron tomography showed regions of abnormal stroma, where collagen fibrils came together to form thicker fibrillar structures, showing that Decorin plays a key role in the maintenance of the order in the normal corneal extracellular matrix. Average diameter of individual fibrils throughout the thickness of the cornea however remained normal.
wn.com/Role Of Decorin Core Protein In Collagen Organisation In Congenital Stromal Corneal Dystrophy (Cscd)
Role of Decorin Core Protein in Collagen Organisation in Congenital Stromal Corneal Dystrophy (CSCD). Christina S. Kamma-Lorger et al (2016), PLoS ONE http://dx.doi.org/10.1371/journal.pone.0147948
The role of Decorin in organising the extracellular matrix was examined in normal human corneas and in corneas from patients with Congenital Stromal Corneal Dystrophy (CSCD). In CSCD, corneal clouding occurs due to a truncating mutation (c.967delT) in the decorin (DCN) gene. Normal human Decorin protein and the truncated one were reconstructed in silico using homology modelling techniques to explore structural changes in the diseased protein. Corneal CSCD specimens were also examined using 3-D electron tomography and Small Angle X-ray diffraction (SAXS), to image the collagen-proteoglycan arrangement and to quantify fibrillar diameters, respectively. Homology modelling showed that truncated Decorin had a different spatial geometry to the normal one, with the truncation removing a major part of the site that interacts with collagen, compromising its ability to bind effectively. Electron tomography showed regions of abnormal stroma, where collagen fibrils came together to form thicker fibrillar structures, showing that Decorin plays a key role in the maintenance of the order in the normal corneal extracellular matrix. Average diameter of individual fibrils throughout the thickness of the cornea however remained normal.
- published: 01 Feb 2016
- views: 2
I cut myself by accident and lost the tendons in 2 of my fingers permanantly
The common flexor tendon is a tendon that attaches to the medial epicondyle of the humerus (lower part of the bone of the upper arm that is near the elbow joint...
The common flexor tendon is a tendon that attaches to the medial epicondyle of the humerus (lower part of the bone of the upper arm that is near the elbow joint).
It serves as the upper attachment point for the superficial muscles of the front of the forearm: A tendon (or sinew) is a tough band of fibrous connective tissue that usually connects muscle to bone and is capable of withstanding tension. Tendons are similar to ligaments and fasciae; all three are made of collagen. Ligaments join one bone to another bone; fasciae connect muscles to other muscles. Tendons and muscles work together to move bones. Tendons have been traditionally considered to simply be a mechanism by which muscles connect to bone, functioning simply to transmit forces. This connection allows tendons to passively modulate forces during locomotion, providing additional stability with no active work. However, over the past two decades, much research focused on the elastic properties of some tendons and their ability to function as springs. Not all tendons are required to perform the same functional role, with some predominantly positioning limbs, such as the fingers when writing (positional tendons) and others acting as springs to make locomotion more efficient (energy storing tendons).[16] Energy storing tendons can store and recover energy at high efficiency. For example, during a human stride, the Achilles tendon stretches as the ankle joint dorsiflexes. During the last portion of the stride, as the foot plantar-flexes (pointing the toes down), the stored elastic energy is released. Furthermore, because the tendon stretches, the muscle is able to function with less or even no change in length, allowing the muscle to generate greater force.
The mechanical properties of the tendon are dependent on the collagen fiber diameter and orientation. The collagen fibrils are parallel to each other and closely packed, but show a wave-like appearance due to planar undulations, or crimps, on a scale of several micrometers. In tendons, the collagen fibres have some flexibility due to the absence of hydroxyproline and proline residues at specific locations in the amino acid sequence, which allows the formation of other conformations such as bends or internal loops in the triple helix and results in the development of crimps The crimps in the collagen fibrils allow the tendons to have some flexibility as well as a low compressive stiffness. In addition, because the tendon is a multi-stranded structure made up of many partially independent fibrils and fascicles, it does not behave as a single rod, and this property also contributes to its flexibility. The proteoglycan components of tendons also are important to the mechanical properties. While the collagen fibrils allow tendons to resist tensile stress, the proteoglycans allow them to resist compressive stress. These molecules are very hydrophilic, meaning that they can absorb a large amount of water and therefore have a high swelling ratio. Since they are noncovalently bound to the fibrils, they may reversibly associate and disassociate so that the bridges between fibrils can be broken and reformed. This process may be involved in allowing the fibril to elongate and decrease in diameter under tension However, the proteoglycans may also have a role in the tensile properties of tendon. The structure of tendon is effectively a fibre composite material, built as a series of hierarchical levels. At each level of the hierarchy, the collagen units are bound together by either collagen crosslinks, or the proteglycans, to create a structure highly resistant to tensile load.The elongation and the strain of the collagen fibrils alone have been shown to be much lower than the total elongation and strain of the entire tendon under the same amount of stress, demonstrating that the proteoglycan-rich matrix must also undergo deformation, and stiffening of the matrix occurs at high strain rates This deformation of the non-collagenous matrix occurs at all levels of the tendon hierarchy, and by modulating the organisation and structure of this matrix, the different mechanical properties required by different tendons can be achieved Energy storing tendons have been shown to utilise significant amounts of sliding between fascicles to enable the high strain characteristics they require, whilst positional tendons rely more heavily on sliding between collagen fibres and fibrils However, recent data suggests that energy storing tendons may also contain fascicles which are twisted, or helical, in nature - an arrangement that would be highly beneficial for providing the spring-like behaviour required in these tendons. Several studies have demonstrated that tendons respond to changes in mechanical loading with growth and remodeling processes, much like bones. In particular, a study showed that disuse of the
wn.com/I Cut Myself By Accident And Lost The Tendons In 2 Of My Fingers Permanantly
The common flexor tendon is a tendon that attaches to the medial epicondyle of the humerus (lower part of the bone of the upper arm that is near the elbow joint).
