Insulin-like growth factor 1 (somatomedin C)
PDB rendering based on 1bqt.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1B9G, 1BQT, 1GZR, 1GZY, 1GZZ, 1H02, 1H59, 1IMX, 1PMX, 1TGR, 1WQJ, 2DSP, 2DSQ, 2DSR, 2GF1, 3GF1, 3LRI
Identifiers
Symbols	IGF1; IGF-I; IGF1A; IGFI
External IDs	OMIM: 147440 MGI: 96432 HomoloGene: 515 GeneCards: IGF1 Gene
Gene Ontology Molecular function • insulin receptor binding • insulin-like growth factor receptor binding • integrin binding • hormone activity • hormone activity • protein binding • growth factor activity Cellular component • extracellular region • extracellular region • extracellular region • extracellular space • extracellular space • insulin-like growth factor binding protein complex • platelet alpha granule lumen Biological process • skeletal system development • regulation of protein phosphorylation • blood vessel remodeling • platelet degranulation • DNA replication • anti-apoptosis • cellular component movement • signal transduction • Ras protein signal transduction • nervous system development • muscle organ development • blood coagulation • positive regulation of cell proliferation • negative regulation of cell proliferation • glycolate metabolic process • glial cell differentiation • positive regulation of cardiac muscle hypertrophy • positive regulation of phosphatidylinositol 3-kinase cascade • satellite cell maintenance involved in skeletal muscle regeneration • muscle hypertrophy • myotube cell development • positive regulation of smooth muscle cell migration • positive regulation of cerebellar granule cell precursor proliferation • water homeostasis • proteoglycan biosynthetic process • platelet activation • mammary gland development • exocrine pancreas development • regulation of establishment or maintenance of cell polarity • positive regulation of protein import into nucleus, translocation • negative regulation of smooth muscle cell apoptosis • bone mineralization involved in bone maturation • regulation of multicellular organism growth • positive regulation of activated T cell proliferation • positive regulation of tyrosine phosphorylation of Stat5 protein • positive regulation of DNA binding • positive regulation of MAPK cascade • positive regulation of insulin-like growth factor receptor signaling pathway • myoblast differentiation • positive regulation of osteoblast differentiation • positive regulation of glycogen biosynthetic process • positive regulation of DNA replication • positive regulation of DNA replication • positive regulation of glycolysis • positive regulation of mitosis • positive regulation of transcription, DNA-dependent • positive regulation of transcription from RNA polymerase II promoter • positive regulation of glucose import • positive regulation of Ras protein signal transduction • phosphatidylinositol-mediated signaling • positive regulation of fibroblast proliferation • lung alveolus development • positive regulation of smooth muscle cell proliferation • branching morphogenesis of a tube • chondroitin sulfate proteoglycan biosynthetic process • positive regulation of epithelial cell proliferation • positive regulation of peptidyl-tyrosine phosphorylation • regulation of protein metabolic process • myoblast proliferation • positive regulation of protein kinase B signaling cascade • lung vasculature development • lung lobe morphogenesis • Type I pneumocyte differentiation • Type II pneumocyte differentiation • prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis • prostate gland growth • prostate gland epithelium morphogenesis • prostate gland stromal morphogenesis • negative regulation of androgen receptor signaling pathway • negative regulation of ERK1 and ERK2 cascade • positive regulation of calcineurin-NFAT signaling cascade • negative regulation of release of cytochrome c from mitochondria Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3479	16000
Ensembl	ENSG00000017427	ENSMUSG00000020053
UniProt	P05019	P05017
RefSeq (mRNA)	NM_000618.3	NM_001111274.1
RefSeq (protein)	NP_000609.1	NP_001104744.1
Location (UCSC)	Chr 12: 102.79 – 102.87 Mb	Chr 10: 87.32 – 87.4 Mb
PubMed search	[1]	[2]
This box: view talk edit

Insulin-like growth factor 1 (IGF-1), also called somatomedin C, is a protein that in humans is encoded by the IGF1 gene.^[1][2] IGF-1 has also been referred to as a "sulfation factor"^[3] and its effects were termed "nonsuppressible insulin-like activity" (NSILA) in the 1970s.

IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure.^[4]

IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons.

Synthesis and circulation[link]

IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. Production is stimulated by growth hormone (GH) and can be retarded by undernutrition, growth hormone insensitivity, lack of growth hormone receptors, or failures of the downstream signalling pathway post GH receptor including SHP2 and STAT5B. Approximately 98% of IGF-1 is always bound to one of 6 binding proteins (IGF-BP). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio.

In rat experiments the amount of IGF-1 mRNA in the liver was positively associated with dietary casein and negatively associated with a protein-free diet.^[5]

Recently, an efficient plant expression system was developed to produce biologically active recombinant human IGF-I (rhIGF-I) in transgenic rice grains.^[6]

Mechanism of action[link]

Its primary action is mediated by binding to its specific receptor, the Insulin-like growth factor 1 receptor, abbreviated as ""IGF1R"", present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death.

IGF-1 is a primary mediator of the effects of growth hormone (GH). Growth hormone is made in the anterior pituitary gland, is released into the blood stream, and then stimulates the liver to produce IGF-1. IGF-1 then stimulates systemic body growth, and has growth-promoting effects on almost every cell in the body, especially skeletal muscle, cartilage, bone, liver, kidney, nerves, skin, hematopoietic cell, and lungs. In addition to the insulin-like effects, IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNA synthesis.

Deficiency of either growth hormone or IGF-1 therefore results in diminished stature. GH-deficient children are given recombinant GH to increase their size. IGF-1 deficient humans, who are categorized as having Laron syndrome, or Laron's dwarfism, are treated with recombinant IGF-1. In beef cattle, circulating IGF-I concentrations are related to reproductive performance.^[7]

Insulin-like growth factor 1 receptor (IGF-1R) and other tyrosine kinase growth factor receptors signal through multiple pathways. A key pathway is regulated by phosphatidylinositol-3 kinase (PI3K) and its downstream partner, the mammalian target of rapamycin (mTOR). Rapamycins complex with FKBPP12 to inhibit the mTORC1 complex. mTORC2 remains unaffected and responds by upregulating Akt, driving signals through the inhibited mTORC1. Phosphorylation of eukaryotic initiation factor 4e (eif-4E) [4EBP] by mTOR inhibits the capacity of 4EBP to inhibit eif-4E and slow metabolism.

Receptors[link]

IGF-1 binds to at least two cell surface receptors: the IGF-1 receptor (IGF1R), and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. IGF-1 activates the insulin receptor at approximately 0.1x the potency of insulin. Part of this signaling may be via IGF1R/Insulin Receptor heterodimers (the reason for the confusion is that binding studies show that IGF1 binds the insulin receptor 100-fold less well than insulin, yet that does not correlate with the actual potency of IGF1 in vivo at inducing phosphorylation of the insulin receptor, and hypoglycemia)..

IGF-1 is produced throughout life. The highest rates of IGF-1 production occur during the pubertal growth spurt. The lowest levels occur in infancy and old age.

Other IGFBPs are inhibitory. For example, both IGFBP-2 and IGFBP-5 bind IGF-1 at a higher affinity than it binds its receptor. Therefore, increases in serum levels of these two IGFBPs result in a decrease in IGF-1 activity.

Related growth factors[link]

IGF-1 is closely related to a second protein called "IGF-2". IGF-2 also binds the IGF-1 receptor. However, IGF-2 alone binds a receptor called the "IGF-2 receptor" (also called the mannose-6 phosphate receptor). The insulin growth factor-II receptor (IGF2R) lacks signal transduction capacity, and its main role is to act as a sink for IGF-2 and make less IGF-2 available for binding with IGF-1R. As the name "insulin-like growth factor 1" implies, IGF-1 is structurally related to insulin, and is even capable of binding the insulin receptor, albeit at lower affinity than insulin.

