The presence of a 33-40 KDa gastrin binding protein on human and mouse colon cancer

Louis Chicone, Satya Narayan, Courtney Townsend, Pomila Singh

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Human and mouse colon cancers have specific binding sites for gastrin and demonstrate a trophic response to gastrin. In the present study we used radiolabeled gastrin (2-17), to determine the molecular weight of gastrin binding proteins (receptors) on mouse and human colon cancers, by cross-linking methods. Crude membrane aliquots prepared from the tumors were radiolabeled with [125I]gastrin (2-17) ± 1000 fold excess of unlabeled gastrin and cross-linked with 1 mM disuccinimidyl suberate. The cross-linked radiolabeled binding protein complexes were solubilized and subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis. The autoradiographs of the gels demonstrated the presence of a predominant band of ∼33-40 KDa gastrin binding protein, that was specific for gastrin analogs. Our present findings thus indicate that specific gastrin binding proteins/gastrin receptors on colon cancers are primarily present as one band with a molecular mass of ∼33-40 KDa and are specific for gastrin-like peptides.

Original languageEnglish (US)
Pages (from-to)512-519
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume164
Issue number1
DOIs
StatePublished - Oct 16 1989

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Gastrins
Colonic Neoplasms
Carrier Proteins
Cholecystokinin B Receptor
Sodium Dodecyl Sulfate
Molecular mass
Polyacrylamide Gel Electrophoresis
Electrophoresis
Molecular Weight
Gels
Binding Sites
Tumors
Peptides
Molecular weight
Membranes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The presence of a 33-40 KDa gastrin binding protein on human and mouse colon cancer. / Chicone, Louis; Narayan, Satya; Townsend, Courtney; Singh, Pomila.

In: Biochemical and Biophysical Research Communications, Vol. 164, No. 1, 16.10.1989, p. 512-519.

Research output: Contribution to journalArticle

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N2 - Human and mouse colon cancers have specific binding sites for gastrin and demonstrate a trophic response to gastrin. In the present study we used radiolabeled gastrin (2-17), to determine the molecular weight of gastrin binding proteins (receptors) on mouse and human colon cancers, by cross-linking methods. Crude membrane aliquots prepared from the tumors were radiolabeled with [125I]gastrin (2-17) ± 1000 fold excess of unlabeled gastrin and cross-linked with 1 mM disuccinimidyl suberate. The cross-linked radiolabeled binding protein complexes were solubilized and subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis. The autoradiographs of the gels demonstrated the presence of a predominant band of ∼33-40 KDa gastrin binding protein, that was specific for gastrin analogs. Our present findings thus indicate that specific gastrin binding proteins/gastrin receptors on colon cancers are primarily present as one band with a molecular mass of ∼33-40 KDa and are specific for gastrin-like peptides.

AB - Human and mouse colon cancers have specific binding sites for gastrin and demonstrate a trophic response to gastrin. In the present study we used radiolabeled gastrin (2-17), to determine the molecular weight of gastrin binding proteins (receptors) on mouse and human colon cancers, by cross-linking methods. Crude membrane aliquots prepared from the tumors were radiolabeled with [125I]gastrin (2-17) ± 1000 fold excess of unlabeled gastrin and cross-linked with 1 mM disuccinimidyl suberate. The cross-linked radiolabeled binding protein complexes were solubilized and subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis. The autoradiographs of the gels demonstrated the presence of a predominant band of ∼33-40 KDa gastrin binding protein, that was specific for gastrin analogs. Our present findings thus indicate that specific gastrin binding proteins/gastrin receptors on colon cancers are primarily present as one band with a molecular mass of ∼33-40 KDa and are specific for gastrin-like peptides.

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