描述：
Growth Differentiation Factor 8 (GDF-8), also known as Myostatin, is a secreted TGF-β
superfamily protein that is expressed specifically in developing and adult skeletal muscle.
It controls myoblast proliferation and is a potent negative regulator of skeletal muscle mass.
Mouse GDF-8 is synthesized as a 376 amino acid (aa) preproprotein that consists of a 24 aa
signal peptide, a 243 aa propeptide, and a 109 aa mature protein.Within the propeptide,
mouse GDF-8 shares 96% and 99% aa sequence identity with human and rat GDF-8, respectively. GDF8 is secreted as a preproprotein that is cleaved by BMP1 family proteases to separate the 35-40 kDa propeptide from the 12 kDa
bioactive mature protein .This results in a latent complex containing a disulfidelinked dimer of the mature protein and two noncovalentlyassociated molecules
of the propeptide.The GDF-8 propeptide functions as an inhibitor of mature GDF-8,
and GDF-8 activity can also be inhibited through association with Follistatin, FLRG, Decorin, or
GASP1. The uncleaved GDF8 proprotein binds Latent TGF-β bp3 which can sequester it in the
extracellular matrix and prevent the proteolytic cleavage of the propeptide. GDF-8 binds to the
type II Activin receptor Activin RIIB which then associates with the type I receptors Activin
RIB/ALK-4 or TGFbeta RI/ALK5 to induce signaling. GDF-8 additionally inhibits adipogenic
differentiation of mesenchymal stem cells and preadipocytes .Genetic deletion of GDF-8 or in
vivo administration of the GDF-8 propeptide induces muscle hypertrophy as well as enhanced
glucose utilization and insulin sensitivity and a reduction in overall fat mass.
原厂资料：
Growth Differentiation Factor 8 (GDF-8), also known as Myostatin, is a secreted TGF-β
superfamily protein that is expressed specifically in developing and adult skeletal muscle.
It controls myoblast proliferation and is a potent negative regulator of skeletal muscle mass.
Mouse GDF-8 is synthesized as a 376 amino acid (aa) preproprotein that consists of a 24 aa
signal peptide, a 243 aa propeptide, and a 109 aa mature protein.Within the propeptide,
mouse GDF-8 shares 96% and 99% aa sequence identity with human and rat GDF-8, respectively. GDF8 is secreted as a preproprotein that is cleaved by BMP1 family proteases to separate the 35-40 kDa propeptide from the 12 kDa
bioactive mature protein .This results in a latent complex containing a disulfidelinked dimer of the mature protein and two noncovalentlyassociated molecules
of the propeptide.The GDF-8 propeptide functions as an inhibitor of mature GDF-8,
and GDF-8 activity can also be inhibited through association with Follistatin, FLRG, Decorin, or
GASP1. The uncleaved GDF8 proprotein binds Latent TGF-β bp3 which can sequester it in the
extracellular matrix and prevent the proteolytic cleavage of the propeptide. GDF-8 binds to the
type II Activin receptor Activin RIIB which then associates with the type I receptors Activin
RIB/ALK-4 or TGFbeta RI/ALK5 to induce signaling. GDF-8 additionally inhibits adipogenic
differentiation of mesenchymal stem cells and preadipocytes .Genetic deletion of GDF-8 or in
vivo administration of the GDF-8 propeptide induces muscle hypertrophy as well as enhanced
glucose utilization and insulin sensitivity and a reduction in overall fat mass.
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