A splice variant of IGF-1 sharing an identical mature region, but with a different E domain is known as mechano growth factor (MGF).^[8]

Contribution to aging[link]

It is now widely accepted that signaling through the insulin/IGF-1-like receptor pathway is a significant contributor to the biological aging process in many organisms. This avenue of research first achieved prominence with the work of Cynthia Kenyon, who showed that mutations in the daf-2 gene could double the lifespan of the roundworm C. elegans.^[9] daf-2 encodes the worm's unified insulin/IGF-1-like receptor.

Insulin/IGF-1-like signaling is conserved from worms to humans. In vitro experiments show that mutations that reduce insulin/IGF-1 signaling have been shown to decelerate the degenerative aging process and extend lifespan in a wide range of organisms, including Drosophila melanogaster, mice,^[10] and possibly humans.^{[11][12][13][14]} Reduced IGF-1 signaling is also thought to contribute to the "anti-aging" effects of Calorie restriction.^[15]

Nevertheless the situation in vivo (alive human beings) is definitely different, in fact IGF-I deficiency is associated with neurodegenerative disease.^[16] cardiovascular diseases, heart failure, and shorter life span.^[17][18]

Factors influencing the levels in the circulation[link]

3-d model of IGF-1

Factors that are known to cause variation in the levels of growth hormone (GH) and IGF-1 in the circulation include: genetic make-up, the time of day, age, sex, exercise status, stress levels, nutrition level and body mass index (BMI), disease state, race, estrogen status and xenobiotic intake.^[19] The later inclusion of xenobiotic intake as a factor influencing GH-IGF status highlights the fact that the GH-IGF axis is a potential target for certain endocrine disrupting chemicals - see also endocrine disruptor.

Diseases of deficiency and resistance[link]

IGF-I deficiency is associated with neurodegenerative disease,^[16] cardiovascular diseases, heart failure, and shorter life span.^[17][18]

Rare diseases characterized by inability to make or respond to IGF-1 produce a distinctive type of growth failure. One such disorder, termed Laron dwarfism does not respond at all to growth hormone treatment due to a lack of GH receptors. The FDA has grouped these diseases into a disorder called severe primary IGF deficiency. Patients with severe primary IGFD typically present with normal to high GH levels, height below -3 standard deviations (SD), and IGF-1 levels below -3SD. Severe primary IGFD includes patients with mutations in the GH receptor, post-receptor mutations or IGF mutations, as previously described. As a result, these patients cannot be expected to respond to GH treatment.

The IGF signaling pathway appears to play a crucial role in cancer. Several studies have shown that increased levels of IGF lead to an increased risk of cancer.^[20] Studies done on lung cancer cells show that drugs inhibiting such signaling can be of potential interest in cancer therapy.^[21]

Use as a diagnostic test[link]

IGF-1 levels can be measured in the blood in 10-1000 ng/ml amounts. As levels do not fluctuate greatly throughout the day for an individual person, IGF-1 is used by physicians as a screening test for growth hormone deficiency and excess in acromegaly and gigantism.

Interpretation of IGF-1 levels is complicated by the wide normal ranges, and variations by age, sex, and pubertal stage. Clinically significant conditions and changes may be masked by the wide normal ranges. Sequential management over time is often useful for the management of several types of pituitary disease, undernutrition, and growth problems.

As a therapeutic agent[link]

Mecasermin (brand name Increlex) is a synthetic analog of IGF-1 which is approved for the treatment of growth failure.^[23] IGF-1 has been manufactured recombinantly on a large scale using both yeast and E. coli.

Several companies have evaluated IGF-1 in clinical trials for a variety of additional indications, including type 1 diabetes, type 2 diabetes, amyotrophic lateral sclerosis (ALS aka "Lou Gehrig's Disease"),^[16] severe burn injury and myotonic muscular dystrophy (MMD). Results of clinical trials evaluating the efficacy of IGF-1 in type 1 diabetes and type 2 diabetes showed great promise in reducing hemoglobin A1C levels, as well as daily insulin consumption. However, the sponsor, Genentech, discontinued the program due to an exacerbation of diabetic retinopathy^{[citation needed]} in patients coupled with a shift in corporate focus towards oncology. Cephalon and Chiron conducted two pivotal clinical studies of IGF-1 for ALS, and although one study demonstrated efficacy, the second was equivocal, and the product has never been approved by the FDA.

