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. 1988 Jun;85(12):4218–4222. doi: 10.1073/pnas.85.12.4218

Primary structure of the human follistatin precursor and its genomic organization.

S Shimasaki 1, M Koga 1, F Esch 1, K Cooksey 1, M Mercado 1, A Koba 1, N Ueno 1, S Y Ying 1, N Ling 1, R Guillemin 1
PMCID: PMC280398  PMID: 3380788

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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