TY - JOUR
T1 - Identification, structural determination, and biological activity of bovine and canine calcitonin receptor-stimulating peptides
AU - Katafuchi, Takeshi
AU - Hamano, Kazumasa
AU - Minamino, Naoto
N1 - Funding Information:
This work was supported in part by research grants from the Ministry of Education, Culture, Sports, Science and Technology (Special Coordination Funds for the Promotion of Science and Technology, and Grant-in-Aid for Scientific Research on Encouragement of Young Scientists), from the Ministry of Health, Labor and Welfare (Cardiovascular Diseases), and from the Organization for Pharmaceutical Safety and Research (Medical Frontier Project) of Japan. The authors are grateful to Dr. Kangawa of this institute and Dr. Matsuo of Miyazaki Medical College for discussion, and to Ms. A. Okabe, Y. Takada, and S. Fujiwara of this institute for technical assistance.
PY - 2004/1/2
Y1 - 2004/1/2
N2 - 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-PK1 cells 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-PK1 cells 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.
AB - 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-PK1 cells 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-PK1 cells 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.
KW - Calcitonin
KW - Calcitonin gene-related peptide
KW - Calcitonin receptor
KW - Calcitonin receptor-stimulating peptide
KW - Calcitonin-like receptor
KW - Receptor activity-modifying protein
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U2 - 10.1016/j.bbrc.2003.11.114
DO - 10.1016/j.bbrc.2003.11.114
M3 - Article
C2 - 14672700
AN - SCOPUS:0346850787
SN - 0006-291X
VL - 313
SP - 74
EP - 79
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -