Identification, structural determination, and biological activity of bovine and canine calcitonin receptor-stimulating peptides.
Identification, structural determination, and biological activity of bovine and canine calcitonin receptor-stimulating peptides.
复制标题
牛和犬降钙素受体刺激肽的鉴定、结构测定和生物活性。
DOI:
10.1016/j.bbrc.2003.11.114
复制
发表时间:
2004
影响因子:
3.1
通讯作者:
N. Minamino
中科院分区:
文献类型:
--
作者:
T. Katafuchi;K. Hamano;N. Minamino
We have recently identified in porcine brain a series of new peptides, designated calcitonin receptor-stimulating peptide-1 (CRSP-1), CRSP-2, and CRSP-3, but failed to find their counterparts in humans and rodents by either database searching or experimental cross-hybridization. In this study, we isolated cDNAs encoding precursors of bovine CRSP-1, canine CRSP-1, and canine CRSP-2 from their thyroid cDNA libraries. Although the deduced mature amino acid sequences of bovine and canine CRSP-1s and canine CRSP-2 showed identity with their respective porcine CRSP counterparts, none of them had a C-terminal amide structure. In LLC-PK1cells endogenously expressing the calcitonin (CT) receptor, bovine and canine CRSP-1s enhanced the cAMP production, while canine CRSP-2 did not stimulate it at all. Equine CGRP-I had a high identity in its amino acid sequence with porcine CRSP-1 and stimulated LLC-PK1cells at a potency comparable to that of porcine CT. None of these CRSPs or equine CGRP-I stimulated the CT-like receptor, even in the presence of receptor activity-modifying proteins. These results demonstrate that CRSP-1, a new class of biologically active peptide, is present in animals evolutionarily close to pigs and induces its activity through the calcitonin receptor, suggesting a wide existence and common properties of this peptide in mammals.
影响因子:
56.9
作者:
LIN, HY;HARRIS, TL;GOLDRING, SR
通讯作者:
GOLDRING, SR