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 ser16 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.


CONCLUSIONS
Cytoplasmic localization of HSP20 is consistent with a potential function of HSP20 as a regulator of smooth muscle contractile force.
Rembold
C M
CM
Cardiovascular Division, Department of Internal Medicine, University of Virginia, Health System Charlottesville, Virginia 22908, USA. crembold@virginia.edu
Zhang
E
E
D000818:Animals; D002339:Carotid Arteries / Q000737:chemistry*; D003593:Cytoplasm / Q000737:chemistry; D050886:HSP20 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000032:analysis*; D018613:Microscopy, Confocal; D010750:Phosphoproteins / Q000032:analysis*; D013552:Swine
D050886:HSP20 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D010750:Phosphoproteins