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also known as activin-binding protein is a protein that in humans is encoded by the FST gene.[1][2]
Follistatin is an autocrine glycoprotein that is expressed in nearly all tissues of higher animals.
Its primary function is the binding and bioneutralization of members of the TGF-β superfamily, with
a particular focus on activin, a paracrine hormone.An earlier name for the same protein was
FSH-suppressing protein (FSP). At the time of its initial isolation from follicular fluid, it was
found to inhibit the anterior pituitary's secretion of follicle-stimulating hormone (FSH).

 follistatin is part of the inhibin-activin-follistatin axis.Currently there are three reported isoforms,
FS-288, FS-300, and FS-315. Two, FS-288 and FS-315, are known to be created by alternative splicing of
the primary mRNA transcript. FS-300 (porcine follistatin) is thought to be the product ofposttranslational
modification via truncation of the C-terminal domain from the primary amino-acid chain.Although FS is
ubiquitous its highest concentration has been found to be in the female ovary, followed by the skin.The
activin-binding protein follistatin is produced by folliculostellate (FS) cells of the anterior pituitary.
FS cells make numerous contacts with the classical endocrine cells of the anterior pituitary including
gonadotrophs.In the tissues activin has a strong role in cellular proliferation, thereby making follistatin
the safeguard against uncontrolled cellular proliferation and also allowing it to function as an instrument of
cellular differentiation. Both of these roles are vital in tissue rebuilding and repair, and may account for
follistatin's high presence in the skin.In the blood, activin and follistatin are both known to be involved in
the inflammatory response following tissue injury or pathogenic incursion. The source of follistatin in
circulating blood plasma has yet to be determined, but due to its autocrinenature speculation suggests the
endothelial cells lining all blood vessels, or the macrophages and monocytes also circulating within the whole
blood, may be sources.Follistatin is involved in the development of the embryo. It has inhibitory action on bone
morphogenic proteins (BMPs); BMPs induce the ectoderm to become epidermal ectoderm. Inhibition of BMPs allows
neuroectoderm to arise from ectoderm, a process which eventually forms the neural plate. Other inhibitors involved
in this process are noggin and chordin.Follistatin and BMPs are also known to play a role in folliculogenesis within
the ovary. The main role of follistatin in the oestrus/menstrus ovary, so far, appears to be progression of the follicle
from early antral to antral/dominant, and importantly the promotion of cellular differentiation of the estrogen producing
granulosa cells (GC) of the dominant follicle into theprogesterone producing large lutein cells (LLC) of the corpus luteum.

 Follistatin is being studied for its role in regulation of muscle growth in mice, as an antagonist to myostatin (also
known as GDF-8, a TGF superfamily member) which inhibitsexcessive muscle growth. Lee & McPherron demonstrated that inhibition
of GDF-8, either by genetic elimination (knockout mice) or by increasing the amount of follistatin, resulted in greatly
increased muscle mass.[3][4] In 2009, research with macaque monkeys demonstrated that regulating follistatin via gene
therapy also resulted in muscle growth and increases in strength. This research paves the way for human clinical trials,
which are hoped to begin in the summer of 2010 on Inclusion body myositis.[5]A study has also shown that increased levels
of follistatin, by leading to increased muscle mass of certain core muscular groups, can increase life expectancy in cases
of spinal muscular atrophy (SMA) in animal models.[6]It is also being investigated for its involvement in
polycystic ovary syndrome (PCOS), though there is debate as to its direct role in this infertility disease.