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Evidence for participation of a calpain-like cysteine protease in cell cycle progression through late G1 phase

Biochem Biophys Res Commun. 1997 Jul 30;236(3):555-8. doi: 10.1006/bbrc.1997.7003.

Abstract

Recent studies have demonstrated that cell-permeant protease inhibitors arrest human fibroblasts in late G1. The target for the inhibitors has been claimed to be either the proteasome, or a calpain-like cysteine protease activity. In the present investigation, the progression of serum-stimulated WI-38 fibroblasts into S-phase was partially inhibited by the cell-permeant general inhibitor of cysteine proteases, E64d, but not by its non-permeant anolog, E64c. Exposure of fibroblasts in late G1 to the proteasome inhibitor, lactacystin, produced only a modest inhibition of progression into S-phase, and did not influence the extensive inhibition produced by the calpain-selective inhibitor, ZLLY-DMK. ZLLnV-CHO and ZLLL-CHO, which are reportedly selective for the proteasome, were less potent than ZLLY-DMK as inhibitors of S-phase progression. These results argue for the involvement of a calpain-like protease acting in late G1 to allow transit into S-phase.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylcysteine / analogs & derivatives
  • Acetylcysteine / pharmacology
  • Calpain / antagonists & inhibitors
  • Calpain / metabolism*
  • Cell Cycle / physiology*
  • Cell Line
  • Cysteine Proteinase Inhibitors / pharmacology*
  • Diazomethane / analogs & derivatives
  • Diazomethane / pharmacology
  • Fibroblasts
  • G1 Phase / drug effects
  • G1 Phase / physiology*
  • Humans
  • Leupeptins / pharmacology
  • Oligopeptides / pharmacology
  • S Phase / drug effects

Substances

  • Cysteine Proteinase Inhibitors
  • Leupeptins
  • Oligopeptides
  • benzyloxycarbonylleucyl-leucyl-tyrosine diazomethyl ketone
  • lactacystin
  • Diazomethane
  • Calpain
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde
  • Acetylcysteine