Follistatin
| Follistatin | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 315 amino acids | |
| Secondary to quaternary structure | Monomer | |
| Isoforms | FS315, FS288, FS303 | |
| Identifier | ||
| Gene name | FST | |
| External IDs | ||
| Occurrence | ||
| Parent taxon | Vertebrates | |
Follistatin is an autocrine glycoprotein . It occurs throughout the body in almost all more highly developed animals, with the highest concentrations being found in the ovaries and skin . It is part of the so-called inhibin -activin-follistatin axis.
A single gene, which is a direct target gene of the Wnt / beta-catenin signaling pathway during embryonic development, is held responsible for its production .
Three isoforms of follistatin are known: FS-288, FS-315 and FS-300. The first two come about through alternative splicing , FS-300 through the post-translational modification .
Effects known so far
Follistatin was isolated for the first time from the follicular fluid . The first thing we noticed was that it inhibits FSH production in the anterior pituitary gland , which is why it is also known as FSH-suppressing protein (FSP). Only later was it established that its actual main function is the antagonism to transforming growth factor (TGF) , more precisely its subgroup, the TGF-β superfamily . Here, the inhibition of activin, which in turn stimulates FSH production in the pituitary gland, plays the decisive role. It has a controlling influence on cell proliferation , on cell differentiation , and is also involved in healing after injury . During embryonic genesis, it has an inhibiting effect on the formation of bone morphogenetic protein (BMP) and is formed, among other things, by the Spemann-Mangold organizer and comparable signaling centers that control the formation of axes in the early embryo.
animal
- Follistatin is an important cofactor in liver regeneration (after liver failure) in the mouse model
- Animal experiments suggest that
- Follistatin both plays an essential role in tumor growth
- as well as stimulates vascular growth in tumors and on the corneal cells of rabbits.
- Follistatin enhances muscle growth in mammalian embryos.
- The domestic cattle breed White-Blue Belgians is bred for improved meat production with genetic defects.
- An observed improved cartilage protection in rheumatoid arthritis is associated with a reduction in F. in the SCID mouse model. (Note: the reverse conclusion that an increased incidence of follistatin is to be expected in the case of accelerated cartilage destruction in the context of rheumatoid arthritis, but has not yet been confirmed.)
human
In the case of gene mutations / defects in human newborns, follistatin is postulated as the cause of unphysiological high muscle mass.
Interactions with other substances
Trichostatin A (TSA) activates the synthesis of follistatin in the mouse model. Follistatin also inhibits myostatin and activin.
Summary
Follistatin, together with myostatin, appears to be an essential part of a control loop that controls muscle formation and regeneration. A shift in the ratio of the two substances in his favor leads to muscle hyperplasia and trophy before birth.
Manufacturing
Currently, Follistatin is made using genetically modified bacteria ( E. coli ).
Doping agents
In 2019, the seized Zollfahndungsamt food at a doping - raid also follistatin which, according to press release "written" "by experts as" new form of escalation in recreational sports will.
Individual evidence
- ↑ Homologues at OMA
- ↑ Christian Wehrle: Wnt / beta-catenin target genes in mouse development . Freiburg 2003, urn : nbn: de: bsz: 25-opus-12171 (dissertation, University of Freiburg).
- ↑ Ali Hemmati-Brivanlou, Olivia G. Kelly, Douglas A. Melton: Follistatin, an antagonist of activin, is expressed in the Spemann organizer and displays direct neuralizing activity . In: Cell . tape 77 , no. 2 , 1994, p. 283-295 , doi : 10.1016 / 0092-8674 (94) 90320-4 .
- ↑ F. J Hoetomo, K. Presser, H. Ittrich, M. Blessing, A. Quaas, AW Lohse, C. Schramm: The effect of follistatin on liver regeneration in a mouse model . In: Journal of Gastroenterology . tape 45 , no. 1 , 2007, doi : 10.1055 / s-2007-967811 .
- ↑ a b Jelena Krneta: The role of the activin / follistatin system during angiogenesis and tumor progression . Freiburg 2004, urn : nbn: de: bsz: 25-opus-13741 (dissertation, University of Freiburg).
- ↑ Rocnik EF, Liu P, Sato K, Walsh K, Vaziri C: The novel SPARC family member SMOC-2 potentiates angiogenic growth factor activity . In: J. Biol. Chem. . 281, No. 32, August 2006, pp. 22855-64. doi : 10.1074 / jbc.M513463200 . PMID 16774925 .
- ↑ Helge Amthor: About the stimulation of embryonic muscle growth by follistatin . Freiburg 2001, DNB 962290971 (dissertation, University of Freiburg).
- ↑ Genetic defect in the cattle breed "Belgian Blue" ( Memento of the original from September 30, 2007 in the Internet Archive ) Info: The archive link was inserted automatically and has not yet been checked. Please check the original and archive link according to the instructions and then remove this notice. .
- ↑ a b Metabolism of the fibroblasts in rheumatoid arthritis ( Memento from September 5, 2004 in the Internet Archive ) (PDF; 1.1 MB)
- ↑ Holger Dambeck: Mutation: boy prodigy carries muscle gene. In: Spiegel Online . June 24, 2004, accessed May 3, 2018 .
- ↑ a b Page no longer available , search in web archives: Lorenzo Puri ( Page no longer available , search in web archives ) Info: The link was automatically marked as defective. Please check the link according to the instructions and then remove this notice.
- ↑ Data sheet Follistatin (FST), human, recombinant ( Memento of the original from June 7, 2007 in the Internet Archive ) Info: The archive link has been inserted automatically and has not yet been checked. Please check the original and archive link according to the instructions and then remove this notice.
- ↑ ZOLL-E: Webshop for doping substances smashed on presseportal.de from April 3, 2019, accessed on April 3, 2019.