It serves as the upper attachment point for the superficial muscles of the front of the forearm: A tendon (or sinew) is a tough band of fibrous connective tissue that usually connects muscle to bone and is capable of withstanding tension. Tendons are similar to ligaments and fasciae; all three are made of collagen. Ligaments join one bone to another bone; fasciae connect muscles to other muscles. Tendons and muscles work together to move bones. Tendons have been traditionally considered to simply be a mechanism by which muscles connect to bone, functioning simply to transmit forces. This connection allows tendons to passively modulate forces during locomotion, providing additional stability with no active work. However, over the past two decades, much research focused on the elastic properties of some tendons and their ability to function as springs. Not all tendons are required to perform the same functional role, with some predominantly positioning limbs, such as the fingers when writing (positional tendons) and others acting as springs to make locomotion more efficient (energy storing tendons).[16] Energy storing tendons can store and recover energy at high efficiency. For example, during a human stride, the Achilles tendon stretches as the ankle joint dorsiflexes. During the last portion of the stride, as the foot plantar-flexes (pointing the toes down), the stored elastic energy is released. Furthermore, because the tendon stretches, the muscle is able to function with less or even no change in length, allowing the muscle to generate greater force.
The mechanical properties of the tendon are dependent on the collagen fiber diameter and orientation. The collagen fibrils are parallel to each other and closely packed, but show a wave-like appearance due to planar undulations, or crimps, on a scale of several micrometers. In tendons, the collagen fibres have some flexibility due to the absence of hydroxyproline and proline residues at specific locations in the amino acid sequence, which allows the formation of other conformations such as bends or internal loops in the triple helix and results in the development of crimps The crimps in the collagen fibrils allow the tendons to have some flexibility as well as a low compressive stiffness. In addition, because the tendon is a multi-stranded structure made up of many partially independent fibrils and fascicles, it does not behave as a single rod, and this property also contributes to its flexibility. The proteoglycan components of tendons also are important to the mechanical properties. While the collagen fibrils allow tendons to resist tensile stress, the proteoglycans allow them to resist compressive stress. These molecules are very hydrophilic, meaning that they can absorb a large amount of water and therefore have a high swelling ratio. Since they are noncovalently bound to the fibrils, they may reversibly associate and disassociate so that the bridges between fibrils can be broken and reformed. This process may be involved in allowing the fibril to elongate and decrease in diameter under tension However, the proteoglycans may also have a role in the tensile properties of tendon. The structure of tendon is effectively a fibre composite material, built as a series of hierarchical levels. At each level of the hierarchy, the collagen units are bound together by either collagen crosslinks, or the proteglycans, to create a structure highly resistant to tensile load.The elongation and the strain of the collagen fibrils alone have been shown to be much lower than the total elongation and strain of the entire tendon under the same amount of stress, demonstrating that the proteoglycan-rich matrix must also undergo deformation, and stiffening of the matrix occurs at high strain rates This deformation of the non-collagenous matrix occurs at all levels of the tendon hierarchy, and by modulating the organisation and structure of this matrix, the different mechanical properties required by different tendons can be achieved Energy storing tendons have been shown to utilise significant amounts of sliding between fascicles to enable the high strain characteristics they require, whilst positional tendons rely more heavily on sliding between collagen fibres and fibrils However, recent data suggests that energy storing tendons may also contain fascicles which are twisted, or helical, in nature - an arrangement that would be highly beneficial for providing the spring-like behaviour required in these tendons. Several studies have demonstrated that tendons respond to changes in mechanical loading with growth and remodeling processes, much like bones. In particular, a study showed that disuse of the
- published: 04 Jan 2016
- views: 42
Periodontal Plus AB
PPAB is collagen fibril based formulation containing tetracycline hydrochloride (2 mg of tetracycline) in 25 mg of collagen fibrils. It has a dual mode of actio...
PPAB is collagen fibril based formulation containing tetracycline hydrochloride (2 mg of tetracycline) in 25 mg of collagen fibrils. It has a dual mode of action, Via the active agent, Tetracycline, and the vehicle, high purity, bio compatible Type-I collagen which are used. This very unique features of PPAB enables the active agent as well as the vehicle to be able to work positively towards the repair of the Periodontal lesion.
