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- Thread starter Zuperman
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Zuperman
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Copied from the site for those who r to lazy to click.........
A specific gene has been found that limits the size of skeletal muscles. This size effect appears to be exclusively from skeletal muscle. All other cells are unaffected. The gene produces a protein called myostatin. This protein is secreted in the part of the embryo that controls skeletal muscle. It is also found in the muscles of adult mammals. These act like hormones as there are specific receptors for them on the cell wall outer membranes.
Click here to learn more about myostatin
Over the past 30 years, the farmers in Belgium have bred a strain of cattle - The mighty Belgium Blue - that gives 20% more meat per animal on roughly the same food intake as ordinary animals. Indeed, the cattle develop such bulging muscles that in extreme cases, they have to be delivered by cesarean section. This "double muscling trait" had been reported as early as 1807.
Genetic Mutation
In the September issue of Nature Genetics, a European research team reports that double muscling is caused by a mutation in the bovine version of the recently discovered gene that makes the protein called myostatin. In the U.S., two other groups, one from the U.S. Department of Agriculture, and the other from John Hopkins University, reported in September issue of Genome Research and in the Proceedings of the National Academy of Sciences, that the myostatin gene is mutated in Belgium Blues and have linked mutations in the gene to double muscling in a second breed of cattle, the Piedmontese, as well.
How does Myostatin work?
Discovered in mice just four months ago, myostatin normally serves to limit skeletal muscle growth. Apparently, the genetic mutations block its activity in limiting muscle growth. The animals muscles grow larger-but without harming meat quality. The muscles of animals with the myostatin genetic mutations have been discovered to have larger numbers of normal-size fibers. Nevertheless, the meat of the cattle is "so tender, even round steaks fall apart on the grill". It is also lower in fat than that from ordinary breeds.
Lee-Benner Institute Research
Here at the Lee-Benner Institute, we have been working with a group of protein chemists who are developing peptide analogues (short chains of amino acids). These analogues, combined with vitamin co-factors, function as enzyme inhibitors that interfere with the growth limiting action of the myostatin protein. These analogues might be useful in treating muscle-wasting diseases. In mice, the effects of inactivating the gene has increased muscle-cell number by 86%. Most of the muscle growth in adult humans, for example, whether from weight-training or steroids, is caused by hypertrophy (increasing the size of the muscle cell), not hyperplasia (increasing the number of muscle cells).
Peptide Analogues and the brain
Another aspect of these peptide analogues is that they seem to impart many of their actions in the brain. When they are injected into frail, elderly adult humans, there appears to be an increase in drive, energy, motivation, and overall improvement in complex mental functions such as memory, concentration, comprehension, calculation. Even balance and coordination are improved. We are currently studying the effects on strength and stamina in humans. Keep watching this newsletter for future updates on these and other exciting developments in Anti-Aging research.
A specific gene has been found that limits the size of skeletal muscles. This size effect appears to be exclusively from skeletal muscle. All other cells are unaffected. The gene produces a protein called myostatin. This protein is secreted in the part of the embryo that controls skeletal muscle. It is also found in the muscles of adult mammals. These act like hormones as there are specific receptors for them on the cell wall outer membranes.
Click here to learn more about myostatin
Over the past 30 years, the farmers in Belgium have bred a strain of cattle - The mighty Belgium Blue - that gives 20% more meat per animal on roughly the same food intake as ordinary animals. Indeed, the cattle develop such bulging muscles that in extreme cases, they have to be delivered by cesarean section. This "double muscling trait" had been reported as early as 1807.
Genetic Mutation
In the September issue of Nature Genetics, a European research team reports that double muscling is caused by a mutation in the bovine version of the recently discovered gene that makes the protein called myostatin. In the U.S., two other groups, one from the U.S. Department of Agriculture, and the other from John Hopkins University, reported in September issue of Genome Research and in the Proceedings of the National Academy of Sciences, that the myostatin gene is mutated in Belgium Blues and have linked mutations in the gene to double muscling in a second breed of cattle, the Piedmontese, as well.
How does Myostatin work?
Discovered in mice just four months ago, myostatin normally serves to limit skeletal muscle growth. Apparently, the genetic mutations block its activity in limiting muscle growth. The animals muscles grow larger-but without harming meat quality. The muscles of animals with the myostatin genetic mutations have been discovered to have larger numbers of normal-size fibers. Nevertheless, the meat of the cattle is "so tender, even round steaks fall apart on the grill". It is also lower in fat than that from ordinary breeds.
