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Follistatin

  • Reference work entry
  • First Online:
Endocrine Pathology

Part of the book series: Encyclopedia of Pathology ((EP))

  • 34 Accesses

Synonyms

Activin-binding protein

Definition

FST is a cystein-rich glycosylated polypeptide chain of 31–39 kDa expressed in nearly all tissues of higher animals and in humans encoded by FST gene.

Features

FST is a single-chain glycosylated (N-glycosylation sites on asparagines 124 and 288) protein whose primary function consists in binding and neutralizing some members of the transforming growth factor-β (TGF-β) superfamily such as activin and bone morphogenic proteins. FST was originally identified in porcine ovarian follicular fluid and received its name because it suppresses synthesis and secretion of follicle-stimulating hormone (FSH) from the pituitary gland. FST messenger expression is stimulated by TGF-β and Activin A through Smad protein, by gonadotropin-releasing hormone (GnRH) through cyclic adenosine monophosphate (cAMP) and by the transcription factor GLI2 through the hedgehog signaling (Shukovski et al. 1995). FST is expressed in a wide variety of tissues and organs with...

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References and Further Reading

  • Amthor, H., Christ, B., Rashid-Doubell, F., Kemp, C. F., Lang, E., & Patel, K. (2002). Follistatin regulates bone morphogenetic protein-7 (BMP-7) activity to stimulate embryonic muscle growth. Developmental Biology, 243(1), 115–127.

    Article  CAS  PubMed  Google Scholar 

  • Lee, S. J., Lee, Y. S., Zimmers, T. A., Soleimani, A., Matzuk, M. M., Tsuchida, K., Cohn, R. D., & Barton, E. R. (2010). Regulation of muscle mass by follistatin and activins. Molecular Endocrinology, 24(10), 1998–2008.

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  • Matzuk, M. M., Lu, N., Vogel, H., Sellheyer, K., Roop, D. R., & Bradley, A. (1995). Multiple defects and perinatal death in mice deficient in follistatin. Nature, 374, 360–363.

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  • Phillips, D. J., & de Kretser, D. M. (1998). Follistatin: A multifunctional regulatory protein. Frontiers in Neuroendocrinology, 19, 287–322.

    Article  CAS  PubMed  Google Scholar 

  • Rodino-Klapac, L. R., Haidet, A. M., Janaiah Kota, A. M., Handy, C., Kaspar, B. K., & Mendell, J. R. (2009). Inhibition of Myostatin with emphasis on Follistatin as a therapy for muscle disease. Muscle & Nerve, 39(3), 283–296.

    Article  CAS  Google Scholar 

  • Schneyer, A. L., Hall, H. A., Lambert-Messerlian, G., Wang, Q. F., Sluss, P., & Crowley, W. F., Jr. (1996). Follistatin-activin complexes in human serum and follicular fluid differ immunologically and biochemically. Endocrinology, 137, 240–247.

    Article  CAS  PubMed  Google Scholar 

  • Schneyer, A., Schoen, A., Quigg, A., & Sidis, Y. (2003). Differential binding and neutralization of activins a and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG). Endocrinology, 144(5), 1671–1674.

    Article  PubMed  Google Scholar 

  • Shi, L., Resaul, J., Owen, S., Ye, L., & Jiang, W. J. (2016). Clinical and therapeutic implications of Follistatin in solid Tumours. Cancer Genomics Proteomics, 13(6), 425–435.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Shukovski, L., Keren-Tal, I., Dantes, A., & Amsterdam, A. (1995). Regulation of follistatin messenger ribonucleic acid in steroidogenic rat granulosa cell lines. Endocrinology, 136, 2889–2895.

    Article  CAS  PubMed  Google Scholar 

  • Sidis, Y., Schneyer, A. L., Sluss, P. M., Johnson, L. N., & Keutmann, H. T. (2001). Follistatin: Essential role for the N-terminal domain in activin binding and neutralization. The Journal of Biological Chemistry, 276, 17718–17726.

    Article  CAS  PubMed  Google Scholar 

  • Sugino, K., Kurosawa, N., Nakamura, T., Takio, K., Shimasaki, S., Ling., N., Titani, K. and Sugino, H. (1993). Molecular heterogeneity of follistatin, an activin-binding protein. The Journal of Biological Chemistry 268:15579–15587.

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  • Ueno, N., Ling, N., Ying, S. Y., Esch, F., Shimasaki, S., & Guillemin, R. (1987). Isolation and partial characterization of follistatin: A single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone. Proceedings of the National Academy of Sciences of the United States of America, 84, 8282–8286.

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Correspondence to Annamaria Colao .

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Colao, A., Pivonello, C. (2022). Follistatin. In: La Rosa, S., Uccella, S. (eds) Endocrine Pathology. Encyclopedia of Pathology. Springer, Cham. https://doi.org/10.1007/978-3-030-62345-6_5106

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  • DOI: https://doi.org/10.1007/978-3-030-62345-6_5106

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  • Publisher Name: Springer, Cham

  • Print ISBN: 978-3-030-62344-9

  • Online ISBN: 978-3-030-62345-6

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