Packing Details
Each box contains 4 Vial.
Quantity
Each Vial contains 25mg totally 100mgs
for more details visit http://www.abpdental.com/products.html
wn.com/Periodontal Plus Ab
PPAB is collagen fibril based formulation containing tetracycline hydrochloride (2 mg of tetracycline) in 25 mg of collagen fibrils. It has a dual mode of action, Via the active agent, Tetracycline, and the vehicle, high purity, bio compatible Type-I collagen which are used. This very unique features of PPAB enables the active agent as well as the vehicle to be able to work positively towards the repair of the Periodontal lesion.
Packing Details
Each box contains 4 Vial.
Quantity
Each Vial contains 25mg totally 100mgs
for more details visit http://www.abpdental.com/products.html
- published: 12 Jul 2014
- views: 180
Cell Motility and Mechanics in Three-Dimensional Collagen Matrices: Supplemental Video 1
A supplemental video from the 2010 review by Frederick Grinnell and W. Matthew Petroll, "Cell Motility and Mechanics in Three-Dimensional Collagen Matrices," fr...
A supplemental video from the 2010 review by Frederick Grinnell and W. Matthew Petroll, "Cell Motility and Mechanics in Three-Dimensional Collagen Matrices," from the Annual Review of Cell and Developmental Biology: http://www.annualreviews.org/doi/abs/10.1146/annurev.cellbio.042308.113318
Time-lapse video microscopy of cell migration shows that in addition to cells migrating out of the inner matrix, collagen fibrils in the outer matrix translocate toward the interface between the outer and inner matrices.
wn.com/Cell Motility And Mechanics In Three Dimensional Collagen Matrices Supplemental Video 1
A supplemental video from the 2010 review by Frederick Grinnell and W. Matthew Petroll, "Cell Motility and Mechanics in Three-Dimensional Collagen Matrices," from the Annual Review of Cell and Developmental Biology: http://www.annualreviews.org/doi/abs/10.1146/annurev.cellbio.042308.113318
Time-lapse video microscopy of cell migration shows that in addition to cells migrating out of the inner matrix, collagen fibrils in the outer matrix translocate toward the interface between the outer and inner matrices.
- published: 24 Apr 2012
- views: 574
First full atomistic model of collagen microfibril
Collagen is the most abundant protein in humans, providing mechanical stability, elasticity, and strength to tissues such as bone, tendon, skin and cartilage. C...
Collagen is the most abundant protein in humans, providing mechanical stability, elasticity, and strength to tissues such as bone, tendon, skin and cartilage. Collagen constitutes one-third of the human proteome, providing mechanical stability, elasticity, and strength to organisms and is the prime construction material in biology. Collagen is also the dominating material in the extracellular matrix and its stiffness controls cell differentiation, growth, and pathology. However, the origin of the unique mechanical properties of collagenous tissues, and in particular its stiffness, extensibility, and nonlinear mechanical response at large deformation, remains unknown.
By using X-ray diffraction data of a collagen fibril (Orgel, J. P. R. O. et al. Proc. Natl. Acad. Sci. 2006, 103, 9001) we can construct and simulate an experimentally validated model of the nanomechanics of a collagen microfibril that incorporates the full biochemical details of the amino acid sequence of constituting molecules and the nanoscale molecular arrangement.
We found by direct mechanical testing that hydrated (wet) collagen microfibrils feature a Young's modulus of ≈300 MPa at small, and ≈1.2 GPa at larger deformation in excess of 10% strain, which is in excellent agreement with experimental data. We found that dehydrated (dry) collagen microfibrils show a significantly increased Young's modulus of ≈1.8-2.25 GPa, which is in agreement with experimental measurements and owing to tighter molecular packing.
Here we show a simulated 10 ns time lapse of the collagen fibril atomistic model during equilibration. It shows the typical periodic banding (called "D-banding") which arise due to the staggering of molecules within the fibril. The close-up shows the fine atomistic details in the "overlap" region (the denser area) and then move to the "gap" region (the less dense area).
The atomistic model of collagen fibril mechanics now enables the bottom-up elucidation of structure-property relationships in collagen materials (e.g., tendon, bone), including studies of genetic disease where the incorporation of biochemical details is essential.
For more information, see:
A. Gautieri, S. Vesentini , A. Redaelli, M.J. Buehler , "Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up," Nano Letters, Vol. 11(2), pp. 757-766, 2011
http://pubs.acs.org/doi/abs/10.1021/nl103943u
wn.com/First Full Atomistic Model Of Collagen Microfibril
Collagen is the most abundant protein in humans, providing mechanical stability, elasticity, and strength to tissues such as bone, tendon, skin and cartilage. Collagen constitutes one-third of the human proteome, providing mechanical stability, elasticity, and strength to organisms and is the prime construction material in biology. Collagen is also the dominating material in the extracellular matrix and its stiffness controls cell differentiation, growth, and pathology. However, the origin of the unique mechanical properties of collagenous tissues, and in particular its stiffness, extensibility, and nonlinear mechanical response at large deformation, remains unknown.