Lee-Benner Institute Research
Here at the Lee-Benner Institute, we have been working with a group of protein chemists who are developing peptide analogues (short chains of amino acids). These analogues, combined with vitamin co-factors, function as enzyme inhibitors that interfere with the growth limiting action of the myostatin protein. These analogues might be useful in treating muscle-wasting diseases. In mice, the effects of inactivating the gene has increased muscle-cell number by 86%. Most of the muscle growth in adult humans, for example, whether from weight-training or steroids, is caused by hypertrophy (increasing the size of the muscle cell), not hyperplasia (increasing the number of muscle cells).
Peptide Analogues and the brain
Another aspect of these peptide analogues is that they seem to impart many of their actions in the brain. When they are injected into frail, elderly adult humans, there appears to be an increase in drive, energy, motivation, and overall improvement in complex mental functions such as memory, concentration, comprehension, calculation. Even balance and coordination are improved. We are currently studying the effects on strength and stamina in humans. Keep watching this newsletter for future updates on these and other exciting developments in Anti-Aging research.
navigatorrs
New member
great read........very interesting
Zuperman
New member
Myostatin: A growth factor that regulates the size of muscles beginning in early embryonic development and continuing throughout life. Myostatin acts by inhibiting the growth of muscles, It prevents them from growing too large. Myostatin is also known as growth and differentiation factor 8 (GDF-8). It is a protein made up of two identical subunits. Each subunit contains 110 amino acids. The gene encoding myostatin is termed MSTN (or GDF8) and is on chromosome 2 in band 2q32.1.
Myostatin is a member of the transforming growth factor beta (TGF-beta) family. All of the members of this gene family regulate growth and differentiation from early embryogenesis to mature cell types and tissues.
Myostatin was first found to regulate muscle mass in mice from which the gene encoding myostatin had been knocked out (deleted). In these "mighty mice," there is muscle overgrowth due to an increase both in the number of myocytes (muscle cells) and the size (hypertrophy) of the myofibers (muscle fibers). Breeds of cattle with exceptional muscle development -- referred to as "double-muscled" cattle -- have a mutation in the bovine MSTN gene encoding myostatin.
A child born with very large muscles was discovered to have mutation of the MSTN gene encoding myostatin, providing very strong evidence that myostatin is a lead actor in regulating muscle mass in humans. Aside from the increase in the size of his muscles, the child appeared normal at age 4. The child has a loss-of-function mutation in the MSTN gene that inactivates myostatin It may be possible to increase muscle mass and strength by inactivating myostatin in people with muscle wasting due to disease (Schuelke M et al. New Engl J Med 350:2682,2004)
Higher concentrations of myostatin in the body cause the individual to have less developed muscles. The myostatin protein is produced in skeletal muscle cells, circulates in the blood and acts on muscle tissue, apparently by slowing down the development of muscle stem cells . The precise mechanism remains unknown. Myostatin and the associated gene were discovered in 1997 by geneticists McPherron and Se-Jin Lee, who also produced a strain of mutant mice that lack the gene and are about twice as strong as normal mice. The gene has been sequenced in humans, mice, zebrafish and several other animals, showing few differences among species. Lee found in 1997 that the strong /Belgian Blue / and /Piedmontese/ cattle strains have a defective myostatin gene; these strains have been produced through breeding. In 2001, Lee created mice with intact myostatin gene and large muscle mass by inserting mutations that boosted the production of various myostatin blocking substances. In 2004, a German boy was diagnosed with a mutation in both copies of the myostatin-producing gene, making him considerably stronger than his peers. His mother, a former sprinter, has a mutation in one copy of the gene. The idea is to introduce substances that block myostatin. In 2002, researchers at the University of Pennsylvania showed that monoclonal antibody specific to myostatin improves the condition of mice with muscular dystrophy, presumably by blocking myostatin's action. In 2004 , Lee showed that a two-week treatment of normal mice with soluble /activin type IIB receptor /, a molecule that is normally attached to cells and binds to myostatin, leads to a significantly increased muscle mass (up to 60%). It is thought that binding of myostatin to the soluble activin receptor prevents it from interacting with the cell-bound receptors. It remains unclear whether long term treatment of muscular dystropy with myostatin inhibitors is beneficial: the depletion of muscle stem cells could worsen the disease later on. As of 2006, no myostatin inhibiting drugs for humans are on the market, but an antibody genetically engineered to neutralize myostatin is being developed by New Jersey pharmaceutical company Wyeth . The inhibitor is called MYO-029 and is currently undergoing human testing. Some athletes, eager to get their hands on such drugs, turn to the internet, where fake "myostatin blockers" are being sold. Myostatin is a member of the TGF-beta superfamily of proteins. Human Myostatin consists of two identical subunits, each consisting of 110 amino acid residues. Its total molecular weight is 25.0 kDa . It can be produced in genetically engineered E. coli and is available for sale. Johns Hopkins University owns the patents on myostatin.
