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Results: 421 to 424 of 424

Publication Record


The melanoma growth stimulatory activity receptor consists of two proteins. Ligand binding results in enhanced tyrosine phosphorylation.
Cheng QC, Han JH, Thomas HG, Balentien E, Richmond A
(1992) J Immunol 148: 451-6
MeSH Terms: Binding, Competitive, Calcium, Carrier Proteins, Chemokine CXCL1, Chemokines, CXC, ErbB Receptors, Growth Substances, Humans, Intercellular Signaling Peptides and Proteins, Interleukin-8, Membrane Proteins, Molecular Weight, Neoplasm Proteins, Phosphorylation, Placenta, Receptors, Immunologic, Receptors, Interleukin-8A, Signal Transduction, Tyrosine
Show Abstract · Added May 30, 2013
The human melanoma growth-stimulatory activities (MGSA alpha, beta, gamma/GRO) are products of immediate early genes coding for cytokines that exhibit sequence similarity to platelet factor-4 and beta-thromboglobulin. MGSA/GRO alpha has been demonstrated to partially complete for binding to the approximately 58-kDa neutrophil receptor for another beta-thromboglobulin-related chemotactic protein, IL-8. We demonstrate that when [125I]MGSA/GRO alpha was cross-linked to receptors/binding proteins from human placenta, there were two major [125I]MGSA cross-linked bands of approximately 64,000 and approximately 84,000 Mr. Because [125I]MGSA exists primarily in monomer and dimer forms at the concentrations used here, it is not clear whether the receptor/binding proteins represented by the cross-linked bands are approximately 50,000 and approximately 70,000 or approximately 58,000 and approximately 78,000 Mr. Ligand binding to the receptor proteins is associated with enhanced tyrosine phosphorylation of a number of substrates, including proteins in the same Mr range as the MGSA/GRO receptor/binding proteins.
2 Communities
1 Members
0 Resources
19 MeSH Terms
Tyrosine phosphorylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen-transformed cells.
Kanner SB, Reynolds AB, Parsons JT
(1991) Mol Cell Biol 11: 713-20
MeSH Terms: Animals, Antigens, Polyomavirus Transforming, Cell Line, Cell Transformation, Neoplastic, Chick Embryo, ErbB Receptors, Humans, Kinetics, Molecular Weight, Moloney murine leukemia virus, Myristic Acid, Myristic Acids, Palmitic Acid, Palmitic Acids, Phosphates, Phosphorylation, Platelet-Derived Growth Factor, Proto-Oncogene Proteins pp60(c-src), Receptors, Cell Surface, Receptors, Platelet-Derived Growth Factor, Tyrosine
Show Abstract · Added March 5, 2014
The monoclonal antibody 2B12 is directed toward p120, a 120-kDa cellular protein originally identified as a protein tyrosine kinase substrate in cells expressing membrane-associated oncogenic variants of pp60src. In this report, we show that p120 was tyrosine phosphorylated in avian cells expressing membrane-associated, enzymatically activated variants of c-src, including variants having structural alterations in the src homology regions 2 and 3. In contrast, p120 was not tyrosine phosphorylated in cells expressing enzymatically activated, nonmyristylated pp60src. Furthermore, p120 was tyrosine phosphorylated in avian cells expressing middle T antigen, the transforming protein of polyomavirus, as well as in rodent cells stimulated with either epidermal growth factor (EGF) or platelet-derived growth factor. Analysis of the time course of p120 tyrosine phosphorylation in EGF-stimulated cells revealed a rapid onset of tyrosine phosphorylation. In addition, both the extent and duration of p120 phosphorylation increased when cells overexpressing the EGF receptor were stimulated with EGF. Biochemical analysis showed that p120 (in both normal and src-transformed cells) was membrane associated, was myristylated, and was phosphorylated on serine and threonine residues. Hence, p120 appears to be a substrate of both nonreceptor- and ligand-activated transmembrane receptor tyrosine kinases and of serine/threonine kinases and is perhaps a component of both mitogen-stimulated and tyrosine kinase oncogene-induced signaling pathways.
