Sandbox Reserved 1092: Difference between revisions
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This protein was firstly named '''Growth/Differentiation Factor 8 (GDF8)''' because it belongs to the group of growth factors. Growth factors constitute a group of proteins that regulate the number of cells, increasing or decreasing their multiplication according to the needs. Then the nomenclature changed and, nowadays, we refer to myostatine as '''MSTN'''. Progressively, the myostatin has been affiliated to the '''TGF-beta family''' (transforming growth factor beta). | This protein was firstly named '''Growth/Differentiation Factor 8 (GDF8)''' because it belongs to the group of growth factors. Growth factors constitute a group of proteins that regulate the number of cells, increasing or decreasing their multiplication according to the needs. Then the nomenclature changed and, nowadays, we refer to myostatine as '''MSTN'''. Progressively, the myostatin has been affiliated to the '''TGF-beta family''' (transforming growth factor beta). | ||
= Function = | = Function = <ref name="patho"/> | ||
Myostatin is a strong '''endogenous, negative regulator of muscle growth''' determining both '''muscle fiber number and size.''' The number of fibers is set during the development of animals while their size adapts during the entire lifetime, depending on '''activity, nutrition and aging.''' Myostatin acts on this by providing regulation on the growth of muscles. It has been found first in mice which, because they had their gene encoding for myostatin '''knocked-out''', developed overgrowth of muscles, due to '''hyperplasia and hypertrophy''', which effects are persistent throughout the life of animals. | Myostatin is a strong '''endogenous, negative regulator of muscle growth''' determining both '''muscle fiber number and size.''' The number of fibers is set during the development of animals while their size adapts during the entire lifetime, depending on '''activity, nutrition and aging.''' Myostatin acts on this by providing regulation on the growth of muscles. It has been found first in mice which, because they had their gene encoding for myostatin '''knocked-out''', developed overgrowth of muscles, due to '''hyperplasia and hypertrophy''', which effects are persistent throughout the life of animals. | ||
Therefore, myostatin appears to act at the level of fiber number during '''embryogenesis''' and its growth in '''adult life.''' | Therefore, myostatin appears to act at the level of fiber number during '''embryogenesis''' and its growth in '''adult life.''' | ||
==Myostatin processing and signal transduction== | ==Myostatin processing and signal transduction== <ref name="patho"/> | ||
The mechanism of myostatin action is similar to those of the members of '''TGF-beta family.''' The mature peptide binds to one of the two '''activin type II receptors''' which recruits phosphorylates and activates the activin type I receptor, propagating signals along the '''Smad''' pathway. (Smad are receptor-associated proteins) | The mechanism of myostatin action is similar to those of the members of '''TGF-beta family.''' The mature peptide binds to one of the two '''activin type II receptors''' which recruits phosphorylates and activates the activin type I receptor, propagating signals along the '''Smad''' pathway. (Smad are receptor-associated proteins) | ||
'''Phosphorylated Smad2 and 3''' form heterodimeric complex with '''Smad4'''(common mediator) and they activate the functions of the smad as '''mediators''' of signalling for myostatin : translocating into the '''nucleus''' and activating the transcription of the target genes (through interaction with DNA and other nuclear factors). | '''Phosphorylated Smad2 and 3''' form heterodimeric complex with '''Smad4'''(common mediator) and they activate the functions of the smad as '''mediators''' of signalling for myostatin : translocating into the '''nucleus''' and activating the transcription of the target genes (through interaction with DNA and other nuclear factors). | ||
==Inhibition of myostatin’s function== | ==Inhibition of myostatin’s function== <ref name="patho"/> | ||
The mechanism of activation of myostatin remains to be fully determined but the function of myostatin appears to be dependent of a network of protein interactions. | The mechanism of activation of myostatin remains to be fully determined but the function of myostatin appears to be dependent of a network of protein interactions. | ||
Indeed, several proteins have been identified as inhibitory binding proteins of myostatin : '''follistatin, hSGT, Titin cap, decorin''' were defined in muscles and '''FLRG and GASP''' (myostatin propeptide, follistatin related proteins) have been found to create a complex with myostatin in serum. All of these proteins '''negatively regulate myostatin''' activity (inhibiting its activation, secretion, or reception binding). | Indeed, several proteins have been identified as inhibitory binding proteins of myostatin : '''follistatin, hSGT, Titin cap, decorin''' were defined in muscles and '''FLRG and GASP''' (myostatin propeptide, follistatin related proteins) have been found to create a complex with myostatin in serum. All of these proteins '''negatively regulate myostatin''' activity (inhibiting its activation, secretion, or reception binding). | ||
