描述：
Activin and Inhibin are members of the TGF-β superfamily of cytokines and are involved in
a wide range of biological processes including tissue morphogenesis and repair, fibrosis,
inflammation, neural development, hematopoiesis, reproductive system function, and
carcinogenesis. Activin and Inhibin are produced as precursor proteins. Their amino terminal
propeptides are proteolytically cleaved and facilitate formation of disulfide-linked dimers of
the bioactive proteins. Activins are nonglycosylated homodimers or heterodimers of various
β subunits (βA, βB, βC, and βE in mammals), while Inhibins are heterodimers of a unique α
subunit and one of the β subunits. Activin A is a widely expressed homodimer of two βA chains.
The βA subunit can also heterodimerize with a βB or βC subunit to form Activin AB and Activin
AC, respectively. The 14 kDa mature human βA chain shares 100% amino acid sequence
identity with bovine, feline, mouse, porcine, and rat βA. Activin A exerts its biological activities
by binding to the type 2 serine/threonine kinase Activin RIIA which then noncovalently
associates with the type 1 serine/threonine kinase Activin RIB/ALK-4. Signaling through this
receptor complex leads to Smad activation and regulation of activin-responsive gene
transcription. The bioactivity of Activin A is regulated by a variety of mechanisms. BAMBI,
Betaglycan, and Cripto are cell-associated molecules that function as decoy receptors or limit
the ability of Activin A to induce receptor complex assembly. The intracellular formation of
Activin A can be prevented by the incorporation of the βA subunit into Activin AC or Inhibin A .
And the bioavailability of Activin A is restricted by its incorporation into inactive complexes
with α2-Macroglobulin, Follistatin, and FLRG.
原厂资料：
Activin and Inhibin are members of the TGF-β superfamily of cytokines and are involved in
a wide range of biological processes including tissue morphogenesis and repair, fibrosis,
inflammation, neural development, hematopoiesis, reproductive system function, and
carcinogenesis. Activin and Inhibin are produced as precursor proteins. Their amino terminal
propeptides are proteolytically cleaved and facilitate formation of disulfide-linked dimers of
the bioactive proteins. Activins are nonglycosylated homodimers or heterodimers of various
β subunits (βA, βB, βC, and βE in mammals), while Inhibins are heterodimers of a unique α
subunit and one of the β subunits. Activin A is a widely expressed homodimer of two βA chains.
The βA subunit can also heterodimerize with a βB or βC subunit to form Activin AB and Activin
AC, respectively. The 14 kDa mature human βA chain shares 100% amino acid sequence
identity with bovine, feline, mouse, porcine, and rat βA. Activin A exerts its biological activities
by binding to the type 2 serine/threonine kinase Activin RIIA which then noncovalently
associates with the type 1 serine/threonine kinase Activin RIB/ALK-4. Signaling through this
receptor complex leads to Smad activation and regulation of activin-responsive gene
transcription. The bioactivity of Activin A is regulated by a variety of mechanisms. BAMBI,
Betaglycan, and Cripto are cell-associated molecules that function as decoy receptors or limit
the ability of Activin A to induce receptor complex assembly. The intracellular formation of
Activin A can be prevented by the incorporation of the βA subunit into Activin AC or Inhibin A .
And the bioavailability of Activin A is restricted by its incorporation into inactive complexes
with α2-Macroglobulin, Follistatin, and FLRG.
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