Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme

Halina Ostrowska, Cezary Wojcik, Satoshi Omura, Krzysztof Worowski

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

Lactacystin, the most specific inhibitor of the proteasome, strongly inhibited at pH 5.5 the activity of human platelet lysosomal cathepsin A-like enzyme. At a concentration as low as 1-5 μM it almost completely decreased the hydrolysis rate of cathepsin A specific substrates: Cbz-Phe-Ala and FA-Phe-Phe. This inhibition was probably due to the lactacystin intermediate β-lactone formed during 10 min hydrolysis at pH 8.0 since nonhydrolyzed inhibitor did not affect cathepsin A activity. Basing on similarities in the inhibitor sensitivity, pH optimum, and substrate preferences it is suggested that the cathepsin A-like activity may be involved in chymotrypsin-like activity of the proteasome.

Original languageEnglish (US)
Pages (from-to)729-732
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume234
Issue number3
DOIs
StatePublished - May 29 1997
Externally publishedYes

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Cathepsin A
Proteasome Inhibitors
Platelets
Blood Platelets
Enzymes
Hydrolysis
Chymotrypsin
Lactones
Proteasome Endopeptidase Complex
Substrates
Human Activities
lactacystin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. / Ostrowska, Halina; Wojcik, Cezary; Omura, Satoshi; Worowski, Krzysztof.

In: Biochemical and Biophysical Research Communications, Vol. 234, No. 3, 29.05.1997, p. 729-732.

Research output: Contribution to journalArticle

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