Myostatin is a member of the transforming growth factor beta (TGF-beta) family. All of the members of this gene family regulate growth and differentiation from early embryogenesis to mature cell types and tissues.
Myostatin was first found to regulate muscle mass in mice from which the gene encoding myostatin had been knocked out (deleted). In these "mighty mice," there is muscle overgrowth due to an increase both in the number of myocytes (muscle cells) and the size (hypertrophy) of the myofibers (muscle fibers). Breeds of cattle with exceptional muscle development -- referred to as "double-muscled" cattle -- have a mutation in the bovine MSTN gene encoding myostatin.
A child born with very large muscles was discovered to have mutation of the MSTN gene encoding myostatin, providing very strong evidence that myostatin is a lead actor in regulating muscle mass in humans. Aside from the increase in the size of his muscles, the child appeared normal at age 4. The child has a loss-of-function mutation in the MSTN gene that inactivates myostatin It may be possible to increase muscle mass and strength by inactivating myostatin in people with muscle wasting due to disease (Schuelke M et al. New Engl J Med 350:2682,2004)
Higher concentrations of myostatin in the body cause the individual to have less developed muscles. The myostatin protein is produced in skeletal muscle cells, circulates in the blood and acts on muscle tissue, apparently by slowing down the development of muscle stem cells . The precise mechanism remains unknown. Myostatin and the associated gene were discovered in 1997 by geneticists McPherron and Se-Jin Lee, who also produced a strain of mutant mice that lack the gene and are about twice as strong as normal mice. The gene has been sequenced in humans, mice, zebrafish and several other animals, showing few differences among species. Lee found in 1997 that the strong /Belgian Blue / and /Piedmontese/ cattle strains have a defective myostatin gene; these strains have been produced through breeding. In 2001, Lee created mice with intact myostatin gene and large muscle mass by inserting mutations that boosted the production of various myostatin blocking substances. In 2004, a German boy was diagnosed with a mutation in both copies of the myostatin-producing gene, making him considerably stronger than his peers. His mother, a former sprinter, has a mutation in one copy of the gene. The idea is to introduce substances that block myostatin. In 2002, researchers at the University of Pennsylvania showed that monoclonal antibody specific to myostatin improves the condition of mice with muscular dystrophy, presumably by blocking myostatin's action. In 2004 , Lee showed that a two-week treatment of normal mice with soluble /activin type IIB receptor /, a molecule that is normally attached to cells and binds to myostatin, leads to a significantly increased muscle mass (up to 60%). It is thought that binding of myostatin to the soluble activin receptor prevents it from interacting with the cell-bound receptors. It remains unclear whether long term treatment of muscular dystropy with myostatin inhibitors is beneficial: the depletion of muscle stem cells could worsen the disease later on. As of 2006, no myostatin inhibiting drugs for humans are on the market, but an antibody genetically engineered to neutralize myostatin is being developed by New Jersey pharmaceutical company Wyeth . The inhibitor is called MYO-029 and is currently undergoing human testing. Some athletes, eager to get their hands on such drugs, turn to the internet, where fake "myostatin blockers" are being sold. Myostatin is a member of the TGF-beta superfamily of proteins. Human Myostatin consists of two identical subunits, each consisting of 110 amino acid residues. Its total molecular weight is 25.0 kDa . It can be produced in genetically engineered E. coli and is available for sale. Johns Hopkins University owns the patents on myostatin.
needtogetaas
New member
very old but not a bad read...some one posted this about 2 years ago guess they found a way to change the dna and make the cow huge.lol
Rickdarula
Member
I can't remember where, but I read some where that Flex Wheeler was subject in a Myostatin test and was found to have a lot less floating around than your average Joe Blow.
There was also some Toddler in Germany that was born Myostatically deficient. It was an extreme case and the little bro looked like he was ready for the Olympia Stage.
Interesting stuff.
There was also some Toddler in Germany that was born Myostatically deficient. It was an extreme case and the little bro looked like he was ready for the Olympia Stage.
Interesting stuff.
