SJA6017, a newly synthesized peptide aldehyde inhibitor of calpain: Amelioration of cataract in cultured rat lenses

Chiho Fukiage, Mitsuyoshi Azuma, Yoshikuni Nakamura, Yoshiyuki Tamada, Masayuki Nakamura, Thomas R. Shearer

Research output: Contribution to journalArticle

70 Scopus citations


The purposes of this experiment were to: (1), characterize the peptide aldehyde SJA6017, N-(4-fluorophenylsulfonyl)-L-valyl-L-leucinal, a newly synthesized inhibitor of calpain, and (2) test the effect of SJA6017 in preventing calcium ionophore-induced cataract in cultured rat lenses. In vitro, SJA6017 strongly inhibited purified m-calpain from porcine kidney. Casein zymography confirmed that SJA6017 reversibly bound to the active site of m-calpain. SJA6017 was also confirmed to be a cell-permeable inhibitor in Molt-4 cells. In cultured lenses, SJA6017 reduced nuclear opacity and proteolysis of crystallins and α-spectrin caused by calcium ionophore A23187. These results suggested that SJA6017 is a reversible and cell-permeable calpain inhibitor which may possess great efficacy against calcium-induced models of cataract.

Original languageEnglish (US)
Pages (from-to)304-312
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Issue number3
StatePublished - Oct 24 1997



  • Calcium ionophore A23187
  • Calpain
  • Cataract
  • Proteolysis
  • SJA6017

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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