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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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EPIDERMAL GROWTH-FACTOR STIMULATES TYROSINE PHOSPHORYLATION OF PHOSPHOLIPASE C-II INDEPENDENTLY OF RECEPTOR INTERNALIZATION AND EXTRACELLULAR CALCIUM

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Title
EPIDERMAL GROWTH-FACTOR STIMULATES TYROSINE PHOSPHORYLATION OF PHOSPHOLIPASE C-II INDEPENDENTLY OF RECEPTOR INTERNALIZATION AND EXTRACELLULAR CALCIUM
Author
Wahl, Matthew I.Nishibe, ShunzoSuh, Pann-GhillRhee, Sue GooCarpenter, Graham
Issue Date
1989-03
Publisher
NATL ACAD SCIENCES
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.86, no.5, pp.1568 - 1572
Abstract
Epidermal growth factor (EGF) rapidly stimulates the formation of inositol 1,4,5-trisphosphate in a variety of cell types. Previously we have found that in intact cells stimulation of phospholipase C (PLC) activity by EGF is correlated with the retention of increased amounts of PLC activity by a phosphotyrosine immunoaffinity matrix, suggesting that the EGF-receptor tyrosine kinase phosphorylates PLC. We now define parameters of the mechanism by which EGF addition to A-431 cells stimulates phosphotyrosine immuno-isolation of PLC activity and demonstrate that EGF addition to A-431 cells increases tyrosine phosphorylation of PLC. EGF rapidly and reversibly stimulated the anti-phosphotyrosine recovery of increased PLC activity when cells were treated with growth factor at 3°C, indicating that receptor internalization is not required and that the phosphorylation event occurs prior to formation of inositol 1,4,5-trisphosphate. Also, the EGF stimulation of anti-phosphotyrosine recovery of PLC activity occurred in the absence of extracellular Ca2+. Stimulation of PLC activity in intact cells by other agonists, such as bradykinin or ATP, did not result in increased anti-phosphotyrosine recovery of PLC activity, suggesting two separate mechanisms exist in A-431 cells for hormone-stimulated formation of inositol phosphates. Finally, using monoclonal antibodies that specifically recognize three distinct PLC isozymes, we show that an ≃145-kDa PLC isozyme (PLC-II) is present in A-431 cells and that EGF treatment of A-431 cells stimulates phosphorylation of PLC-II on both tyrosine and serine residues.
URI
https://scholarworks.unist.ac.kr/handle/201301/16506
URL
http://www.pnas.org/content/86/5/1568
DOI
10.1073/pnas.86.5.1568
ISSN
0027-8424
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