Selective inhibition of protein kinase C beta(2) attenuates inducible nitric oxide synthase-mediated cardiovascular abnormalities in streptozotocin-induced diabetic rats

Diabetes. 2009 Oct;58(10):2355-64. doi: 10.2337/db09-0432. Epub 2009 Jul 8.

Abstract

Objective: Impaired cardiovascular function in diabetes is partially attributed to pathological overexpression of inducible nitric oxide synthase (iNOS) in cardiovascular tissues. We examined whether the hyperglycemia-induced increased expression of iNOS is protein kinase C-beta(2) (PKCbeta(2)) dependent and whether selective inhibition of PKCbeta reduces iNOS expression and corrects abnormal hemodynamic function in streptozotocin (STZ)-induced diabetic rats.

Research design and methods: Cardiomyocytes and aortic vascular smooth muscle cells (VSMC) from nondiabetic rats were cultured in low (5.5 mmol/l) or high (25 mmol/l) glucose or mannitol (19.5 mmol/l mannitol + 5.5 mmol/l glucose) conditions in the presence of a selective PKCbeta inhibitor, LY333531 (20 nmol/l). Further, the in vivo effects of PKCbeta inhibition on iNOS-mediated cardiovascular abnormalities were tested in STZ-induced diabetic rats.

Results: Exposure of cardiomyocytes to high glucose activated PKCbeta(2) and increased iNOS expression that was prevented by LY333531. Similarly, treatment of VSMC with LY333531 prevented high glucose-induced activation of nuclear factor kappaB, extracellular signal-related kinase, and iNOS overexpression. Suppression of PKCbeta(2) expression by small interference RNA decreased high-glucose-induced nuclear factor kappaB and extracellular signal-related kinase activation and iNOS expression in VSMC. Administration of LY333531 (1 mg/kg/day) decreased iNOS expression and formation of peroxynitrite in the heart and superior mesenteric arteries and corrected the cardiovascular abnormalities in STZ-induced diabetic rats, an action that was also observed with a selective iNOS inhibitor, L-NIL.

Conclusions: Collectively, these results suggest that inhibition of PKCbeta(2) may be a useful approach for correcting abnormal hemodynamics in diabetes by preventing iNOS mediated nitrosative stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aorta / enzymology
  • Blood Glucose / metabolism
  • Cardiovascular Diseases / prevention & control*
  • Cells, Cultured
  • Diabetes Mellitus, Experimental / enzymology*
  • Diabetic Angiopathies / prevention & control*
  • Enzyme Induction
  • Enzyme Inhibitors / pharmacology*
  • Glucose / pharmacology
  • Indoles / pharmacology*
  • Lysine / analogs & derivatives
  • Lysine / pharmacology
  • Male
  • Maleimides / pharmacology*
  • Mannitol / pharmacology
  • Muscle, Smooth, Vascular / enzymology
  • Myocytes, Cardiac / cytology
  • Myocytes, Cardiac / enzymology*
  • Nitric Oxide Synthase Type II / antagonists & inhibitors
  • Nitric Oxide Synthase Type II / biosynthesis
  • Nitric Oxide Synthase Type II / metabolism*
  • Protein Kinase C / antagonists & inhibitors*
  • Protein Kinase C beta
  • Rats
  • Rats, Wistar

Substances

  • Blood Glucose
  • Enzyme Inhibitors
  • Indoles
  • Maleimides
  • N(6)-(1-iminoethyl)lysine
  • Mannitol
  • ruboxistaurin
  • Nitric Oxide Synthase Type II
  • Protein Kinase C
  • Protein Kinase C beta
  • Glucose
  • Lysine