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- W50276713 abstract "Publisher Summary Inhibins and activins were discovered by virtue of their effects on the gonadotropic cells of the anterior pituitary. Inhibin/activin subunits and their mRNAs have been detected in many tissues, including the ovary, testis, placenta, pituitary, central nervous system (CNS), adrenal, and bone marrow. Various tissues differ in the amounts of subunits, in the proportions of particular subunits, and in the processing of the precursors. It is possible that the proportions of subunits produced in a given cell determine the relative amounts of activin and inhibin generated. This chapter discusses the role of α2M in the delivery or clearance of inhibin and activin, similar to that proposed for the binding of transforming growth factor-β (TGFβ) and a number of other growth factors by α2M and other high molecular weight binding protiens. The activin–follistatin complex is, in contrast, biologically inactive and this binding protein plays an important role in limiting exposure of cells to activin. The activin is the only member within the TGF-β superfamily that has a functional antagonist formed by a dimer with a common subunit. The development of gonadal tumors in transgenic mice bearing deletions of the inhibin α subunit and, therefore, unable to make inhibin illustrates the importance of constraining activin to the survival/health of the animal. The initial step in the action of activin is to bind to plasma membrane receptors. Activin binds with high affinity to at least two classes of membrane proteins with molecular masses of ∼50 and ∼70 kDa referred to as the Type I and Type II receptors." @default.
- W50276713 created "2016-06-24" @default.
- W50276713 creator A5033348306 @default.
- W50276713 creator A5057904605 @default.
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- W50276713 date "1995-01-01" @default.
- W50276713 modified "2023-09-26" @default.
- W50276713 title "Activins and the Receptor Serine Kinase Superfamily" @default.
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