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XB-ART-29884
Proc Natl Acad Sci U S A 1984 Jan 01;812:380-4.
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Xenopsin: the neurotensin-like octapeptide from Xenopus skin at the carboxyl terminus of its precursor.

Sures I , Crippa M .


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We have synthesized two oligodeoxyribonucleotide mixtures that contain sequences complementary to different parts of the hypothetical mRNA sequence of xenopsin, a biologically active octapeptide found in skin extracts from Xenopus laevis. The two primer pools were independently used to initiate reverse transcription on skin poly(A)+ RNA and the resulting cDNAs were then used to screen in parallel a cDNA library prepared from skin poly(A)+ RNA. One of the clones that hybridized with both probes was subjected to sequence analysis. It contains a nearly full-length DNA copy of a mRNA of approximately equal to 490 nucleotides that encodes a xenopsin precursor protein. The deduced precursor is 80 amino acids long, exhibits a putative signal sequence at the NH2 terminus, and contains the biologically active peptide at the COOH terminus. The region corresponding to the NH2-terminal portion of the xenopsin precursor shows a striking nucleotide and amino acid sequence homology with the precursor of PYLa, another recently described peptide from Xenopus skin.

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Species referenced: Xenopus laevis
Genes referenced: levi pgla

References [+] :
Araki, Isolation and structure of a new active peptide "Xenopsin" on the smooth muscle, especially on a strip of fundus from a rat stomach, from the skin of Xenopus laevis. 1973, Pubmed, Xenbase