OhNoYo
New Member
Any recent novel findings lately or at least a discussion where a timeline has been proposed to declare that a myostatin inhibitor will be available in the near future?
MESO-Rx
Anabolic Steroids
Where are We NOW at with Myostatin Inhibitors?
- Thread starter OhNoYo
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Sworder
Member
Not much progress in terms of what will be available within 5 years, I want one..
OhNoYo
New Member
Do you know much in terms of any clinical trial(s) status?
Wyeth dropped experimentation with MYO-029 awhile back, but I never found out why: [ame=http://en.wikipedia.org/wiki/Stamulumab]Stamulumab - Wikipedia, the free encyclopedia[/ame]
They have done studies on a potent myostatin inhibitor (at least in mice) which has resulted in significant increases in muscle mass: Regulation of muscle growth by multiple ligands signaling through activin type II receptors
However, I think the problem with that myostatin inhibitor is it doesn't just affect myostatin, but other mechanisms in the body as well.
Reinheart
New Member
Creatine monohydrate is an effective Myostatin inhibitor. It's also safe, cheap and readily available. Rumor has it that very high class athletes have access to Myostatin inhibitors but the cost is like 3-4k per mg,
Where are we on this - well there has been some supposed blockers released, but I doubt that the products will be any good - the reason being two things:
1. It would have to be manufactored by some unknown supplements company - reason being - that sales of creatine and other "boosters" would suffer tremendously from such products, and as this is a multimillion dollar industry, I doubt they are willing to give up that income for a product, that likely wont sell as well, and were the full extend of sideeffects are yet unknown.
2. To prevent the above from happenings - the price would need to be set rather high and thus be too much for most to be able to pay for it.
The latest news I have found is thas Resaerch have found some sideeffect to the product - “Those interested in Myostatin inhibitors need to be aware of the fact that by doing these things to muscles, they may be having negative effects on tendons,” says John A. Faulkner, Ph.D" - I found this at
So I am sticking with creatine
1. It would have to be manufactored by some unknown supplements company - reason being - that sales of creatine and other "boosters" would suffer tremendously from such products, and as this is a multimillion dollar industry, I doubt they are willing to give up that income for a product, that likely wont sell as well, and were the full extend of sideeffects are yet unknown.
2. To prevent the above from happenings - the price would need to be set rather high and thus be too much for most to be able to pay for it.
The latest news I have found is thas Resaerch have found some sideeffect to the product - “Those interested in Myostatin inhibitors need to be aware of the fact that by doing these things to muscles, they may be having negative effects on tendons,” says John A. Faulkner, Ph.D" - I found this at
Code:
http://myostatininhibitors.orgSworder
Member
May be of interest 
[ame=http://en.wikipedia.org/wiki/Follistatin]Follistatin - Wikipedia, the free encyclopedia[/ame]
Follistatin induces muscle hyp... [Am J Physiol Endocrinol Metab. 2009] - PubMed - NCBI
Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin.
Gilson H, Schakman O, Kalista S, Lause P, Tsuchida K, Thissen JP.
Source
Unité de Diabétologie et Nutrition, Université Catholique de Louvain, 54 Ave. Hippocrate, B-1200, Brussels, Belgium.
Abstract
Follistatin (FS) inhibits several members of the TGF-beta superfamily, including myostatin (Mstn), a negative regulator of muscle growth. Mstn inhibition by FS represents a potential therapeutic approach of muscle atrophy. The aim of our study was to investigate the mechanisms of the FS-induced muscle hypertrophy. To test the role of satellite cells in the FS effect, we used irradiation to destroy their proliferative capacity. FS overexpression increased the muscle weight by about 37% in control animals, but the increase reached only 20% in irradiated muscle, supporting the role of cell proliferation in the FS-induced hypertrophy. Surprisingly, the muscle hypertrophy caused by FS reached the same magnitude in Mstn-KO as in WT mice, suggesting that Mstn might not be the only ligand of FS involved in the regulation of muscle mass. To assess the role of activin (Act), another FS ligand, in the FS-induced hypertrophy, we electroporated FSI-I, a FS mutant that does not bind Act with high affinity. Whereas FS electroporation increased muscle weight by 32%, the muscle weight gain induced by FSI-I reached only 14%. Furthermore, in Mstn-KO mice, FSI-I overexpression failed to induce hypertrophy, in contrast to FS. Therefore, these results suggest that Act inhibition may contribute to FS-induced hypertrophy. Finally, the role of Act as a regulator of muscle mass was supported by the observation that ActA overexpression induced muscle weight loss (-15%). In conclusion, our results show that satellite cell proliferation and both Mstn and Act inhibition are involved in the FS-induced muscle hypertrophy.
