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DC Field | Value | Language |
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dc.citation.endPage | 1572 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 1568 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 86 | - |
dc.contributor.author | Wahl, Matthew I. | - |
dc.contributor.author | Nishibe, Shunzo | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Rhee, Sue Goo | - |
dc.contributor.author | Carpenter, Graham | - |
dc.date.accessioned | 2023-12-22T13:10:15Z | - |
dc.date.available | 2023-12-22T13:10:15Z | - |
dc.date.created | 2015-08-17 | - |
dc.date.issued | 1989-03 | - |
dc.description.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. | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.86, no.5, pp.1568 - 1572 | - |
dc.identifier.doi | 10.1073/pnas.86.5.1568 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-0024507990 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/16506 | - |
dc.identifier.url | http://www.pnas.org/content/86/5/1568 | - |
dc.identifier.wosid | A1989T552200032 | - |
dc.language | 영어 | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | EPIDERMAL GROWTH-FACTOR STIMULATES TYROSINE PHOSPHORYLATION OF PHOSPHOLIPASE C-II INDEPENDENTLY OF RECEPTOR INTERNALIZATION AND EXTRACELLULAR CALCIUM | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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