By using X-ray diffraction data of a collagen fibril (Orgel, J. P. R. O. et al. Proc. Natl. Acad. Sci. 2006, 103, 9001) we can construct and simulate an experimentally validated model of the nanomechanics of a collagen microfibril that incorporates the full biochemical details of the amino acid sequence of constituting molecules and the nanoscale molecular arrangement.
We found by direct mechanical testing that hydrated (wet) collagen microfibrils feature a Young's modulus of ≈300 MPa at small, and ≈1.2 GPa at larger deformation in excess of 10% strain, which is in excellent agreement with experimental data. We found that dehydrated (dry) collagen microfibrils show a significantly increased Young's modulus of ≈1.8-2.25 GPa, which is in agreement with experimental measurements and owing to tighter molecular packing.
Here we show a simulated 10 ns time lapse of the collagen fibril atomistic model during equilibration. It shows the typical periodic banding (called "D-banding") which arise due to the staggering of molecules within the fibril. The close-up shows the fine atomistic details in the "overlap" region (the denser area) and then move to the "gap" region (the less dense area).
The atomistic model of collagen fibril mechanics now enables the bottom-up elucidation of structure-property relationships in collagen materials (e.g., tendon, bone), including studies of genetic disease where the incorporation of biochemical details is essential.
For more information, see:
A. Gautieri, S. Vesentini , A. Redaelli, M.J. Buehler , "Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up," Nano Letters, Vol. 11(2), pp. 757-766, 2011
http://pubs.acs.org/doi/abs/10.1021/nl103943u
- published: 02 Aug 2011
- views: 2961
Golden Crocoduck nominees 2012 (Part 1)
Here are three nominees for the 2012 coveted Golden Crocoduck. Please don't ask how you can vote -- voting begins in October and details will be announced in a ...
Here are three nominees for the 2012 coveted Golden Crocoduck. Please don't ask how you can vote -- voting begins in October and details will be announced in a video at that time.
All three videos shown here can be found in the nominees' playlist on my channel.
2:45 Fake skeletons shown at http://michaelsheiser.com/PaleoBabble/2010/02/giant-paleobabble/
2:55 Fake skeleton from Worth 1000
3:08 Hindu Voice story from http://karsewak.blogspot.com.au/2007/03/bhimas-son-gadhotkach-like-skeleton.html
3:29 "Skeleton of Giant is Internet Hoax" - National Geographic, Dec 14 2007.
3:41 Worth1000 competition entry http://fx.worth1000.com/entries/18533/giants
4:39 http://www.biblebelievers.org.au/giants.htm
5:05 "Fossilized" giant described at http://www.archive.org/stream/cu31924092530546/cu31924092530546_djvu.txt
8:06 onwards --
"Type V Collagen Controls the Initiation of Collagen
Fibril Assembly*
Richard J. Wenstrup et al., Aug 2004
"Collagen fibril formation"
Karl E. Kadler 1996
"Collagen fibril morphology and organization: Implications for force
transmission in ligament and tendon"
Paolo P. Provenzano 2005
"Extracellular Compartments in Tendon Morphogenesis:
Collagen Fibril, Bundle, and Macroaggregate Formation"
David E. Birk et al 1986
Clip of Jenna Bus from "Jenna Bush - Predator 2" on YouTube
For those not familiar with cockney rhyming slang:
Frog and toad = road
Jimmy riddle = piddle (urination)
Adam and Eve = believe
Porky pie = lie
wn.com/Golden Crocoduck Nominees 2012 (Part 1)
Here are three nominees for the 2012 coveted Golden Crocoduck. Please don't ask how you can vote -- voting begins in October and details will be announced in a video at that time.
All three videos shown here can be found in the nominees' playlist on my channel.
2:45 Fake skeletons shown at http://michaelsheiser.com/PaleoBabble/2010/02/giant-paleobabble/
2:55 Fake skeleton from Worth 1000
3:08 Hindu Voice story from http://karsewak.blogspot.com.au/2007/03/bhimas-son-gadhotkach-like-skeleton.html
3:29 "Skeleton of Giant is Internet Hoax" - National Geographic, Dec 14 2007.
3:41 Worth1000 competition entry http://fx.worth1000.com/entries/18533/giants
4:39 http://www.biblebelievers.org.au/giants.htm
5:05 "Fossilized" giant described at http://www.archive.org/stream/cu31924092530546/cu31924092530546_djvu.txt
8:06 onwards --
"Type V Collagen Controls the Initiation of Collagen
Fibril Assembly*
Richard J. Wenstrup et al., Aug 2004
"Collagen fibril formation"
Karl E. Kadler 1996
"Collagen fibril morphology and organization: Implications for force
transmission in ligament and tendon"
Paolo P. Provenzano 2005
"Extracellular Compartments in Tendon Morphogenesis:
Collagen Fibril, Bundle, and Macroaggregate Formation"
David E. Birk et al 1986
Clip of Jenna Bus from "Jenna Bush - Predator 2" on YouTube
For those not familiar with cockney rhyming slang:
Frog and toad = road
Jimmy riddle = piddle (urination)
Adam and Eve = believe
Porky pie = lie
- published: 12 Mar 2012
- views: 106166
internal structure of the human heart [ Medical videos ]
Structure of chordae tendineae in the left ventricle of the human heart
Abstract
The bicuspid (mitral) valve complex of the human heart consists of functional u...
