BIOMAT Database Logo BIOMAT Database Logo

Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor. 1990

B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Rorer Biotechnology, Inc., King of Prussia, Pennsylvania 19406.

Epidermal growth factor (EGF) treatment of NIH 3T3 cells transfected with wild-type EGF receptor induced tyrosine phosphorylation of phospholipase C-gamma (PLC-gamma). The EGF receptor and PLC-gamma were found to be physically associated such that antibodies directed against PLC-gamma or the EGF receptor coimmunoprecipitated both proteins. The association between PLC-gamma and wild-type EGF receptor was dependent on the concentration of EGF, but EGF did not enhance the association between PLC-gamma and a kinase-negative mutant of the EGF receptor. Oligomerization of the EGF receptor was not sufficient to induce association of the EGF receptor with PLC-gamma, since the kinase-negative mutant receptor underwent normal dimerization in response to EGF yet did not associate with PLC-gamma. The form of PLC-gamma associated with the EGF receptor appeared to be primarily the non-tyrosine-phosphorylated form. It is concluded that the kinase activity of the EGF receptor is essential for association of PLC-gamma with the EGF receptor, possibly by stimulating receptor autophosphorylation.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008815 Mice, Inbred Strains Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations, or by parent x offspring matings carried out with certain restrictions. All animals within an inbred strain trace back to a common ancestor in the twentieth generation. Inbred Mouse Strains,Inbred Strain of Mice,Inbred Strain of Mouse,Inbred Strains of Mice,Mouse, Inbred Strain,Inbred Mouse Strain,Mouse Inbred Strain,Mouse Inbred Strains,Mouse Strain, Inbred,Mouse Strains, Inbred,Strain, Inbred Mouse,Strains, Inbred Mouse
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D010738 Type C Phospholipases A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS. Lecithinase C,Phospholipase C,Phospholipases, Type C,Phospholipases C
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011505 Protein-Tyrosine Kinases Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors. Tyrosine Protein Kinase,Tyrosine-Specific Protein Kinase,Protein-Tyrosine Kinase,Tyrosine Kinase,Tyrosine Protein Kinases,Tyrosine-Specific Protein Kinases,Tyrosylprotein Kinase,Kinase, Protein-Tyrosine,Kinase, Tyrosine,Kinase, Tyrosine Protein,Kinase, Tyrosine-Specific Protein,Kinase, Tyrosylprotein,Kinases, Protein-Tyrosine,Kinases, Tyrosine Protein,Kinases, Tyrosine-Specific Protein,Protein Kinase, Tyrosine-Specific,Protein Kinases, Tyrosine,Protein Kinases, Tyrosine-Specific,Protein Tyrosine Kinase,Protein Tyrosine Kinases,Tyrosine Specific Protein Kinase,Tyrosine Specific Protein Kinases
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D004815 Epidermal Growth Factor A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form. EGF,Epidermal Growth Factor-Urogastrone,Urogastrone,Human Urinary Gastric Inhibitor,beta-Urogastrone,Growth Factor, Epidermal,Growth Factor-Urogastrone, Epidermal,beta Urogastrone
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
The tyrosine kinase activity of the epidermal-growth-factor receptor is necessary for phospholipase A2 activation.
April 1990, The Biochemical journal,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
The epidermal growth factor receptor is associated with phospholipase C-gamma 1 in meningiomas.
February 1994, Human pathology,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.
February 1984, The Journal of biological chemistry,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro.
March 1990, The Journal of biological chemistry,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Interaction of phospholipase C-gamma with activated growth factor receptor tyrosine kinases.
January 1997, Advances in experimental medicine and biology,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Protein kinase C inhibits epidermal growth factor-dependent tyrosine phosphorylation of phospholipase C gamma and activation of phosphoinositide hydrolysis.
October 1990, Endocrinology,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Suppression of protein tyrosine kinase activity of the epidermal growth factor receptor by epidermal growth factor.
June 1986, The Journal of biological chemistry,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Stimulation of phospholipase C-gamma 1 membrane association by epidermal growth factor.
July 1990, Science (New York, N.Y.),
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling.
May 2003, The Journal of biological chemistry,
B Margolis, and F Bellot, and A M Honegger, and A Ullrich, and J Schlessinger, and A Zilberstein
Epidermal growth factor receptor tyrosine kinase inhibitors.
June 2004, British journal of cancer,
Copied contents to your clipboard!