PMID:
19435857
[PubMed - indexed for MEDLINE]
Free full text
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LinkOut - more resources
[ame=http://en.wikipedia.org/wiki/Follistatin]Follistatin - Wikipedia, the free encyclopedia[/ame]
Follistatin induces muscle hyp... [Am J Physiol Endocrinol Metab. 2009] - PubMed - NCBI
Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin.
Gilson H, Schakman O, Kalista S, Lause P, Tsuchida K, Thissen JP.
Source
Unité de Diabétologie et Nutrition, Université Catholique de Louvain, 54 Ave. Hippocrate, B-1200, Brussels, Belgium.
Abstract
Follistatin (FS) inhibits several members of the TGF-beta superfamily, including myostatin (Mstn), a negative regulator of muscle growth. Mstn inhibition by FS represents a potential therapeutic approach of muscle atrophy. The aim of our study was to investigate the mechanisms of the FS-induced muscle hypertrophy. To test the role of satellite cells in the FS effect, we used irradiation to destroy their proliferative capacity. FS overexpression increased the muscle weight by about 37% in control animals, but the increase reached only 20% in irradiated muscle, supporting the role of cell proliferation in the FS-induced hypertrophy. Surprisingly, the muscle hypertrophy caused by FS reached the same magnitude in Mstn-KO as in WT mice, suggesting that Mstn might not be the only ligand of FS involved in the regulation of muscle mass. To assess the role of activin (Act), another FS ligand, in the FS-induced hypertrophy, we electroporated FSI-I, a FS mutant that does not bind Act with high affinity. Whereas FS electroporation increased muscle weight by 32%, the muscle weight gain induced by FSI-I reached only 14%. Furthermore, in Mstn-KO mice, FSI-I overexpression failed to induce hypertrophy, in contrast to FS. Therefore, these results suggest that Act inhibition may contribute to FS-induced hypertrophy. Finally, the role of Act as a regulator of muscle mass was supported by the observation that ActA overexpression induced muscle weight loss (-15%). In conclusion, our results show that satellite cell proliferation and both Mstn and Act inhibition are involved in the FS-induced muscle hypertrophy.
PMID:
19435857
[PubMed - indexed for MEDLINE]
Free full text
Publication Types, MeSH Terms, Substances
LinkOut - more resources
Sworder
Member
ScienceDirect.com - Biochemical and Biophysical Research Communications - Acute inhibition of myostatin-family proteins preserves skeletal muscle in mouse models of cancer cachexia
Acute inhibition of myostatin-family proteins preserves skeletal muscle in mouse models of cancer cachexia
Abstract:
Cachexia, progressive loss of fat and muscle mass despite adequate nutrition, is a devastating complication of cancer associated with poor quality of life and increased mortality. Myostatin is a potent tonic muscle growth inhibitor. We tested how myostatin inhibition might influence cancer cachexia using genetic and pharmacological approaches. First, hypermuscular myostatin null mice were injected with Lewis lung carcinoma or B16F10 melanoma cells. Myostatin null mice were more sensitive to tumor-induced cachexia, losing more absolute mass and proportionately more muscle mass than wild-type mice. Because myostatin null mice lack expression from development, however, we also sought to manipulate myostatin acutely. The histone deacetylase inhibitor Trichostatin A has been shown to increase muscle mass in normal and dystrophic mice by inducing the myostatin inhibitor, follistatin. Although Trichostatin A administration induced muscle growth in normal mice, it failed to preserve muscle in colon-26 cancer cachexia. Finally we sought to inhibit myostatin and related ligands by administration of the Activin receptor extracellular domain/Fc fusion protein, ACVR2B-Fc. Systemic administration of ACVR2B-Fc potently inhibited muscle wasting and protected adipose stores in both colon-26 and Lewis lung carcinoma cachexia, without affecting tumor growth. Enhanced cachexia in myostatin knockouts indicates that host-derived myostatin is not the sole mediator of muscle wasting in cancer. More importantly, skeletal muscle preservation with ACVR2B-Fc establishes that targeting myostatin-family ligands using ACVR2B-Fc or related molecules is an important and potent therapeutic avenue in cancer cachexia.
