Inhibin A-subunit cDNAs from porcine ovary and human placenta.
Inhibin, a gonadal protein that preferentially suppresses the secretion of pituitary follicle-stimulating hormone, has been isolated from porcine follicular fluid and characterized as a 32-kDa protein composed of 18-kDa and 14-kDa subunits. In the present work, oligonucleotide probes predicted from amino-terminal inhibin amino acid sequences have been used to isolate, from a porcine ovarian lambda gt11 cDNA library, clones encoding the 18-kDa subunit, or A chain, of inhibin. DNA sequence analysis showed that the inhibin A chain is initially synthesized as a larger precursor protein and is predicted to be a glycopeptide. Inhibin A-chain mRNA is present specifically in the gonads, and its synthesis can be induced by treatment of the animal with gonadotropins. The porcine probe was used to isolate a human inhibin A-subunit cDNA from a placental cDNA library. The human precursor is highly homologous to its porcine counterpart and is predicted to generate an 18-kDa glycosylated inhibin A subunit.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D005260:Female; D006801:Humans; D007265:Inhibins / Q000235:genetics*; D010053:Ovary / Q000378:metabolism*; D010920:Placenta / Q000378:metabolism*; D011247:Pregnancy; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013552:Swine
D007265:Inhibins; D004247:DNA; D004262:DNA Restriction Enzymes