However, in the last few years, two additional companies Tercica and Insmed compiled enough clinical trial data to seek FDA approval in the United States. In August 2005, the FDA approved Tercica's IGF-1 drug, Increlex, as replacement therapy for severe primary IGF-1 deficiency based on clinical trial data from 71 patients. In December 2005, the FDA also approved Iplex, Insmed's IGF-1/IGFBP-3 complex. The Insmed drug is injected once a day versus the twice-a-day version that Tercica sells.

Insmed was found to infringe on patents licensed by Tercica, which then sought to get a U.S. district court judge to ban sales of Iplex.^[24] To settle patent infringement charges and resolve all litigation between the two companies, Insmed in March 2007 agreed to withdraw Iplex from the U.S. market, leaving Tercica's Increlex as the sole version of IGF-1 available in the United States.^[25]

By delivering Iplex in a complex, patients might get the same efficacy with regard to growth rates but experience fewer side effects with less severe hypoglycemia^{[citation needed]}. This medication might emulate IGF-1's endogenous complexing, as in the human body 97–99% of IGF-1 is bound to one of six IGF binding proteins^{[citation needed]}. IGFBP-3 is the most abundant of these binding proteins, accounting for approximately 80% of IGF-1 binding.

In a clinical trial of an investigational compound MK-677, which raises IGF-1 in patients, did not result in an improvement in patients' Alzheimer's symptoms.^[26] Another clinical demonstrated that Cephalon's IGF-1 does not slow the progression of weakness in ALS patients, but other studies shown strong beneficial effects of IGF-I replacement therapy in ALS patients ^[27], and therefore IGF-I may have the potential to be an effective and safe medicine against ALS ^[28], however other studies had conflicting results.^[29]

IGFBP-3 is a carrier for IGF-1, meaning that IGF-1 binds IGFBP-3, creating a complex whose combined molecular weight and binding affinity allows the growth factor to have an increased half-life in serum. Without binding to IGFBP-3, IGF-1 is cleared rapidly through the kidney, due to its low molecular weight. But when bound to IGFBP-3, IGF-1 evades renal clearance. Also, since IGFBP-3 has a lower affinity for IGF-1 than IGF-1 has for its receptor, IGFR, its binding does not interfere with IGF-1 function. For these reasons, an IGF-1/IGFBP-3 combination approach was approved for human treatment... brought forward by a small company called Insmed. However, Insmed fell afoul patent issues, and was ordered to desist in this approach.

IGF-1 has also been shown to be effective in animal models of stroke when combined with Erythropoietin. Both behavioural and cellular improvements were found.^[30]

Interactions[link]

Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6).

Specific references are provided for interactions with IGFBP3,^{[31][32][33][34][35][36]} IGFBP4,^[37][38] and IGFBP7.^[39][40]

References[link]

Further reading[link]

External links[link]

• Insulin-Like+Growth+Factor+I at the US National Library of Medicine Medical Subject Headings (MeSH)

v t e PDB gallery 1bqt: THREE-DIMENSIONAL STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR-I (IGF-I) DETERMINED BY 1H-NMR AND DISTANCE GEOMETRY, 6 STRUCTURES   1gzr: HUMAN INSULIN-LIKE GROWTH FACTOR; ESRF DATA   1gzy: HUMAN INSULIN-LIKE GROWTH FACTOR; IN-HOUSE DATA   1gzz: HUMAN INSULIN-LIKE GROWTH FACTOR; HAMBURG DATA   1h02: HUMAN INSULIN-LIKE GROWTH FACTOR; SRS DARESBURY DATA   1h59: COMPLEX OF IGFBP-5 WITH IGF-I   1imx: 1.8 Angstrom crystal structure of IGF-1   1pmx: INSULIN-LIKE GROWTH FACTOR-I BOUND TO A PHAGE-DERIVED PEPTIDE   1wqj: Structural Basis for the Regulation of Insulin-Like Growth Factors (IGFs) by IGF Binding Proteins (IGFBPs)   2dsp: Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins   2dsq: Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins   2dsr: Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins   2gf1: SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY   3gf1: SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY   3lri: Solution structure and backbone dynamics of long-[Arg(3)]insulin-like growth factor-I

