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Activin



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

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.

Additional recommended knowledge

Contents

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:

  • Activin is strongly expressed in wounded skin, and overexpression of activin in epidermis of transgenic mice improves wound healing and enhances scar formation. Its action in wound repair and skin morphogenesis is through stimulation of keratinocytes and stromal cells in a dose-dependent manner.[3]
  • Activin also regulates the morphogenesis of branching organs such as the prostate, lung, and especially kidney. Activin A increased the expression level of type I collagen suggesting that activtin A acts as a potent activator of fibroblasts.

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.
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Activin". A list of authors is available in Wikipedia.
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