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Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets

Exposure to low temperature causes platelets to change shape in a manner similar to the shape change that precedes secretagogue-induced serotonin release. Previous studies have shown that two proteins, of approximately 20,000 and approximately 40,000 Mr, become phosphorylated before secretion. We ha...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1980
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110668/
https://www.ncbi.nlm.nih.gov/pubmed/7419577
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description Exposure to low temperature causes platelets to change shape in a manner similar to the shape change that precedes secretagogue-induced serotonin release. Previous studies have shown that two proteins, of approximately 20,000 and approximately 40,000 Mr, become phosphorylated before secretion. We have investigated whether low temperature can induce phosphorylation of these proteins and/or serotonin secretion. The data indicate that low-temperature-induced shape change has no requirement for extracellular calcium, whereas phosphorylation of the two proteins and subsequent serotonin release both have strong calcium requirements. Because cold treatment is thought to influence platelet shape through an effect on microtubules, the events in the shape change- release sequence would seem to be ordered as follows: microtubule disassembly leads to shape change leads to protein phosphorylation leads to secretion.
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spelling pubmed-21106682008-05-01 Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets J Cell Biol Articles Exposure to low temperature causes platelets to change shape in a manner similar to the shape change that precedes secretagogue-induced serotonin release. Previous studies have shown that two proteins, of approximately 20,000 and approximately 40,000 Mr, become phosphorylated before secretion. We have investigated whether low temperature can induce phosphorylation of these proteins and/or serotonin secretion. The data indicate that low-temperature-induced shape change has no requirement for extracellular calcium, whereas phosphorylation of the two proteins and subsequent serotonin release both have strong calcium requirements. Because cold treatment is thought to influence platelet shape through an effect on microtubules, the events in the shape change- release sequence would seem to be ordered as follows: microtubule disassembly leads to shape change leads to protein phosphorylation leads to secretion. The Rockefeller University Press 1980-07-01 /pmc/articles/PMC2110668/ /pubmed/7419577 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
Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
title Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
title_full Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
title_fullStr Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
title_full_unstemmed Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
title_short Low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
title_sort low-temperature induction of calcium-dependent protein phosphorylation in blood platelets
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110668/
https://www.ncbi.nlm.nih.gov/pubmed/7419577