Endothelial-dependent vasodilation is associated with increases in the phosphorylation of a small heat shock protein (HSP20)

J Vasc Surg. 1999 Apr;29(4):678-84. doi: 10.1016/s0741-5214(99)70314-9.

Abstract

Purpose: Increases in the phosphorylation of a small heat shock protein (HSP20) are associated with cyclic nucleotide-dependent vasorelaxation. The effect of pressure and flow on vessel diameter was studied. We hypothesized that physiologic conditions that induce vasorelaxation would lead to increases in HSP20 phosphorylation.

Methods: Flow-dependent changes in vessel diameter, at different intraluminal pressures, were measured with a laser optical micrometer in intact bovine carotid arteries. Experiments were performed in the presence and absence of norepinephrine (10(-5) mol/L). Increases in the phosphorylation of HSP20 were determined with isoelectric focusing immunoblots.

Results: The increase in vessel diameter was most significant at low intraluminal pressures (20 mm Hg), high flow rates (200 mL/min), and in the presence of the vasoconstrictor norepinephrine (10(-5) mol/L). The addition of methylene blue (a guanylate cyclase inhibitor) completely inhibited flow-induced vasodilation. Under conditions in which maximal flow induced vasodilation occurred, there were significant increases in the phosphorylation of HSP20.

Conclusion: Flow-dependent vasodilation in isolated perfused segments of bovine carotid arteries was maximal when the intraluminal pressures were low and when the vessels were precontracted with norepinephrine. Flow-dependent vasodilation was inhibited by methylene blue and was associated with increases in the phosphorylation of HSP20, suggesting that the vasodilation was mediated by endothelial production of nitric oxide.

MeSH terms

  • Animals
  • Carotid Arteries / physiology
  • Cattle
  • Endothelium, Vascular / physiology*
  • HSP20 Heat-Shock Proteins
  • Heat-Shock Proteins / metabolism*
  • In Vitro Techniques
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Vasodilation / physiology*

Substances

  • HSP20 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Phosphoproteins