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Biochemistry (Moscow)

, Volume 74, Issue 3, pp 281–287 | Cite as

A secreted caspase-3-substrate-cleaving activity at low pH belongs to cathepsin B: a study on primary brain cell cultures

  • M. V. Onufriev
  • A. A. Yakovlev
  • A. A. Lyzhin
  • M. Yu. Stepanichev
  • L. G. Khaspekov
  • N. V. GulyaevaEmail author
Article

Abstract

The cysteine proteases caspase-3 and cathepsins are involved in both neuronal plasticity and neuropathology. Using primary neuroglial and glial cerebellar cultures, the pH dependence of cleavage of a synthetic caspase-3 substrate, Ac-DEVD-AMC, was studied. At acidic pH, cathepsin B cleaved Ac-DEVD, this activity being significantly higher than that of caspase-3 at pH 7.4. This activity is blocked by peptide inhibitors of both caspase-3 and cathepsin B. Substitution of culture medium for balanced salt solution stimulated cathepsin B secretion in both types of cultures. Ischemia (oxygen-glucose deprivation) significantly decreased secretion of cathepsin B activities into the culture medium.

Key words

cathepsin B caspase-3 ischemia/reoxygenation neurons glia 

Abbreviations

AMC

7-amino-4-methylcoumarin

CA074

N-[L-3-trans-(propylcarbamoyl)-oxyran-2-carbonyl]-L-isoleucyl-L-proline

LDH

lactate hehydrogenase

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Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • M. V. Onufriev
    • 1
  • A. A. Yakovlev
    • 1
    • 2
  • A. A. Lyzhin
    • 3
  • M. Yu. Stepanichev
    • 1
  • L. G. Khaspekov
    • 3
  • N. V. Gulyaeva
    • 1
    Email author
  1. 1.Institute of Higher Nervous Activity and NeurophysiologyRussian Academy of SciencesMoscowRussia
  2. 2.Institute of Theoretical and Experimental BiophysicsRussian Academy of SciencesPushchino, Moscow RegionRussia
  3. 3.Neurology Research CenterRussian Academy of Medical SciencesMoscowRussia

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