Structure of chordae tendineae in the left ventricle of the human heart
Abstract
The bicuspid (mitral) valve complex of the human heart consists of functional units which include the valve leaflets, chordae tendineae and the papillary muscles. The mechanical properties of these functional units depend to a large extent on the link between the muscle and the valve. This link is usually arranged in a branching network of avascular tendinous chordae composed of collagen and elastic fibres, which transmit contractions of the papillary muscle to the valve leaflets. In order to perform their function efficiently, the chordae have to possess a high degree of elasticity, as well as considerable strength and endurance. Human chordae tendineae originating from the left ventricles were obtained from 7 embalmed cadavers and 6 postmortem subjects of various ages. Samples washed in saline were fixed or postfixed in 9% formol saline. Observations were made by illuminating the chordae along their axes. The reflected images originating from the superficial collagenous layers of the relaxed chordae showed a striped pattern 11 μm in width. Scanning electron and light microscopy of the chordae confirmed an undulating pattern of collagen fibrils arranged in bundles of planar waves in register and around the entire circumference of the chorda. The dimensions of the waves correlated with those of the striped reflected pattern. The observed undulating arrangement of the collagen fibrils appears to produce an inherent built-in elasticity which is likely to be of considerable advantage for a tissue which is under continuous repetitive stress. The chordae were covered by endocardium composed of a superficial layer of smooth squamous endothelial cells and an underlying dense layer of elastic fibres. It is suggested that the relaxed striped chordae, consisting of undulating collagen fibrils, straighten when the chordae become stretched by papillary muscle contraction, thereby mitigating the peak stress developed during muscle contraction. On relaxation the elastic tissue tends to return the collagen to its wavy configuration. It is also suggested that the regular wavy pattern of collagen seen in young individuals gradually changes with age by elongation of the wave pattern which eventually becomes randomised. In addition, with increasing age, substantial cushions of connective tissue appear below endocardium while the dense collagenous core has a reduced cross-sectional area which may lead to stretching and eventual rupture of the chordae.
wn.com/Internal Structure Of The Human Heart Medical Videos
Structure of chordae tendineae in the left ventricle of the human heart
Abstract
The bicuspid (mitral) valve complex of the human heart consists of functional units which include the valve leaflets, chordae tendineae and the papillary muscles. The mechanical properties of these functional units depend to a large extent on the link between the muscle and the valve. This link is usually arranged in a branching network of avascular tendinous chordae composed of collagen and elastic fibres, which transmit contractions of the papillary muscle to the valve leaflets. In order to perform their function efficiently, the chordae have to possess a high degree of elasticity, as well as considerable strength and endurance. Human chordae tendineae originating from the left ventricles were obtained from 7 embalmed cadavers and 6 postmortem subjects of various ages. Samples washed in saline were fixed or postfixed in 9% formol saline. Observations were made by illuminating the chordae along their axes. The reflected images originating from the superficial collagenous layers of the relaxed chordae showed a striped pattern 11 μm in width. Scanning electron and light microscopy of the chordae confirmed an undulating pattern of collagen fibrils arranged in bundles of planar waves in register and around the entire circumference of the chorda. The dimensions of the waves correlated with those of the striped reflected pattern. The observed undulating arrangement of the collagen fibrils appears to produce an inherent built-in elasticity which is likely to be of considerable advantage for a tissue which is under continuous repetitive stress. The chordae were covered by endocardium composed of a superficial layer of smooth squamous endothelial cells and an underlying dense layer of elastic fibres. It is suggested that the relaxed striped chordae, consisting of undulating collagen fibrils, straighten when the chordae become stretched by papillary muscle contraction, thereby mitigating the peak stress developed during muscle contraction. On relaxation the elastic tissue tends to return the collagen to its wavy configuration. It is also suggested that the regular wavy pattern of collagen seen in young individuals gradually changes with age by elongation of the wave pattern which eventually becomes randomised. In addition, with increasing age, substantial cushions of connective tissue appear below endocardium while the dense collagenous core has a reduced cross-sectional area which may lead to stretching and eventual rupture of the chordae.
- published: 29 Aug 2015
- views: 41
Application of Creme Egalisante by COLOSE
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fib...
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fibrils, leading to skin regeneration. At the same time elasticity is improved and moisture content is increased, helping to smooth wrinkles on the face and neck. Our collagen cream also contains UVA & UVB Sun Filters.
wn.com/Application Of Creme Egalisante By Colose
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fibrils, leading to skin regeneration. At the same time elasticity is improved and moisture content is increased, helping to smooth wrinkles on the face and neck. Our collagen cream also contains UVA & UVB Sun Filters.
