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Mechanisms of sodium nitroprusside-induced death in human chondrocytes

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Overview

authors

  • Kuhn, K.
  • Lotz, Martin

publication date

  • September 2003

journal

  • Rheumatology International  Journal

abstract

  • The nitric oxide (NO) donor sodium nitroprusside (SNP) has been used to study NO-dependent cell death in human chondrocytes. This study compares SNP-induced chondrocyte death and SNP-activated signaling mechanisms with apoptosis induced by CD95 activation. Sodium nitroprusside increased cell death dose-dependently. Compared to CD95 stimulation, SNP induced only low levels of internucleosomal DNA fragmentation as measured by cell-death enzyme-linked immunosorbent assay (ELISA). However, SNP caused substantial nuclear DNA cleavage, as evidenced by terminal deoxynucleotidyltransferase (TdT)-mediated deoxyuridine triphosphate (dUTP) nick end-labeling (TUNEL). Caspase-3 processing in response to SNP was not detected. The pancaspase inhibitor Z-VAD.FMK partially abrogated the TUNEL signal but did not block cell death or internucleosomal DNA fragmentation. The caspase-3-specific inhibitor Ac-DEVD-CHO did not inhibit the SNP-induced TUNEL signal or internucleosomal DNA fragmentation. DNA degradation was not blocked by the p38 inhibitor SB 202190 but by the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine. The results of this study support the hypothesis that the phenotype and mechanisms of SNP-induced chondrocyte death are distinct from apoptosis induction via CD95.

subject areas

  • Antigens, CD95
  • Apoptosis
  • Caspase 3
  • Caspases
  • Cell Death
  • Cell Survival
  • Cells, Cultured
  • Chondrocytes
  • DNA Fragmentation
  • Humans
  • In Situ Nick-End Labeling
  • Mitogen-Activated Protein Kinases
  • Necrosis
  • Nitric Oxide Donors
  • Nitroprusside
  • Reactive Oxygen Species
  • Signal Transduction
  • p38 Mitogen-Activated Protein Kinases
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Research

keywords

  • DNA fragmentation
  • apoptosis
  • necrosis
  • sodium nitroprusside
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Identity

International Standard Serial Number (ISSN)

  • 0172-8172

Digital Object Identifier (DOI)

  • 10.1007/s00296-003-0299-y

PubMed ID

  • 14504917
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Additional Document Info

start page

  • 241

end page

  • 247

volume

  • 23

issue

  • 5

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