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Follistatin Binds to both Activin and Inhibin through the Common Beta-Subunit
Abstract
Inhibin, activin, and follistatin are three families of polypeptides originally isolated and characterized from ovarian follicular fluid based on their modulation of FSH release from pituitary cell culture. In addition to their effects on FSH synthesis and secretion, inhibin and activin have other biological functions. By contrast, the physiological significance of follistatin was obscure, until it was discovered that follistatin is a binding protein to activin. Since activin binds to follistatin, it is imperative to determine the nature of the activin/follistatin binding complex. Moreover, because inhibin contains a beta-subunit derived from activin, it is important to determine whether inhibin will also bind follistatin. Using a double-ligand blotting technique, we have determined that activin-A has two binding sites for follistatin, whereas inhibin-A has only one binding site for follistatin. Therefore, these results suggest that follistatin binds to both activin and inhibin through the common beta-subunit.
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Citations
Cited by
Qiao, J., & Feng, H. L. (2011) · Human Reproduction Update · doi:10.1093/humupd/dmq032 · Cited by 479
Burger, L. L., Dalkin, A. C., Aylor, K. W., Haisenleder, D. J., & Marshall, J. C. (2002) · Endocrinology · doi:10.1210/en.2002-220216 · Cited by 98
Circulating follistatin in relation to energy metabolism
Hansen, J. S., & Plomgaard, P. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.06.002 · Cited by 62
Clinical and therapeutic implications of follistatin in solid tumours
SHI, L., RESAUL, J., OWEN, S., YE, L., & JIANG, W. G. (2016) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20005 · Cited by 47
Popovics, P., Rekasi, Z., Stewart, A. J., & Kovacs, M. (2011) · Journal of Endocrinology · doi:10.1530/joe-10-0485 · Cited by 13
Metadata
- Authors
- Shimonaka, M., Inouye, S., Shimasaki, S., & Ling, N.
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1991-06
- Volume
- 128
- Issue
- 6
- Pages
- 3313-3315
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2044804295
- Cited by
- 258
- References
- 0
- FWCI
- 5.45
- Type
- journal article
- Language
- en
- Open access
- closed
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