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.
| Original language | English |
|---|---|
| Pages (from-to) | 4218-4222 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 85 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - Jan 1 1988 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
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Cite this
Primary structure of the human follistatin precursor and its genomic organization. / Shimasaki, S.; Koga, M.; Esch, F.; Cooksey, K.; Mercado, M.; Koba, A.; Ueno, N.; Ying, S. Y.; Ling, N.; Guillemin, R.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 12, 01.01.1988, p. 4218-4222.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Primary structure of the human follistatin precursor and its genomic organization
AU - Shimasaki, S.
AU - Koga, M.
AU - Esch, F.
AU - Cooksey, K.
AU - Mercado, M.
AU - Koba, A.
AU - Ueno, N.
AU - Ying, S. Y.
AU - Ling, N.
AU - Guillemin, R.
PY - 1988/1/1
Y1 - 1988/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0023772938&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023772938&partnerID=8YFLogxK
U2 - 10.1073/pnas.85.12.4218
DO - 10.1073/pnas.85.12.4218
M3 - Article
C2 - 3380788
AN - SCOPUS:0023772938
VL - 85
SP - 4218
EP - 4222
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 12
ER -