2003 Volume 24 Issue 4 Pages 181-186
Gastrin-releasing peptide (GRP) was originally isolated from porcine upper gastric tissue. Its structure was found to contain a C-terminal region with striking homology toward bombesin. Recently, GRP has been suggested as an important novel regulatoiy peptide in the female reproductive tract of mammals, including the cow. However, the nature of GRP in the uterus of cows remains to be determined, and there are no reports on the nucleotide sequence of cDNA encoding bovine GRP. In this study, we have determined the GRP cDNA from bovine endometrial tissues. The GRP cDNA consists of 973 bp, comprising a short 5'-untranslated region (108 bp), an open reading frame (543 bp), a stop codon (TGA), and a 3'-untranslated region (319 bp), including a polyadenylation signal (AATAAA) and a poly (A) tail. The deduced amino acid sequence shows that bovine GRP is part of a 182 amino acids precursor. The putative mature bovine GRP is composed of 27 amino acids after 28 amino acid signal peptide. At the C-terminus, the GRP sequence is flanked by one Gly and two basic residues (Lys-Lys), indicative of C-terminal amidation and cleavage site.