Competition record
Strongman
Competitor for  United States
IFSA Pan-American Championships
7th	2005
IFSA Strongman World Team Championships
2nd	2005 Team Pan-America
IFSA Holland Grand Prix
2nd	2006
North America's Strongest Man
1st	2003
America's Strongest Man
7th	2003
5th	2004
2nd	2006
World Muscle Power Championships
8th	2004
World Strongman Challenge
3rd	2006
3rd	2007
Strongest Man Alive
3rd	2004
X-TREME Strongman Showdown
4th	2004
World's Strongest Nation
3rd	2005
Ukraine Open
2nd	2006
St Patrick's Day Festival
3rd	2006
3rd	2007
U.S. National Strongman Championships
2nd	2006
All Nations Strength Challenge
4th	2003
3rd	2004

Jon Andersen Reel, normally referred to simply as Jon Andersen (born January 8, 1972) is an American bodybuilder, strongman competitor and professional wrestler. Anderson currently splits his time between working for Pro Wrestling Revolution in California and Consejo Mundial de Lucha Libre (CMLL) in Mexico. He has also worked for the Inoki Genome Federation (IGF) and New Japan Pro Wrestling (NJPW) in Japan. In CMLL he is billed as Jon Strongman, playing off his massive physique.

Professional wrestling career[link]

Jon Anderson trained for his professional wrestling career in the All Pro Wrestling (APW) Bootcamp, making his debut in 2003. From 2003 until 2007 he wrestled only part time to focus on his bodybuilding and strongman career and primarily for APW.^[3] By 2008 he began making regular appearances for California based Pro Wrestling Revolution (PWR) promotion as a "Special feature" due to his enormous size. He also worked tours of Japan, wrestling for Antonio Inoki's Inoki Genome Federation (IGF) in both 2008 and 2009.^[3] He received further training between 2008 and 2009 in Pro Wrestling Revolution by Vaquero Fantasma to prepare him for his work in Mexico.

Jon Strongman[link]

In September, 2009 Jon Anderson signed a contract to wrestle for the Mexico City, Mexico based Consejo Mundial de Lucha Libre (CMLL) promotion and made his debut for the company on October 5, 2009 using the name "Jon Strongman". The storyline used to introduce Jon Strongman to CMLL was that Shocker found him while on tour with Pro Wrestling Revolution as the first member of his faction Los Guapos ("The good looking").^[3] In his debut Strongman teamed with Shocker and Héctor Garza to defeat El Terrible, El Texano, Jr. and Ray Mendoza, Jr..^[3] In the months after his debut Strongman began a storyline feud with Último Guerrero, holder of the CMLL World Heavyweight Championship.^[4] The storyline heated up after Último Guerrera was accidentally knocked unconscious during a match with Jon Strongman and CMLL decided to write it into the storyline between the two.

Strongman appeared at CMLL's Sin Salida event on December 4, 2009 teaming with Místico and Héctor Garza to defeat Guerrero, Atlantis and Mr. Niebla, his first appearance at a major CMLL event.^[5] On March 1, 2010 Strong Man defeated Último Guerrero in the main event of a Puebla, Puebla show, after which último Guerrero offered to defend his championship against Jon Strongman.^[6] A title match has not yet been announced between the two.

