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Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells.

Publication ,  Journal Article
Khurana, RN; Maddala, RL; Shimokawa, H; Samuel Zigler, J; Epstein, DL; Vasantha Rao, P
Published in: Biochem Biophys Res Commun
June 28, 2002

The small heat shock protein, alphaB-crystallin, has been shown to interact with actin and intermediate filament proteins. However, little is known regarding the cellular mechanisms regulating such interactions. In this study, we explored the role of the Rho/Rho-kinase pathway in alphaB-crystallin distribution and expression in porcine lens epithelial cells. alphaB-crystallin was distributed uniformly throughout the cytoplasm and did not exhibit any unique redistribution in response to actin depolymerization induced by Rho/Rho-kinase inhibitors (C3-exoenzyme or Y-27632) or by overexpression of the dominant negative mutant of Rho-kinase (DNRK) in porcine lens epithelial cells. Interestingly, alphaB-crystallin levels markedly increased in lens epithelial cells treated with the inhibitors of Rho/Rho-kinase proteins (lovastatin, Y-27632 or DNRK) while a protein kinase C inhibitor (GF109203x) was found to have no effect. Further, Y-27632 showed a dose (2-50 microM) response effect on alphaB-crystallin induction. Nocodazole, a microtubule-depolymerizing agent, elicited an increase in alphaB-crystallin levels but latrunculin, an actin depolymerizing agent, did not show any significant effect. Pretreatment with cycloheximide or genistein blocked the Rho-kinase inhibitor-induced increase in alphaB-crystallin protein levels. Rho-kinase inhibitor-induced increases in alphaB-crystallin levels were found to be associated with activation of P38 mitogen-activated protein kinase (MAPK). These results suggest that Rho/Rho-kinase negatively regulates alphaB-crystallin expression, and this response appears to be dependent on tyrosine-protein kinase and P38 MAPK function. Finally, alphaB-crystallin induction appears to be better correlated with the direct inhibition of Rho/Rho-kinase than with actin depolymerization per se.

Duke Scholars

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

June 28, 2002

Volume

294

Issue

5

Start / End Page

981 / 987

Location

United States

Related Subject Headings

  • rho-Associated Kinases
  • rho GTP-Binding Proteins
  • p38 Mitogen-Activated Protein Kinases
  • Swine
  • Stress Fibers
  • Pyridines
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Mutation
  • Mitogen-Activated Protein Kinases
 

Citation

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Khurana, R. N., Maddala, R. L., Shimokawa, H., Samuel Zigler, J., Epstein, D. L., & Vasantha Rao, P. (2002). Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells. Biochem Biophys Res Commun, 294(5), 981–987. https://doi.org/10.1016/S0006-291X(02)00583-1
Khurana, Rahul N., Rupa Latha Maddala, Hiroaki Shimokawa, J. Samuel Zigler, David L. Epstein, and P. Vasantha Rao. “Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells.Biochem Biophys Res Commun 294, no. 5 (June 28, 2002): 981–87. https://doi.org/10.1016/S0006-291X(02)00583-1.
Khurana RN, Maddala RL, Shimokawa H, Samuel Zigler J, Epstein DL, Vasantha Rao P. Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells. Biochem Biophys Res Commun. 2002 Jun 28;294(5):981–7.
Khurana, Rahul N., et al. “Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells.Biochem Biophys Res Commun, vol. 294, no. 5, June 2002, pp. 981–87. Pubmed, doi:10.1016/S0006-291X(02)00583-1.
Khurana RN, Maddala RL, Shimokawa H, Samuel Zigler J, Epstein DL, Vasantha Rao P. Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells. Biochem Biophys Res Commun. 2002 Jun 28;294(5):981–987.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

June 28, 2002

Volume

294

Issue

5

Start / End Page

981 / 987

Location

United States

Related Subject Headings

  • rho-Associated Kinases
  • rho GTP-Binding Proteins
  • p38 Mitogen-Activated Protein Kinases
  • Swine
  • Stress Fibers
  • Pyridines
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Mutation
  • Mitogen-Activated Protein Kinases