Acute inhibition of myostatin-family proteins preserves skeletal muscle in mouse models of cancer cachexia
Abstract:
Cachexia, progressive loss of fat and muscle mass despite adequate nutrition, is a devastating complication of cancer associated with poor quality of life and increased mortality. Myostatin is a potent tonic muscle growth inhibitor. We tested how myostatin inhibition might influence cancer cachexia using genetic and pharmacological approaches. First, hypermuscular myostatin null mice were injected with Lewis lung carcinoma or B16F10 melanoma cells. Myostatin null mice were more sensitive to tumor-induced cachexia, losing more absolute mass and proportionately more muscle mass than wild-type mice. Because myostatin null mice lack expression from development, however, we also sought to manipulate myostatin acutely. The histone deacetylase inhibitor Trichostatin A has been shown to increase muscle mass in normal and dystrophic mice by inducing the myostatin inhibitor, follistatin. Although Trichostatin A administration induced muscle growth in normal mice, it failed to preserve muscle in colon-26 cancer cachexia. Finally we sought to inhibit myostatin and related ligands by administration of the Activin receptor extracellular domain/Fc fusion protein, ACVR2B-Fc. Systemic administration of ACVR2B-Fc potently inhibited muscle wasting and protected adipose stores in both colon-26 and Lewis lung carcinoma cachexia, without affecting tumor growth. Enhanced cachexia in myostatin knockouts indicates that host-derived myostatin is not the sole mediator of muscle wasting in cancer. More importantly, skeletal muscle preservation with ACVR2B-Fc establishes that targeting myostatin-family ligands using ACVR2B-Fc or related molecules is an important and potent therapeutic avenue in cancer cachexia.
Sworder
Member
Myostatin is a skeletal muscle targe... [J Clin Endocrinol Metab. 2003] - PubMed - NCBI
Myostatin is a skeletal muscle target of growth hormone anabolic action.
Abstract
Myostatin is a cytokine that has recently been shown to selectively and potently inhibit myogenesis. To investigate the mechanisms of anabolic actions of GH on skeletal muscle growth, we examined the in vitro and in vivo effects of GH on myostatin regulation. Twelve GH-deficient hypopituitary adult subjects were treated with recombinant GH (5 micro g/kg.d) in a double-blind, placebo-controlled fashion. Body composition and physical function were assessed and skeletal muscle biopsies from the vastus lateralis performed at 6-monthly intervals during 18 months of treatment. Myostatin mRNA expression was significantly inhibited to 31 +/- 9% (P < 0.001) of control by GH but not by placebo administration (79 +/- 11%) as determined by quantitative real-time PCR normalized for the housekeeping glyceraldehyde-3-phosphate dehydrogenase gene. The inhibitory effect of GH on myostatin was sustained after 12 and 18 months of GH treatment. These effects were associated with increases in lean body mass and translated into enhanced aerobic performance as determined by maximal oxygen uptake and ventilation threshold. Parallel in vitro studies of skeletal muscle cells demonstrated significant reduction of myostatin expression by myotubes in response to GH, compared with vehicle treatment. Conversely, GH receptor antagonism resulted in up-regulation of myostatin in myoblasts. Given the potent catabolic actions of myostatin, our data suggest that myostatin represents a potential key target for GH-induced anabolism.
Myostatin is a skeletal muscle target of growth hormone anabolic action.
Abstract
Myostatin is a cytokine that has recently been shown to selectively and potently inhibit myogenesis. To investigate the mechanisms of anabolic actions of GH on skeletal muscle growth, we examined the in vitro and in vivo effects of GH on myostatin regulation. Twelve GH-deficient hypopituitary adult subjects were treated with recombinant GH (5 micro g/kg.d) in a double-blind, placebo-controlled fashion. Body composition and physical function were assessed and skeletal muscle biopsies from the vastus lateralis performed at 6-monthly intervals during 18 months of treatment. Myostatin mRNA expression was significantly inhibited to 31 +/- 9% (P < 0.001) of control by GH but not by placebo administration (79 +/- 11%) as determined by quantitative real-time PCR normalized for the housekeeping glyceraldehyde-3-phosphate dehydrogenase gene. The inhibitory effect of GH on myostatin was sustained after 12 and 18 months of GH treatment. These effects were associated with increases in lean body mass and translated into enhanced aerobic performance as determined by maximal oxygen uptake and ventilation threshold. Parallel in vitro studies of skeletal muscle cells demonstrated significant reduction of myostatin expression by myotubes in response to GH, compared with vehicle treatment. Conversely, GH receptor antagonism resulted in up-regulation of myostatin in myoblasts. Given the potent catabolic actions of myostatin, our data suggest that myostatin represents a potential key target for GH-induced anabolism.
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