- published: 08 Feb 2011
- views: 973
Atomic Force Microscopy - Fast scanning of collagen type I
Fast scanning of reconstituted type I collagen fibrillar layer. The video is a real-time screen recording of the AFM software for the JPK NanoWizard® ULTRA Spe...
Fast scanning of reconstituted type I collagen fibrillar layer. The video is a real-time screen recording of the AFM software for the JPK NanoWizard® ULTRA Speed AFM. The imaging in liquid starts with near 2.8 frames per second (fps) and shows the unaffected characteristic axial periodicity of 67 nm, by a subsequent zooming out of the original scanning area. The scanning was carried out with USC-F0.3-k0.3 cantilever from NanoWorld.
Read more about the NanoWizard® ULTRA Speed and check if it is available in your region on our website: http://www.jpk.com/nanowizard-r-ultra-speed-overview.764.en.html
wn.com/Atomic Force Microscopy Fast Scanning Of Collagen Type I
Fast scanning of reconstituted type I collagen fibrillar layer. The video is a real-time screen recording of the AFM software for the JPK NanoWizard® ULTRA Speed AFM. The imaging in liquid starts with near 2.8 frames per second (fps) and shows the unaffected characteristic axial periodicity of 67 nm, by a subsequent zooming out of the original scanning area. The scanning was carried out with USC-F0.3-k0.3 cantilever from NanoWorld.
Read more about the NanoWizard® ULTRA Speed and check if it is available in your region on our website: http://www.jpk.com/nanowizard-r-ultra-speed-overview.764.en.html
- published: 12 Feb 2015
- views: 339
Creme Egalisante by COLOSE
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fib...
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fibrils, leading to skin regeneration. At the same time elasticity is improved and moisture content is increased, helping to smooth wrinkles on the face and neck. Our collagen cream also contains UVA & UVB Sun Filters.
wn.com/Creme Egalisante By Colose
This anti-aging skin care cream is designed to reduce the skin aging process and to regulate moisture. The Collagen stimulates the formation of new collagen fibrils, leading to skin regeneration. At the same time elasticity is improved and moisture content is increased, helping to smooth wrinkles on the face and neck. Our collagen cream also contains UVA & UVB Sun Filters.
- published: 08 Feb 2011
- views: 548
Collagen
Collagen /ˈkɒlədʒɨn/ is the main structural protein of the various connective tissues in animals. As the main component of connective tissue, it is the most ab...
Collagen /ˈkɒlədʒɨn/ is the main structural protein of the various connective tissues in animals. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin, and is also abundant in corneas, cartilage, bones, blood vessels, the gut, and intervertebral discs. The fibroblast is the most common cell that creates collagen.
This video targeted to blind users.
Attribution:
Article text available under CC-BY-SA
Creative Commons image source in video
wn.com/Collagen
Collagen /ˈkɒlədʒɨn/ is the main structural protein of the various connective tissues in animals. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin, and is also abundant in corneas, cartilage, bones, blood vessels, the gut, and intervertebral discs. The fibroblast is the most common cell that creates collagen.
This video targeted to blind users.
Attribution:
Article text available under CC-BY-SA
Creative Commons image source in video
- published: 05 May 2014
- views: 665
What is Cartilage? what is cartilage made of
What is Cartilage?
What is Cartilage?,what is cartilage made of,what is cartilage function,what is cartilage for,what is cartilage and what does it doCartilage ...
What is Cartilage?
What is Cartilage?,what is cartilage made of,what is cartilage function,what is cartilage for,what is cartilage and what does it doCartilage is an important structural component of the body. It is a firm tissue but is softer and much more flexible than bone.
Cartilage is a connective tissue found in many areas of the body including:
Joints between bones e.g. the elbows, knees and ankles
Ends of the ribs
Between the vertebrae in the spine
Ears and nose
Bronchial tubes or airways
Cartilage is made up of specialized cells called chondrocytes. These chondrocytes produce large amounts of extracellular matrix composed of collagen fibres, proteoglycan, and elastin fibers. There are no blood vessels in cartilage to supply the chondrocytes with nutrients.
Instead, nutrients diffuse through a dense connective tissue surrounding the cartilage (called the perichondrium) and into the core of the cartilage. Due to the lack of blood vessels, cartilage grows and repairs more slowly than other tissues.
Cartilage type
Cartilage is categorized into three types which include:
Hyaline cartilage
This is a low-friction, wear-resistant tissue present within joints that is designed to bear and distribute weight. It is a strong, rubbery, flexible tissue but has a poor regenerative capacity.
Elastic cartilage
Elastic cartilage is more flexible that hyaline cartilage and is present in the ear, larynx and epiglottis.
Fibrocartilage
Fibrocartilage is a tough and inflexible form of cartilage found in the knee and between vertebrae.
