Biochemical characterization of the pancreatic cholecystokinin receptor: A possible marker of cell differentiation and development

Laurence J Miller, S. P. Powers

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The biochemical expression of the cholecystokinin (CCK) receptor on the surface of the pancreatic acinar cell is a potential marker of the state of differentiation of that cell. In this report we review the basis for and the results of the use of affinity labeling techniques for the biochemical characterization of this macromolecular receptor assembly on the adult rat pancreatic acinar cell. A series of specially designed molecular probes are used to define the subunit structure of this receptor, based on the relationships between the sites of covalent attachment of these probes and their receptor-binding domains. We suggest that the receptor-binding domain resides on a Mr = 85.000-95.000 subunit. whereas a distinct Mr = 80.000 also exists as part of this complex.

Original languageEnglish (US)
Pages (from-to)104-107
Number of pages4
JournalScandinavian Journal of Gastroenterology
Volume23
Issue numberS151
DOIs
StatePublished - 1988

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Cholecystokinin A Receptor
Acinar Cells
Cell Differentiation
Cholecystokinin Receptors
Molecular Probes
Differentiation Antigens

Keywords

  • Affinity labeling
  • Cholecystokinin receptor
  • Differentiation

ASJC Scopus subject areas

  • Gastroenterology

Cite this

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AB - The biochemical expression of the cholecystokinin (CCK) receptor on the surface of the pancreatic acinar cell is a potential marker of the state of differentiation of that cell. In this report we review the basis for and the results of the use of affinity labeling techniques for the biochemical characterization of this macromolecular receptor assembly on the adult rat pancreatic acinar cell. A series of specially designed molecular probes are used to define the subunit structure of this receptor, based on the relationships between the sites of covalent attachment of these probes and their receptor-binding domains. We suggest that the receptor-binding domain resides on a Mr = 85.000-95.000 subunit. whereas a distinct Mr = 80.000 also exists as part of this complex.

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