Processing of mammalian preprogastrin-releasing peptide.


Journal Article (Review)

The processing of preprogastrin-releasing peptide in mammalian tissues and in cultured cells takes place at discrete sites (Figure 6). Signal peptidase cleaves away the signal peptide from the amino terminus of gastrin-releasing peptide. An exopeptidase activity may remove dipeptides from the amino terminus. The amidation site (not shown in Fig. 6; see Fig. 2) has the same general sequence (Gly-Lys-Lys) seen for other amidated peptides. Cleavage after single basic residues yields gene-related products from Form I or II preproGRP. A unique non-basic cleavage yields a gene-related product from Form III preproGRP. The processing that occurs to form GRP, GRP, and GRP gene-related peptides is shown in Figure 7. ProGRP is cleaved by a series of enzymes to form GRP with an amidated carboxyl-terminal methionine (indicated by an asterisk in Fig. 7). GRP is cleaved to form the decapeptide GRP. The carboxyl-terminal flanking peptides of all three mRNA translation products are cleaved to form several gastrin-releasing peptide gene-related products. Knowledge of the processing of gastrin-releasing peptide and its gene-related products will allow synthesis of duplicates of the stored forms of these peptides, which can then be used for biological testing.

Full Text

Duke Authors

Cited Authors

  • Reeve, JR; Cuttitta, F; Vigna, SR; Shively, JE; Walsh, JH

Published Date

  • January 1988

Published In

Volume / Issue

  • 547 /

Start / End Page

  • 21 - 29

PubMed ID

  • 3071218

Pubmed Central ID

  • 3071218

Electronic International Standard Serial Number (EISSN)

  • 1749-6632

International Standard Serial Number (ISSN)

  • 0077-8923

Digital Object Identifier (DOI)

  • 10.1111/j.1749-6632.1988.tb23872.x


  • eng