Articular cartilage
Articular cartilage is the hyaline cartilage that lies on the surface of bones. This cartilage is often described in terms of four zones between the articular surface and the subchondral bone which include:
The surface or superficial tangential zone
This cartilage covers the articular surface and has a smooth contour that allows gliding of the ends of the bones and resists shear. It forms around 10% to 20% of articular cartilage thickness and has the highest collagen content of all the zones.
The collagen fibrils are densely packed and are aligned in a highly organized manner parallel to the articular surface. The chondrocytes in this zone are elongated in shape.
The middle (or transitional) zone
The middle zone makes up 40% to 60% of the articular cartilage volume. The collagen fibrils are thicker and aligned loosely and not in parallel to the surface. Chondrocytes in this layer are more rounded.
The deep zone
This makes up 30% of the cartilage. The collagen fibrils are large in diameter and aligned perpendicular to the articular surface. This layer has the highest proportion of proteoglycan and lowest concentration of water. The chondrocytes are arranged in a columnar fashion, parallel to the collagen fibers.
The calcified zone
This lies directly on the subchondral bone and contains small cells in a chondroid matrix that has apatitic salts scattered through it.
what is cartilage in the knee,what is cartilage piercing,what is cartilage used for,what is cartilage matrix,what is cartilage attached to,what is cartilage damage
wn.com/What Is Cartilage What Is Cartilage Made Of
What is Cartilage?
What is Cartilage?,what is cartilage made of,what is cartilage function,what is cartilage for,what is cartilage and what does it doCartilage is an important structural component of the body. It is a firm tissue but is softer and much more flexible than bone.
Cartilage is a connective tissue found in many areas of the body including:
Joints between bones e.g. the elbows, knees and ankles
Ends of the ribs
Between the vertebrae in the spine
Ears and nose
Bronchial tubes or airways
Cartilage is made up of specialized cells called chondrocytes. These chondrocytes produce large amounts of extracellular matrix composed of collagen fibres, proteoglycan, and elastin fibers. There are no blood vessels in cartilage to supply the chondrocytes with nutrients.
Instead, nutrients diffuse through a dense connective tissue surrounding the cartilage (called the perichondrium) and into the core of the cartilage. Due to the lack of blood vessels, cartilage grows and repairs more slowly than other tissues.
Cartilage type
Cartilage is categorized into three types which include:
Hyaline cartilage
This is a low-friction, wear-resistant tissue present within joints that is designed to bear and distribute weight. It is a strong, rubbery, flexible tissue but has a poor regenerative capacity.
Elastic cartilage
Elastic cartilage is more flexible that hyaline cartilage and is present in the ear, larynx and epiglottis.
Fibrocartilage
Fibrocartilage is a tough and inflexible form of cartilage found in the knee and between vertebrae.
Articular cartilage
Articular cartilage is the hyaline cartilage that lies on the surface of bones. This cartilage is often described in terms of four zones between the articular surface and the subchondral bone which include:
The surface or superficial tangential zone
This cartilage covers the articular surface and has a smooth contour that allows gliding of the ends of the bones and resists shear. It forms around 10% to 20% of articular cartilage thickness and has the highest collagen content of all the zones.
The collagen fibrils are densely packed and are aligned in a highly organized manner parallel to the articular surface. The chondrocytes in this zone are elongated in shape.
The middle (or transitional) zone
The middle zone makes up 40% to 60% of the articular cartilage volume. The collagen fibrils are thicker and aligned loosely and not in parallel to the surface. Chondrocytes in this layer are more rounded.
The deep zone
This makes up 30% of the cartilage. The collagen fibrils are large in diameter and aligned perpendicular to the articular surface. This layer has the highest proportion of proteoglycan and lowest concentration of water. The chondrocytes are arranged in a columnar fashion, parallel to the collagen fibers.
The calcified zone
This lies directly on the subchondral bone and contains small cells in a chondroid matrix that has apatitic salts scattered through it.
what is cartilage in the knee,what is cartilage piercing,what is cartilage used for,what is cartilage matrix,what is cartilage attached to,what is cartilage damage
- published: 01 Dec 2014
- views: 2618
Assembly of Type IV Collagen
The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have divers...
The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds, and registers cognate alpha-chains for assembly of triple helical protomers that subsequently oligomerize into specific suprastructures. In this article, we review recent findings on the mechanism of chain selection and infer that terminal noncollagenous domains function as recognition modules in trimerization and are therefore key determinants of specificity in the assembly of suprastructures. This mechanism is also illustrated with computer-generated animations.
http://www.ncbi.nlm.nih.gov/pubmed/17082192
wn.com/Assembly Of Type Iv Collagen
The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds, and registers cognate alpha-chains for assembly of triple helical protomers that subsequently oligomerize into specific suprastructures. In this article, we review recent findings on the mechanism of chain selection and infer that terminal noncollagenous domains function as recognition modules in trimerization and are therefore key determinants of specificity in the assembly of suprastructures. This mechanism is also illustrated with computer-generated animations.
http://www.ncbi.nlm.nih.gov/pubmed/17082192
- published: 05 Jun 2014
- views: 597
Premier Dead Sea Collagen, Beta Carotene,and Seaweed Mask
Premier Dead Sea:
Collagen, Beta Carotene, and Seaweed Mask
=================================
http://bit.ly/1c8i5Es
The soluble form of collagen & Beta-carotene...
Premier Dead Sea:
Collagen, Beta Carotene, and Seaweed Mask
=================================
http://bit.ly/1c8i5Es
The soluble form of collagen & Beta-carotene is the basis for the continual renewal of fibrils. These are dense chains of amino acids, which lie in the tissues forming a network of supporting elements to which the skin woes kits of elasticity. Moreover it increases the capacity of the skin to absorb moisture so tired skin becomes revitalized This rich concentrate, a vital source of energy, oxygen and Dead Sea Minerals targets particularly dehydrated areas and fine lines to help prevent premature aging. The skins wrinkles and fine lines become less apparent and the skins protection against the formation of new wrinkles is reinforced.
wn.com/Premier Dead Sea Collagen, Beta Carotene,And Seaweed Mask
Premier Dead Sea:
Collagen, Beta Carotene, and Seaweed Mask
=================================
http://bit.ly/1c8i5Es
The soluble form of collagen & Beta-carotene is the basis for the continual renewal of fibrils. These are dense chains of amino acids, which lie in the tissues forming a network of supporting elements to which the skin woes kits of elasticity. Moreover it increases the capacity of the skin to absorb moisture so tired skin becomes revitalized This rich concentrate, a vital source of energy, oxygen and Dead Sea Minerals targets particularly dehydrated areas and fine lines to help prevent premature aging. The skins wrinkles and fine lines become less apparent and the skins protection against the formation of new wrinkles is reinforced.
- published: 06 Aug 2013
- views: 2195
What Is The Definition Of ADAMTS2 Medical Dictionary Free Online
what is the definition of ADAMTS2: A gene that encodes a metalloproteinase enzyme. This enzyme is responsible for processing type I, type II, and type V procoll...
what is the definition of ADAMTS2: A gene that encodes a metalloproteinase enzyme. This enzyme is responsible for processing type I, type II, and type V procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off of one end of the procollagen. The clipping step is necessary for proper assembly and function of collagen molecules.
Mutations in the ADAMTS2 gene have been identified in patients with Ehlers-Danlos syndrome, dermatosparaxis type. These mutations greatly reduce the production of the enzyme made by ADAMTS2. Procollagen cannot be processed correctly without this enzyme. As a result, type I collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope. Cross-links, or chemical interactions, between collagen fibrils are also affected. These defects weaken connective tissue, particularly in the skin, which causes the symptoms of the disorder.
The ADAMTS2 gene is located on the long (q) arm of chromosome 5 at the end (terminal) of the arm. ADAMTS2 stands for A disintegrin-like and metalloprotease with thrombospondin type 1 motif, 2.
medical terminology, medical dictionary, medical dictionary free download, medical terminology made easy, medical terminology song
wn.com/What Is The Definition Of Adamts2 Medical Dictionary Free Online
what is the definition of ADAMTS2: A gene that encodes a metalloproteinase enzyme. This enzyme is responsible for processing type I, type II, and type V procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off of one end of the procollagen. The clipping step is necessary for proper assembly and function of collagen molecules.
Mutations in the ADAMTS2 gene have been identified in patients with Ehlers-Danlos syndrome, dermatosparaxis type. These mutations greatly reduce the production of the enzyme made by ADAMTS2. Procollagen cannot be processed correctly without this enzyme. As a result, type I collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope. Cross-links, or chemical interactions, between collagen fibrils are also affected. These defects weaken connective tissue, particularly in the skin, which causes the symptoms of the disorder.
The ADAMTS2 gene is located on the long (q) arm of chromosome 5 at the end (terminal) of the arm. ADAMTS2 stands for A disintegrin-like and metalloprotease with thrombospondin type 1 motif, 2.
medical terminology, medical dictionary, medical dictionary free download, medical terminology made easy, medical terminology song
- published: 09 Sep 2014
- views: 25
Anisotropic Collagen Fibrillogenesis within an accordion-like honeycomb scaffold
Visualization of the collagen fibril organization within the a pore of an accordion-like honeycomb scaffold, using fluorescence microscopy. (Jean and Engelmayr,...
Visualization of the collagen fibril organization within the a pore of an accordion-like honeycomb scaffold, using fluorescence microscopy. (Jean and Engelmayr, Adv. Healh. Mater. 2012.)
wn.com/Anisotropic Collagen Fibrillogenesis Within An Accordion Like Honeycomb Scaffold
Visualization of the collagen fibril organization within the a pore of an accordion-like honeycomb scaffold, using fluorescence microscopy. (Jean and Engelmayr, Adv. Healh. Mater. 2012.)
- published: 06 Mar 2014
- views: 98