On March 14, 2010, Anderson, billed as Strong Man, entered New Japan Pro Wrestling's (NJPW) 2010 New Japan Cup, but was defeated in the first round by Hiroshi Tanahashi.^[1] On July 11 New Japan announced that Strong Man would return to the company in August to take part in the 2010 G1 Climax tournament.^[7] After winning two out of his seven matches in the tournament, Strong Man finished seventh out of the eight wrestlers in his block and didn't advance in the tournament.^[8][9] On October 22, 2010, Inoue and Nagata entered the 2010 G1 Climax Tag League.^[10] Strong Man returned to New Japan in late October 2010 to team with Manabu Nakanishi in the 2010 G1 Climax Tag League. After four wins and a loss, Strong Man and Nakanishi, known collectively as Muscle Orchestra, finished second in their block and advanced to the semifinals, where, on November 7, they were defeated by No Limit (Tetsuya Naitō and Yujiro Takahashi).^[11][12] In recognition of their achievement, Tokyo Sports Grand Prix named Strong Man and Nakanishi the Tag Team of the Year for 2010.^[13] On November 20, Strong Man teamed with Misterioso II to defeat Vaquero Fantasma and Oliver John for the PWR Tag Team Championship, Andersen's first professional wrestling title.^[14] On January 4, 2011, Muscle Orchestra returned to New Japan at Wrestle Kingdom V in Tokyo Dome, where they unsuccessfully challenged Bad Intentions (Giant Bernard and Karl Anderson) for the IWGP Tag Team Championship in a three–way match, which also included Beer Money, Inc. (James Storm and Robert Roode).^[15][16] On February 20 Muscle Orchestra received another shot at Bad Intentions and the IWGP Tag Team Championship, but were unable to win the title.^[17] On January 22, 2011, Andersen made his debut for Lucha Libre USA. In the promotion he performs under the ring name "The Firewall" Jon Rekon, and represents rudo group The Right.^[2][18] On June 18, 2011, Rekon and his stablemate in The Right, Petey Williams, defeated the Latin Liberators (Rocky Romero and Super Nova) to win the vacant Lucha Libre USA Tag Team Championship.^[19] In August, Strong Man returned to New Japan to take part in the 2011 G1 Climax. After losing his first seven matches, Strong Man finished the tournament by picking up big wins over Minoru Suzuki and Hirooki Goto, although still finishing last in his block.^[20][21] Strong Man returned to New Japan on October 22 to take part in the 2011 G1 Climax Tag League, forming the tag team Muscle Pavilion with Tama Tonga as his regular partner Manabu Nakanishi was sidelined with an injury.^[22] After one win and four losses, the team was eliminated from the tournament.^[23] Strong Man started his next tour with New Japan on April 21, 2012.^[24]

In wrestling[link]

• Finishing moves

• Chokeslam^[3]
• Diving neckbreaker^[20][21]
• Gorilla press drop^[3]

• Nicknames

• "The Firewall"^[18]

Championships and accomplishments[link]

• Lucha Libre USA

• Lucha Libre USA Tag Team Championship (1 time) – with Petey Williams^[19]

• Pro Wrestling Illustrated

• PWI ranked him #236 of the top 500 singles wrestlers in the PWI 500 in 2011^[25]

• Pro Wrestling Revolution

• PWR Tag Team Championship (1 time, current) – with Misterioso II^[14]

• Tokyo Sports Grand Prix

• Best Tag Team (2010) – with Manabu Nakanishi^[13]

Strongman career[link]

Jon's strongman career began in 2002, winning the New Mexico's Strongest Man show, and he quickly earned his pro status by winning the Azelea Festival in 2003. Also in 2003, Jon won the North America's Strongest Man competition, his career best win. Jon joined the ranks of the IFSA strongman organization in 2005, placing 7th at the Pan-American Championships, and taking 2nd place at the IFSA World Team Championships along with team mates Travis Ortmayer, Geoff Dolan and Van Hatfield.^[26]

Personal Records[link]

(All lifts done raw with only a weight belt)

• Bench Press: 565x3
• Close-Grip Bench Press: 545
• Push Press: 365x6, 275x20
• Squat: 775x3, 500x25, 405x37
• Deadlift: 700x4, 500x21
• Box Jump: 50"
• Vertical Jump: 35"^[26]

References[link]

Professional wrestling portal