Primary structure of frog PYY: Implications for the molecular evolution of the pancreatic polypeptide family
ABSTRACT A peptide belonging to the pancreatic polypeptide (PP) family was isolated in pure form from the intestine of the European green frog (Rana ridibunda). The primary structure of the peptide was established as: Tyr-Pro-Pro-Lys-Pro-Glu-Asn-Pro-Gly-Glu10-Asp-Ala- Ser-Pro-Glu-Glu-Met-Thr-Lys-Tyr20-Leu-Thr-Ala-Leu-Arg-His-Tyr-Ile- Asn-Leu30-Val - Thr-Arg-Gln-Arg-Tyr-NH2. This amino acid sequence shows moderate structural similarity to human PYY (75% identity) but stronger similarity to the PP family peptides isolated from the pancreas of the salmon (86%) and dogfish (83%). The data suggest that the two putative duplications of an ancestral PP family gene that have given rise to PP, PYY and NPY in mammals had already taken place by the time of the appearance of the amphibia. In fish, however, only a single duplication has occurred, giving rise to NPY in nervous tissue and a PYY-related peptide in both pancreas and gut.
- SourceAvailable from: Leonardo De Azevedo Calderon
- "In Phyllomedusa, the only peptide pharmacologically and structurally related to NPY described was the skin polypeptide YY (SPYY) (Mor et al. 1994a). SPYY was purified from acetic extracts of Phyllomedusa bicolor skin (Mor et al. 1994b), exhibiting 94% of similarity with PYY from the frog Rana ridibunda (Conlon et al. 1992) and 86% of similarity with human PYY (Kohri et al. 1993) (Table 10). The primary structures of the two frog NPYs are highly conserved presenting only two amino acid substitutions (positions 7 and 18) (Table 10). "
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ABSTRACT: A peptide of the pancreatic polypeptide (PP) family was isolated in pure form from the brain of an elasmobranch fish, Scyliorhinus canicula (European common dogfish). The primary structure of the peptide was established as: Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu10-Gly-Ala-Pro-Ala-Glu-Asp- Leu-Ala-Lys- Tyr20-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu30-Ile-Thr-Arg- Gln-Arg-Tyr-NH2. This sequence contains only two amino acid substitutions compared with pig neuropeptide Y (NPY) (Gly for Asp11 and Lys for Arg19), and two substitutions (Gly for Asp11 and Leu for Met17) compared with frog NPY. The amino acid sequence of NPY from dogfish brain is appreciably different from the neuropeptide Y-related peptide previously isolated from dogfish pancreas (five amino acid substitutions). The data indicate that evolutionary pressure to conserve the complete primary structure of neuropeptide Y has been very strong. It is suggested that the NPY-related peptide present in the pancreas of elasmobranch and teleost fish represents the piscine equivalent of mammalian peptide tyrosine tyrosine (PYY).Peptides 05/1992; 13(3):493-7. DOI:10.1016/0196-9781(92)90080-M · 2.62 Impact Factor
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ABSTRACT: Although the amino acid sequence of members of the pancreatic polypeptide (PP)-family of regulatory peptides has been poorly conserved during vertebrate evolution, the overall length of the peptides (36 amino acid residues) has remained constant. Nucleotide sequence analysis of cloned cDNAs and/or genomic fragments has shown the PP-related sequence immediately follows the signal peptide in the prepropeptides. A peptide tyrosine-tyrosine (PYY)-related peptide with 37 residues has been isolated from the chicken intestine, and its primary structure was established as: Ala-Tyr-Pro-Pro-Lys-Pro-Glu-Ser-Pro-Gly10-Asp-Ala-Ala-Ser-P ro-Glu-Glu-Ile-Ala-Gln20-Tyr-Phe-Ser-Ala-Leu-Arg-His-Tyr-Il e-Asn30-Leu-Val-Thr-Arg-Gln-Arg-Tyr.CONH2. The presence of an additional alanine residue at the NH2-terminus of the peptide suggests that the site of cleavage of the signal peptide in chicken preproPYY is different from the site of cleavage in other PP-family prepropeptides.FEBS Letters 12/1992; 313(3):225-8. DOI:10.1016/0014-5793(92)81196-S · 3.17 Impact Factor