gastrin-releasing-peptide and ethylene-glycolylbis(succinimidyl-succinate)

gastrin-releasing-peptide has been researched along with ethylene-glycolylbis(succinimidyl-succinate)* in 2 studies

Other Studies

2 other study(ies) available for gastrin-releasing-peptide and ethylene-glycolylbis(succinimidyl-succinate)

ArticleYear
Characterization of a bombesin receptor on Swiss mouse 3T3 cells by affinity cross-linking.
    Journal of cellular biochemistry, 1988, Volume: 38, Issue:4

    We have previously identified by chemical cross-linking a cell surface protein in Swiss 3T3 cells of apparent Mr 75,000-85,000, which may represent a major component of the receptor for peptides of the bombesin family in these cells. Because bombesin-like peptides may interact with other cell surface molecules, it was important to establish the correlation between receptor binding and functions of this complex and further characterize the Mr 75,000-85,000 cross-linked protein. Detailed time courses carried out at different temperatures demonstrated that the Mr 75,000-85,000 affinity-labelled band was the earliest cross-linked complex detected in Swiss 3T3 cells incubated with 125I-labelled gastrin-releasing peptide (125I-GRP). Furthermore, the ability of various nonradioactive bombesin agonists and antagonists to block the formation of the Mr 75,000-85,000 cross-linked complex correlated extremely well (r = 0.994) with the relative capacity of these peptides to inhibit 125I-GRP specific binding. Pretreatment with unlabelled GRP for up to 6 h caused only a slight decrease in both specific 125I-GRP binding and the affinity labelling of the Mr 75,000-85,000 protein. We also show that the cross-linked complex is a glycoprotein. First, solubilized affinity labelled Mr 75,000-85,000 complex applied to wheat germ lectin-sepharose columns was eluted by addition of 0.3 M N-acetyl-D-glucosamine. Second, treatment with endo-beta-N-acetylglucosaminidase F reduced the apparent molecular weight of the affinity-labelled band from 75,000-85,000 to 43,000, indicating the presence of N-linked oligosaccharide groups.

    Topics: Affinity Labels; Animals; Binding, Competitive; Bombesin; Cell Membrane; Cells, Cultured; Cross-Linking Reagents; Gastrin-Releasing Peptide; Iodine Radioisotopes; Kinetics; Mice; Molecular Weight; Peptides; Receptors, Bombesin; Receptors, Neurotransmitter; Succinimides

1988
Identification of a receptor for peptides of the bombesin family in Swiss 3T3 cells by affinity cross-linking.
    The Journal of biological chemistry, 1987, Mar-25, Volume: 262, Issue:9

    The cross-linking agent ethylene glycol-bis(succinimidyl succinate) was used to covalently link 125I-labeled gastrin releasing peptide (125I-GRP) to an Mr 75,000-85,000 surface protein in Swiss 3T3 cells that displays many characteristics of a specific receptor for peptides of the bombesin family. This protein was not present in other cell lines which do not exhibit receptors for bombesin-like peptides. Unlabeled GRP competed for affinity labeling of the Mr 75,000-85,000 protein in a concentration-dependent manner, and other bombesin-related peptides also inhibited the cross-linking of 125I-GRP to this component. In contrast, high concentrations of a variety of other peptide hormones and mitogens had no effect. Affinity labeling of the Mr 75,000-85,000 protein was dependent on the concentration of 125I-GRP and exhibited saturability. 125I-GRP affinity labeling of this protein was also demonstrated by two-dimensional gel electrophoresis. These studies suggest that an Mr 75,000-85,000 surface protein with an isoelectric point of 6.0 to 6.5 is a major component of the receptor for peptides of the bombesin family in Swiss 3T3 cells.

    Topics: Affinity Labels; Animals; Binding, Competitive; Cell Line; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Gastrin-Releasing Peptide; Isoelectric Point; Mice; Molecular Weight; Peptides; Receptors, Bombesin; Receptors, Neurotransmitter; Succinimides

1987