Activation of the protein-tyrosine kinase associated with the bombesin receptor complex in small cell lung carcinomas
Journal Article
·
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
- Univ. of Torino Medical School, Turin (Italy)
It has been hypothesized that bombesin-like peptides produced by small cell lung carcinomas may sustain deregulated proliferation through an autocrine mechanism. The authors have shown that the neuropeptide bombesin leads to the activation of a protein-tyrosine kinase that phosphorylates a 115-kDa protein (p115) associated with the bombesin receptor complex in mouse Swiss 3T3 fibroblasts. They now report that phosphotyrosine antibodies recognize a 115-kDa protein, phosphorylated on tyrosine, in four human small cell lung carcinoma cell lines producing bombesin but not in a nonproducer variant line. p115 from detergent-treated small cell lung carcinoma cells binds to bombesin-Sepharose and can be phosphorylated on tyrosine in the presence of radiolabeled ATP and Mn{sup 2+}. As for the p115 immunoprecipitated from mouse fibroblast, the small cell lung carcinoma p115 can be phosphorylated in an immunocomplex kinase assay. However, the latter does not require the presence of exogenous bombesin for activity. Binding data, obtained by using radiolabeled ligand, suggest receptor occupancy in the cell lines producing bombesin. These observations are consistent with the hypothesis that proliferation in some human small cell lung carcinoma lines is under autocrine control, regulated through activation of bombesin receptors.
- OSTI ID:
- 6827907
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 85:7; ISSN PNASA; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550301* -- Cytology-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMAL CELLS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CARCINOMAS
CELL PROLIFERATION
CHEMICAL REACTIONS
CONNECTIVE TISSUE CELLS
CROSS-LINKING
DAYS LIVING RADIOISOTOPES
DISEASES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
ENZYME INDUCTION
ENZYMES
EVEN-ODD NUCLEI
FIBROBLASTS
GENE REGULATION
GROWTH FACTORS
HYDROXY ACIDS
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPES
LABELLED COMPOUNDS
LIGANDS
LIGHT NUCLEI
LIPOTROPIC FACTORS
MEMBRANE PROTEINS
METHIONINE
MITOGENS
NEOPLASMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PATIENTS
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
POLYMERIZATION
PROTEINS
RADIOISOTOPES
RECEPTORS
SOMATIC CELLS
SULFUR 35
SULFUR ISOTOPES
TRANSFERASES
TUMOR CELLS
TYROSINE
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMAL CELLS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CARCINOMAS
CELL PROLIFERATION
CHEMICAL REACTIONS
CONNECTIVE TISSUE CELLS
CROSS-LINKING
DAYS LIVING RADIOISOTOPES
DISEASES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
ENZYME INDUCTION
ENZYMES
EVEN-ODD NUCLEI
FIBROBLASTS
GENE REGULATION
GROWTH FACTORS
HYDROXY ACIDS
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPES
LABELLED COMPOUNDS
LIGANDS
LIGHT NUCLEI
LIPOTROPIC FACTORS
MEMBRANE PROTEINS
METHIONINE
MITOGENS
NEOPLASMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PATIENTS
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
POLYMERIZATION
PROTEINS
RADIOISOTOPES
RECEPTORS
SOMATIC CELLS
SULFUR 35
SULFUR ISOTOPES
TRANSFERASES
TUMOR CELLS
TYROSINE