Activin

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The Activin dimer, from 2ARV.pdb
inhibin, beta A (activin A, activin AB alpha polypeptide)
Identifiers
Symbol INHBA
Entrez 3624
HUGO 6066
OMIM 147290
RefSeq NM_002192
UniProt P08476
Other data
Locus Chr. 7 p15-p13
inhibin, beta B (activin B, activin AB beta polypeptide)
Identifiers
Symbol INHBB
Entrez 3625
HUGO 6067
OMIM 147390
RefSeq NM_002193
UniProt P09529
Other data
Locus Chr. 2 cen-q13

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Activin is a peptide that enhances FSH synthesis and secretion and participates in the regulation of the menstrual cycle. It does the opposite as inhibin. Many other functions have been found to be exerted by activin, including their roles in cell proliferation, differentiation, apoptosis[1], metabolism, homeostasis, immune response, wound repair[2], and endocrine function

Like inhibin (and AMH) activin belongs to TGF-β superfamily.

Structure

Activin contains two beta subunit that are identical to the two beta subunits (A or B) of inhibin, allowing for the formation of three forms of activin: A, AB, and B.

They are linked by a single covalent disulfide bond.

Function

Activin is produced in the gonads, pituitary gland, placenta and other organs:

Mechanism

As with other members of the superfamily, activins interact with two types of cell surface transmembrane receptors (Types I and II) which have intrinsic serine/threonine kinase activities in their cytoplasmic domains.

Activin binds to the Type II receptor and initiates a cascade reaction that leads to the recruitment, phosphorylation, and activation of Type I activin receptor. This then interacts with and then phosphorylates Smad2 and Smad3, two of the cytoplasmic Smad proteins.

Smad3 then translocates to the nucleus and interacts with Smad4 through multimerization, resulting in their modulation as transcription factor complexes responsible for the expression of a large variety of genes.

References

  1. Chen YG, Wang Q, Lin SL, Chang CD, Chung J, and Ying SY. Activin Signaling and its Role in Regulation of Cell Proliferation, Apoptosis and Carcinogenesis. Exp Biol Med. 2006; 231: 534-544.
  2. Sulyok S, 20 M, Alzheimer C, Werner S. Activin: an important regulator of wound repair, fibrosis, and neuroprotection. Molecular and Cellular Endocrinology. 2005; 225: 126-132.
  3. Bamberger C, Schärer A, Antsiferova M, Tychsen B, Pankow S, Müller M, Rülicke T, Paus R, and Werner S. Activin Controls Skin Morphogenesis and Wound Repair Predominantly via Stromal Cells and in a Concentration-Dependent Manner via Keratinocytes. American Journal of Pathology. 2005; 167 (3): 733-741.

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Acknowledgement and Attribution Regarding Sources of Content

Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

fr:Activine ja:アクチビン

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