The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

FST  -  follistatin

Sus scrofa

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of FST

  • To further explore the physiological role of follistatin, we have expressed recombinant human follistatins with 315 (rhFS-315) and 288 (rhFS-288) amino acids in Chinese hamster ovary cells under the control of the simian virus-40 promoter [1].

High impact information on FST


Biological context of FST

  • The first exon encodes the putative signal sequence, followed by four exons which encode the four domains of FS, three of which are highly homologous to each other [5].
  • Herein, we report the cloning of the porcine FS gene whose DNA structure reveals that the two populations of mRNA are generated by alternative splicing [5].
  • The FST per locus varied from 0.019 (S0090) to 0.170 (SW951), and the average FST of all loci was 0.077, which means that most of the genetic variation was kept within breeds and only a little of the genetic variation exists between populations [6].
  • Follistatin gene expression was induced by a 2-h incubation with EGF (3 nM), but not by LH (100 ng/ml), GnRH (10 nM) or prostaglandin F2 alpha (80 micrograms/ml) [4].
  • Within an animal, concentration of FS mRNAs was related more to stage of the follicular phase than to follicular size [7].

Anatomical context of FST


Associations of FST with chemical compounds

  • Stimulation of follistatin mRNA accumulation in cultured granulosa cells by dibutyryl cAMP (30, 100 and 300 mumol l-1) and forskolin (3, 10 and 100 mumol l-1) was dose dependent [9].
  • As 50% acetonitrile (CH3CN) separated free and follistatin-bound activin, plasma pretreated with an equal volume of CH3CN was used as the assay sample and B/F separation was also done with 50% CH3CN [10].

Other interactions of FST

  • Characterization of a line of pigs previously selected for increased litter size for RBP4 and follistatin [11].
  • The time course of induction of follistatin mRNA by EGF was very similar to that induced by PMA, with maximal stimulation occurring at 2 h and declining thereafter [4].
  • Follistatin mRNA was quantitated by slot blot hybridization of total RNA from primary cultures of porcine granulosa cells treated with the phorbol ester phorbol 12-myristate 13-acetate (PMA), an activator of PKC [4].
  • This study tested our hypothesis that inhibin/activin (I/A) betaB subunit and not follistatin (FS) gene expression relates positively to plasma FSH concentrations in the anterior pituitary gland of boars [12].

Analytical, diagnostic and therapeutic context of FST


  1. Recombinant expression of human follistatin with 315 and 288 amino acids: chemical and biological comparison with native porcine follistatin. Inouye, S., Guo, Y., DePaolo, L., Shimonaka, M., Ling, N., Shimasaki, S. Endocrinology (1991) [Pubmed]
  2. Radioimmunoassay of follistatin: application for in vitro fertilization procedures. Sugawara, M., Depaolo, L., Nakatani, A., DiMarzo, S.J., Ling, N. J. Clin. Endocrinol. Metab. (1990) [Pubmed]
  3. Breed differences in expression of inhibin/activin subunits in porcine anterior pituitary glands. Li, M.D., MacDonald, G.J., Ford, J.J. Endocrinology (1997) [Pubmed]
  4. Regulation of follistatin messenger ribonucleic acid in porcine granulosa cells by epidermal growth factor and the protein kinase-C pathway. Lindsell, C.E., Misra, V., Murphy, B.D. Endocrinology (1993) [Pubmed]
  5. Porcine follistatin gene structure supports two forms of mature follistatin produced by alternative splicing. Shimasaki, S., Koga, M., Esch, F., Mercado, M., Cooksey, K., Koba, A., Ling, N. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  6. Genetic variation and relationships of eighteen Chinese indigenous pig breeds. Yang, S.L., Wang, Z.G., Liu, B., Zhang, G.X., Zhao, S.H., Yu, M., Fan, B., Li, M.H., Xiong, T.A., Li, K. Genet. Sel. Evol. (2003) [Pubmed]
  7. Expression of follistatin and inhibin/activin subunit genes in porcine follicles. Li, M.D., DePaolo, L.V., Ford, J.J. Biol. Reprod. (1997) [Pubmed]
  8. Uterine-embryonic interaction in pig: activin, follistatin, and activin receptor II in uterus and embryo during early gestation. van de Pavert, S.A., Boerjan, M.L., Stroband, H.W., Taverne, M.A., van den Hurk, R. Mol. Reprod. Dev. (2001) [Pubmed]
  9. Regulation of follistatin gene expression in the ovary and in primary cultures of porcine granulosa cells. Lindsell, C.E., Misra, V., Murphy, B.D. J. Reprod. Fertil. (1994) [Pubmed]
  10. Competitive protein binding assay for activin A/EDF using follistatin determination of activin levels in human plasma. Demura, R., Suzuki, T., Tajima, S., Mitsuhashi, S., Odagiri, E., Eto, Y., Sugino, H., Demura, H. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  11. Characterization of a line of pigs previously selected for increased litter size for RBP4 and follistatin. Blowe, C.D., Boyette, K.E., Ashwell, M.S., Eisen, E.J., Robison, O.W., Cassady, J.P. J. Anim. Breed. Genet. (2006) [Pubmed]
  12. Positive association between expression of follicle-stimulating hormone beta and activin betaB-subunit genes in boars. Li, M.D., Macdonald, G.J., Wise, T., Ford, J.J. Biol. Reprod. (1998) [Pubmed]
  13. Comparison of the V1b antagonist, SSR149415, and the CRF1 antagonist, CP-154,526, in rodent models of anxiety and depression. Hodgson, R.A., Higgins, G.A., Guthrie, D.H., Lu, S.X., Pond, A.J., Mullins, D.E., Guzzi, M.F., Parker, E.M., Varty, G.B. Pharmacol. Biochem. Behav. (2007) [Pubmed]
WikiGenes - Universities