Follistatin-315 is the predominant circulating isoform of follistatin, a glycoprotein that binds and neutralizes TGF-β family members like myostatin and activin to promote muscle growth and regulate various physiological processes.
Holdsworth-Carson. S J SJ; Craythorn. R G RG; Winnall. W R WR; Dhaliwal. K K; Genovese. R R; Nowell....
In female mice that only produce the FST‑315 version of the protein, the reproductive organs develop normally at birth but become abnormal in adulthood, showing poor tube coiling, disorganized muscle layers, fewer glands, and lots of immune cells. Hormone treatments made the inflammation worse. This suggests that having too much FST‑315 (or missing the FST‑288 form) can mess with female reproductive health.
The paper explains how activin A, a protein that influences many cell functions, is tightly regulated by several binding partners, including the two forms of follistatin (288 and 315). It shows that follistatin-315 can latch onto activin A, helping keep its levels in check, and describes the structural details of how these molecules fit together with their receptors.
Canali. Susanna S; Core. Amanda B AB; Zumbrennen-Bullough. Kimberly B KB; Merkulova. Maria M; Wang....
The study shows that a protein called activin B can raise the liver hormone hepcidin, which lowers iron levels during inflammation. The peptide follistatin‑315 blocks this effect, keeping hepcidin from spiking when the body is inflamed. The work was done in mouse liver cells and in mice given inflammatory triggers.
Datta-Mannan. Amita A; Yaden. Benjamin B; Krishnan. Venkatesh V; Jones. Bryan E BE; Croy. Johnny E J...
Scientists made a new version of the protein follistatin by attaching it to an antibody fragment and removing a part that sticks to sugars. This engineered molecule stays in the body much longer (about 100‑times longer) and reaches much higher levels (about 1,600‑times higher) than the natural form. In mice, giving this version under the skin once a week helped prevent muscle loss, something the natural protein couldn’t do when given the same way.
Datta-Mannan. Amita A; Huang. Lihua L; Pereira. Jennifer J; Yaden. Benjamin B; Korytko. Andrew A; Cr...
The study shows that a lab‑made version of follistatin‑315 attached to an antibody fragment (FST‑ΔHBS‑Fc) is covered with different sugar chains, and the amount of a specific sugar called sialic acid determines how quickly the body clears it. More sialic acid means the protein stays in the bloodstream longer, while less leads to faster removal via a liver receptor.
Ungerleider. Nathan A NA; Bonomi. Lara M LM; Brown. Melissa L ML; Schneyer. Alan L AL
Boosting activin activity in the liver makes liver cells respond better to insulin, but it also leads to a buildup of fat in the liver (steatosis). The study used mice that lack natural blockers of activin, showing that while insulin signaling improves, the liver gets fattier.
Necela. Brian M BM; Su. Weidong W; Thompson. E Aubrey EA
The study shows that turning on the PPAR‑gamma pathway (using the drug rosiglitazone) cuts down the amount of the protein follistatin made by gut cells. It does this by blocking a helper protein called Sp1 that normally boosts follistatin production. The effect isn’t because the follistatin RNA breaks down faster, but because the gene’s activity is suppressed.
Lin. Shyr-Yeu SY; Morrison. John R JR; Phillips. David J DJ; de Kretser. David M DM
This paper reviews how the protein follistatin, especially its two forms (follistatin‑288 and follistatin‑315), interacts with several growth factors that control how ovaries work. While it explains the chemistry and the network of signals, it doesn’t give any direct advice on using follistatin for health, fitness, or longevity.
Scientists created a very sensitive lab test that can measure tiny amounts of the protein follistatin in blood and other body fluids. They reported typical levels in healthy people, pregnant women, and other samples, but also found that the test can mistakenly pick up a related form called follistatin‑315, making results harder to interpret. The work is mostly about how to measure the protein, not about how to use it for health or performance.
The paper describes a new lab test for measuring the hormone Inhibin B in blood. It shows the test is fast, accurate, and doesn’t get confused by other similar proteins, including follistatin‑315, but it doesn’t give any advice on how to use Inhibin B or follistatin‑315 for health or performance.