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Localization of heat shock protein 20 in swine carotid artery
BACKGROUND: Cyclic nucleotides can relax vascular smooth muscle by mechanisms distal to myosin regulatory light chain (MRLC) phosphorylation. This mechanism, termed relaxation without MRLC dephosphorylation, may be regulated by ser(16) phosphorylation of heat shock protein 20 (HSP20). RESULTS: Confo...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2001
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48151/ https://www.ncbi.nlm.nih.gov/pubmed/11532202 |
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author | Rembold, Christopher M Zhang, Erik |
author_facet | Rembold, Christopher M Zhang, Erik |
author_sort | Rembold, Christopher M |
collection | PubMed |
description | BACKGROUND: Cyclic nucleotides can relax vascular smooth muscle by mechanisms distal to myosin regulatory light chain (MRLC) phosphorylation. This mechanism, termed relaxation without MRLC dephosphorylation, may be regulated by ser(16) phosphorylation of heat shock protein 20 (HSP20). RESULTS: Confocal imaging of HSP20 in smooth muscle tissues revealed that HSP20 was present throughout the cytoplasm, although some focal regions of the cytoplasm were found to contain more HSP20 than the remaining cytoplasm. The distribution of HSP20 within the cytoplasm was not altered by histamine, forskolin, or nitroglycerin. CONCLUSION: Cytoplasmic localization of HSP20 is consistent with a potential function of HSP20 as a regulator of smooth muscle contractile force. |
format | Text |
id | pubmed-48151 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2001 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-481512001-09-04 Localization of heat shock protein 20 in swine carotid artery Rembold, Christopher M Zhang, Erik BMC Physiol Research Article BACKGROUND: Cyclic nucleotides can relax vascular smooth muscle by mechanisms distal to myosin regulatory light chain (MRLC) phosphorylation. This mechanism, termed relaxation without MRLC dephosphorylation, may be regulated by ser(16) phosphorylation of heat shock protein 20 (HSP20). RESULTS: Confocal imaging of HSP20 in smooth muscle tissues revealed that HSP20 was present throughout the cytoplasm, although some focal regions of the cytoplasm were found to contain more HSP20 than the remaining cytoplasm. The distribution of HSP20 within the cytoplasm was not altered by histamine, forskolin, or nitroglycerin. CONCLUSION: Cytoplasmic localization of HSP20 is consistent with a potential function of HSP20 as a regulator of smooth muscle contractile force. BioMed Central 2001-08-14 /pmc/articles/PMC48151/ /pubmed/11532202 Text en Copyright © 2001 Rembold and Zhang; licensee BioMed Central Ltd. Verbatim copying and redistribution of this article are permitted in any medium for any non-commercial purpose, provided this notice is preserved along with the article's original URL. For commercial use, contact info@biomedcentral.com |
spellingShingle | Research Article Rembold, Christopher M Zhang, Erik Localization of heat shock protein 20 in swine carotid artery |
title | Localization of heat shock protein 20 in swine carotid artery |
title_full | Localization of heat shock protein 20 in swine carotid artery |
title_fullStr | Localization of heat shock protein 20 in swine carotid artery |
title_full_unstemmed | Localization of heat shock protein 20 in swine carotid artery |
title_short | Localization of heat shock protein 20 in swine carotid artery |
title_sort | localization of heat shock protein 20 in swine carotid artery |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48151/ https://www.ncbi.nlm.nih.gov/pubmed/11532202 |
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