The Myostatin Propeptide and the Follistatin-related Gene Are Inhibitory Binding Proteins of Myostatin in Normal Serum

Hill, Jonathan D.; Davies, Monique V.; Pearson, Adele A.; Wang, Jack H.; Hewick, Rodney M.; Wolfman, Neil M.; Qiu, Yongchang

doi:10.1074/jbc.m206379200

Cited by 411 publications

(384 citation statements)

References 42 publications

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“…A representative Western blot for myostatin is provided and revealed a band at approximately 15 kD, consistent with the secreted form of myostatin (Hill et al, 2002;Zimmers et al, 2002). We found that myostatin protein levels tended to be increased in the serum of COPD group compared with that of the group of healthy controls ( Fig.…”

Section: Myostatin Levels Are Increased In Copd Patientsmentioning

confidence: 69%

Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli

Hayot

Rodriguez

Vernus

et al. 2011

Molecular and Cellular Endocrinology

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Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli, Molecular and Cellular Endocrinology (2010), doi:10.1016/j.mce.2010 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Version postprintComment citer ce document : Hayot, M., Rodriguez, J., Vernus, B., Carnac, G., Jean, E., Allen, D., Goret, L., Obert, P., Candau, R., A c c e p t e d M a n u s c r i p t 2 ABSTRACTMyostatin and hypoxia signalling pathways are able to induce skeletal muscle atrophy, but whether a relationship between these two pathways exists is currently unknown. Here, we tested the hypothesis that a potential mechanism for hypoxia effect on skeletal muscle may be through regulation of myostatin. We reported an induction of myostatin expression in muscles of rats exposed to chronic hypoxia. Interestingly, we also demonstrated increased skeletal muscle myostatin protein expression in skeletal muscle of hypoxemic patients with severe Keywords : hypoxic stimulus, myostatin, skeletal muscle atrophy, COPD, myotubes Version postprintComment citer ce document : Hayot, M., Rodriguez, J., Vernus, B., Carnac, G., Jean, E., Allen, D., Goret, L., Obert, P., Candau, R., Bonnieu, A. (2011). Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli.

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Section: Myostatin Levels Are Increased In Copd Patientsmentioning

confidence: 69%

Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli

Hayot

Rodriguez

Vernus

et al. 2011

Molecular and Cellular Endocrinology

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“…Although such cleavage is sufficient for activating most TGFβ-like proteins (Hogan, 1996), prototypical family members TGFβ 1-3 remain noncovalently bound to their cleaved prodomains in latent complexes (Massague, 1998). More recently it has been demonstrated that GDF8 and 11, which share ~90% sequence identity in their mature regions (Gamer et al, 1999;Ge et al, 2005;Nakashima et al, 1999), are also noncovalently bound to their respective prodomains in latent complexes (Ge et al, 2005;Hill et al, 2002;Lee and McPherron, 2001;Wolfman et al, 2003) (Fig. 5B).…”

Section: Growth and Differentiation Factors 8 And 11 (Gdfs 8 And 11)mentioning

confidence: 99%

“…5B). Secreted by myocytes, GDF8, also known as Myostatin, is an important negative regulator of skeletal muscle growth (Hill et al, 2002;Lee and McPherron, 2001;McPherron et al, 1997), whereas GDF11, secreted by mature neurons, serves a comparable function in inhibiting neurogenesis (Wu et al, 2003). GDF11 also appears to play roles in anterior-posterior patterning of the axial skeleton (McPherron et al, 1999).…”

Section: Growth and Differentiation Factors 8 And 11 (Gdfs 8 And 11)mentioning

confidence: 99%

The bone morphogenetic protein 1/Tolloid-like metalloproteinases

2007

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A decade ago, bone morphogenetic protein 1 (BMP1) was shown to provide the activity necessary for proteolytic removal of the C-propeptides of procollagens I-III: precursors of the major fibrillar collagens. Subsequent studies have shown BMP1 to be the prototype of a small group of extracellular metalloproteinases that play manifold roles in regulating formation of the extracellular matrix (ECM). Soon after initial cloning of BMP1, genetic studies showed the related Drosophila proteinase Tolloid (TLD) to be necessary for formation of the dorsal-ventral axis in early embryogenesis. It is now clear that the BMP1/TLD-like proteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of transforming growth factor β (TGFβ)-like proteins BMP2, BMP4 (vertebrates) and decapentaplegic (arthropods). More recently, it has become apparent that the BMP1/TLD-like proteinases are key activators of a broader subset of the TGFβ superfamily of proteins, with implications that these proteinases may be key in orchestrating formation of ECM with growth factor activation and BMP signaling in morphogenetic processes.

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“…Secreted by the skeletal muscle, myostatin is found in an active unbound (free) form, or bound to its own propeptide, or separate peptides such as follistatin, or follistatin‐related gene (FLRG; Hill et al. 2002; Amthor et al. 2004; Gilson et al.…”

Section: Introductionmentioning

confidence: 99%

Lifelong exercise, but not short-term high-intensity interval training, increases GDF11, a marker of successful aging: a preliminary investigation

et al. 2017

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Lifelong exercise is associated with regulation of skeletal mass and function, reductions in frailty, and successful aging. Yet, the influence of exercise on myostatin and myostatin‐interacting factors is relatively under examined in older males. Therefore, we investigated whether serum total myostatin, free myostatin, follistatin, and growth and differentiation factor 11 (GDF11) were altered following high‐intensity interval training (HIIT) in a group of 13 lifelong sedentary (SED; 64 [6] years) and 11 lifelong exercising (LEX; 62 [6] years) older males. SED follistatin was moderately greater than LEX pre‐HIIT (Cohen's d = 0.66), and was largely greater post‐HIIT (Cohen's d = 1.22). The HIIT‐induced increase in follistatin was large in SED (Cohen's d = 0.82) and absent in LEX (Cohen's d = 0.03). GDF11 was higher in LEX pre‐HIIT (Cohen's d = 0.49) and post‐HIIT (Cohen's d = 0.63) compared to SED. HIIT resulted in no change to GDF11 in LEX or SED (Cohen's d = 0.00–0.03). Peak power output and GDF11 were correlated (r = 0.603), independent of grouping. Differences in GDF11 with lifelong exercise training, paired with the correlation between GDF11 and peak power output, suggested that GDF11 may be a relevant myostatin‐interacting peptide to successful aging in humans, and strategies to maintain this need to be further explored.

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The Myostatin Propeptide and the Follistatin-related Gene Are Inhibitory Binding Proteins of Myostatin in Normal Serum

Cited by 411 publications

References 42 publications

Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli

Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli

The bone morphogenetic protein 1/Tolloid-like metalloproteinases

Lifelong exercise, but not short-term high-intensity interval training, increases GDF11, a marker of successful aging: a preliminary investigation

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