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Calcitonin gene-related peptide is metabolized by an endopeptidase hydrolyzing substance-p

Academic Article
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Overview

authors

  • Legreves, P.
  • Nyberg, F.
  • Hokfelt, T.
  • Terenius, Lars

publication date

  • June 1989

journal

  • Regulatory Peptides  Journal

abstract

  • Calcitonin gene-related peptide (CGRP) is cleaved by an endopeptidase, also known to hydrolyze substance P (SP). The enzyme which was isolated from human cerebrospinal fluid, converted rCGRP into two products, clearly separable on HPLC. Amino acid analysis showed cleavage to occur at Leu16-Ser17. The carboxy-terminal fragment, rCGRP-(17-37), was weakly active in inhibiting 125I-rCGRP binding to a rat medulla oblongata membrane preparation, but it showed no binding to spinal cord membranes. The N-terminal fragment, rCGRP-(1-16), had very low or no affinity. Autoradiography with 125I-rCGRP showed distinct labelling of rat dorsal spinal cord, while there was no consistent pattern with 125I-rCGRP-(1-16). In the isolated guinea pig ileum preparation, the two fragments showed no CGRP-like activity. The ability of CGRP to interfere with SP degradation is offered as the explanation why CGRP has been reported to potentiate several biologic actions of SP.

subject areas

  • Amino Acid Sequence
  • Amino Acids
  • Animals
  • Calcitonin
  • Calcitonin Gene-Related Peptide
  • Endopeptidases
  • Humans
  • Hydrolysis
  • Male
  • Medulla Oblongata
  • Molecular Sequence Data
  • Neuropeptides
  • Rats
  • Rats, Inbred Strains
  • Receptors, Calcitonin
  • Receptors, Cell Surface
  • Spinal Cord
  • Substance P
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Identity

International Standard Serial Number (ISSN)

  • 0167-0115

Digital Object Identifier (DOI)

  • 10.1016/0167-0115(89)90176-6

PubMed ID

  • 2475892
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Additional Document Info

start page

  • 277

end page

  • 286

volume

  • 25

issue

  • 3

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