1 Communities
1 Members
0 Resources
21 MeSH Terms
Elevated content of the tyrosine kinase substrate phospholipase C-gamma 1 in primary human breast carcinomas.
Arteaga CL, Johnson MD, Todderud G, Coffey RJ, Carpenter G, Page DL
(1991) Proc Natl Acad Sci U S A 88: 10435-9
MeSH Terms: Amino Acid Sequence, Biomarkers, Tumor, Breast, Breast Neoplasms, Carcinoma, ErbB Receptors, Female, Fibrocystic Breast Disease, Humans, Immune Sera, Immunoblotting, Immunohistochemistry, Isoenzymes, Molecular Sequence Data, Peptides, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Receptor, ErbB-2, Reference Values, Substrate Specificity, Type C Phospholipases
Show Abstract · Added March 5, 2014
Phospholipase C-gamma 1 (PLC-gamma 1) is a substrate for several receptor tyrosine kinases and its catalytic activity is increased by tyrosine phosphorylation. However, the biological significance of this molecule in normal or malignant human epithelial cell proliferation is unknown. We determined the relative content of PLC-gamma 1 in primary human mammary carcinomas and in nonmalignant mammary tissues. By Western blot and immunohistochemistry, considerably higher levels of PLC-gamma 1 protein were detectable in the majority of carcinomas and in one of two benign fibroadenomas compared to normal breast tissues. In 18 of 21 carcinomas that contained high levels of PLC-gamma 1, the presence of phosphotyrosine on PLC-gamma 1 could also be detected. All carcinomas in which tyrosine phosphorylated PLC-gamma 1 was present also expressed detectable levels of the epidermal growth factor receptor or erbB-2, two tyrosine kinases known to phosphorylate this enzyme. Thus, a high percentage of mammary carcinomas concomitantly display increased levels of receptor tyrosine kinases and a direct tyrosine phosphorylation substrate, thereby potentially amplifying two successive steps in a signal transduction pathway.
1 Communities
2 Members
0 Resources
21 MeSH Terms
Epidermal growth factor receptor monoclonal antibody inhibits constitutive receptor phosphorylation, reduces autonomous growth, and sensitizes androgen-independent prostatic carcinoma cells to tumor necrosis factor alpha.
Fong CJ, Sherwood ER, Mendelsohn J, Lee C, Kozlowski JM
(1992) Cancer Res 52: 5887-92
MeSH Terms: Antibodies, Monoclonal, Cell Division, Electrophoresis, Polyacrylamide Gel, Epidermal Growth Factor, ErbB Receptors, Humans, Male, Phosphorylation, Prostatic Neoplasms, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha
Show Abstract · Added October 18, 2015
Results of recent studies indicate that cultured, androgen-independent prostatic carcinoma cells synthesize and secrete transforming growth factor alpha, which interacts with epidermal growth factor receptors (EGFRs) to promote autonomous growth. In the present study, we evaluated the expression and constitutive activation of EGFRs in normal prostatic epithelial cells and the androgen-independent prostatic carcinoma cell lines PC3 and DU145. Our studies showed that cultured normal epithelial cells and androgen-independent prostatic carcinoma cells actively synthesize and exhibit constitutive phosphorylation of the M(r) 170,000 EGFR. The addition of monoclonal anti-EGFR reduced receptor phosphorylation and significantly inhibited the proliferation of prostatic tumor cells. The observed reduction in EGFR phosphorylation could be partially attributed to an antibody-induced decrease in the expression of metabolically labeled EGFR. Results of further studies showed that anti-EGFR enhanced the sensitivity of PC3 cells to the cytotoxic and cytostatic effects of tumor necrosis factor alpha. These studies demonstrate that constitutive activation of EGFR in androgen-independent prostatic carcinoma plays a functional role in the regulation of cellular proliferation in vitro. In addition, the enhanced sensitivity of prostatic carcinoma cells to tumor necrosis factor alpha in the presence of anti-EGFR provides a rationale for the further investigation of combination therapy in the treatment of disseminated, androgen-independent disease.
0 Communities
1 Members
0 Resources
11 MeSH Terms