Cited by 232Sperm and Testicular FunctionHypothalamic control of reproductive hormonesReproductive Biology and Fertility

Primary structure of the human follistatin precursor and its genomic organization

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Shimasaki, S, Koga, M, Esch, F, Cooksey, K, Mercado, M, Koba, A, Ueno, N, Ying, S Y +2 more·1988·Proceedings of the National Academy of Sciences

Abstract

Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. By use of the recently characterized porcine follistatin cDNA as a probe to screen a human testis cDNA library and a genomic library, the structure of the complete human follistatin precursor as well as its genomic organization have been determined. Three of eight cDNA clones that were sequenced predicted a precursor with 344 amino acids, whereas the remaining five cDNA clones encoded a 317 amino acid precursor, resulting from alternative splicing of the precursor mRNA. Mature follistatins contain four contiguous domains that are encoded by precisely separated exons; three of the domains are highly similar to each other, as well as to human epidermal growth factor and human pancreatic secretory trypsin inhibitor. The genomic organization of the human follistatin is similar to that of the human epidermal growth factor gene and thus supports the notion of exon shuffling during evolution.

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  • FST is present in three main isoforms, FST288, FST303, and FST315, with FST315 being the predominant isoform in circulation.

    “FST is present in three main isoforms, FST288, FST303, and FST315, with FST315 being the predominant isoform found in the circulation [185,194,195].”

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Research works printed but not linked: 3

  1. Ling, N., Ying, S.-Y., Ueno, N., Esch, F., Denoroy, L. & Guillemin, R. (1985) Proc. Nati. Acad. Sci. USA 82,7217-7221.
  2. Ueno, N., Ling, N., Ying, S.-Y., Esch, F., Shimasaki, S. & Guillemin, R. (1987) Proc. Natl. Acad. Sci. USA 84,8282-8286.
  3. Sanger, F., Nicklen, S. & Coulson, A. R. (1977) Proc. Natl. Acad. Sci. USA 74, 5463-5467.

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Authors
Shimasaki, S., Koga, M., Esch, F., Cooksey, K., Mercado, M., Koba, A., Ueno, N., Ying, S. Y., Ling, N., & Guillemin, R.
Affiliations
Salk Institute for Biological Studies (US)
Venue
Proceedings of the National Academy of Sciences
Published
1988-06
Volume
85
Issue
12
Pages
4218-4222
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2011775394
Cited by
232
References
24
Citations by year
2025: 2 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 4 · 2017: 9 · 2016: 5 · 2015: 7 · 2014: 2 · 2013: 7 · 2012: 2
FWCI
8.56
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK 18811)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-09690, N01HD6-2944)
Topics
  • Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
  • Health Sciences › Medicine › Reproductive Medicine › Hypothalamic control of reproductive hormones
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Reproductive Biology and Fertility
Keywords
follistatin, primary structure, genome organization, alternative splicing, exon shuffling, testis, epidermal growth factor, pancreatic secretory trypsin inhibitor, cDNA cloning, gene evolution
MeSH terms
Adult, Amino Acid Sequence, Base Sequence, Cloning, Molecular, DNA, Genes, Genetic Vectors, Glycoproteins, Humans, Lymphocytes, Male, Molecular Sequence Data, Protein Precursors, Testis, Follistatin

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