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Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein
Fertilization of the sea urchin egg results in the phosphorylation, on tyrosine, of a high molecular weight protein localized in the egg cortex. In the present study, treatment of unfertilized eggs with the phorbol ester 12-O-tetradecanoylphorbol 13-acetate stimulated tyrosine phosphorylation of the...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1990
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116097/ https://www.ncbi.nlm.nih.gov/pubmed/2157715 |
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collection | PubMed |
description | Fertilization of the sea urchin egg results in the phosphorylation, on tyrosine, of a high molecular weight protein localized in the egg cortex. In the present study, treatment of unfertilized eggs with the phorbol ester 12-O-tetradecanoylphorbol 13-acetate stimulated tyrosine phosphorylation of the high molecular weight cortical protein to levels three- to fivefold higher than that occurring in response to fertilization. Experiments using agents that inhibit the egg Na+/H+ exchange system or mimic the fertilization-induced shift in cytoplasmic pHi, suggest a signal transduction pathway in which protein kinase C activates the egg Na+/H+ exchange system and the resultant cytoplasmic pHi shift promotes tyrosine phosphorylation of the high molecular weight cortical protein. |
format | Text |
id | pubmed-2116097 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21160972008-05-01 Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein J Cell Biol Articles Fertilization of the sea urchin egg results in the phosphorylation, on tyrosine, of a high molecular weight protein localized in the egg cortex. In the present study, treatment of unfertilized eggs with the phorbol ester 12-O-tetradecanoylphorbol 13-acetate stimulated tyrosine phosphorylation of the high molecular weight cortical protein to levels three- to fivefold higher than that occurring in response to fertilization. Experiments using agents that inhibit the egg Na+/H+ exchange system or mimic the fertilization-induced shift in cytoplasmic pHi, suggest a signal transduction pathway in which protein kinase C activates the egg Na+/H+ exchange system and the resultant cytoplasmic pHi shift promotes tyrosine phosphorylation of the high molecular weight cortical protein. The Rockefeller University Press 1990-04-01 /pmc/articles/PMC2116097/ /pubmed/2157715 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
title | Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
title_full | Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
title_fullStr | Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
title_full_unstemmed | Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
title_short | Phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
title_sort | phorbol ester treatment stimulates tyrosine phosphorylation of a sea urchin egg cortex protein |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116097/ https://www.ncbi.nlm.nih.gov/pubmed/2157715 |