Characterization of the bombesin receptor on mouse pancreatic acini by chemical cross-linking

Peptides. 1990 Nov-Dec;11(6):1143-50. doi: 10.1016/0196-9781(90)90144-t.


Bombesin (BN), gastrin-releasing peptide (GRP) and GRP(18-27) (neuromedin C) were equipotent and 30-fold more potent than neuromedin B (NMB) in inhibiting binding of 125I-GRP to and in stimulating amylase release from mouse pancreatic acini. In the present study we used 125I-GRP and chemical cross-linking techniques to characterize the mouse pancreatic BN receptor. After binding of 125I-GRP to membranes, and incubation with various chemical cross-linking agents, cross-linked radioactivity was analyzed by SDS-PAG electrophoresis and autoradiography. With each of 4 different chemical cross-linking agents, there was a single broad polypeptide band of Mr 80,000. Cross-linking did not occur in the absence of the cross-linking agent. Cross-linking was inhibited only by peptides that interact with the BN receptor such as GRP, NMB, GRP(18-27) or BN. Dose-inhibition curves for the ability of BN or NMB to inhibit binding of 125I-GRP to membranes or cross-linking to the 80,000 polypeptide demonstrated for both that BN was 15-fold more potent than NMB. The apparent molecular weight of the cross-linked polypeptide was unchanged by adding dithiothreitol. N-Glycanase treatment reduced the molecular weight of the cross-linked peptide to 40,000. The present results indicate that the BN receptor on mouse pancreatic acinar cell membranes resembles that recently described on various tumor cells in being a single glycoprotein with a molecular weight of 76,000. Because dithiothreitol had no effect, this glycoprotein is not a subunit of a larger disulfide-linked structure.

MeSH terms

  • Amidohydrolases
  • Amylases / metabolism
  • Animals
  • Bombesin* / metabolism
  • Cell Membrane / metabolism
  • Cross-Linking Reagents*
  • Gastrin-Releasing Peptide
  • In Vitro Techniques
  • Iodine Radioisotopes
  • Male
  • Mice
  • Neurokinin B / analogs & derivatives
  • Neurokinin B / metabolism
  • Pancreas / chemistry*
  • Pancreas / enzymology
  • Peptide Fragments / metabolism
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Peptides / metabolism
  • Receptors, Bombesin
  • Receptors, Neurotransmitter / chemistry*
  • Receptors, Neurotransmitter / metabolism


  • Cross-Linking Reagents
  • Iodine Radioisotopes
  • Peptide Fragments
  • Peptides
  • Receptors, Bombesin
  • Receptors, Neurotransmitter
  • Gastrin-Releasing Peptide
  • neuromedin C
  • Neurokinin B
  • neuromedin B
  • Amylases
  • Amidohydrolases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Bombesin