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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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Detalles Bibliográficos
Autores principales: Rembold, Christopher M, Zhang, Erik
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2001
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48151/
https://www.ncbi.nlm.nih.gov/pubmed/11532202
Descripción
Sumario: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.