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Mycoplasma infection can sensitize host cells to apoptosis through contribution of apoptotic-like endonuclease(s).

Abstract
Mycoplasma infection may lead to various pathologies in a broad range of hosts. It has been shown that Mycoplasma may trigger cell death in cell cultures; however, the mechanism remains unknown. In the present paper we show that Mycoplasma infection of different lymphocyte and epithelial tumour cell lines leads to the inhibition of proliferation, and increased cell death, accompanied by DNA fragmentation and the morphological features of apoptosis. We also showed that this infection leads to an increased sensitivity of cells to various inducers of apoptosis targeting different signalling pathways. Finally, we show that increased apoptosis is associated with overexpression of an endonuclease produced by Mycoplasma. This endonuclease is recovered in the nuclear fraction of host cells, introduces mostly DSB and is active at neutral pH in the presence of divalent cations. Activation of this endonuclease is connected with limited proteolysis, which may be reproduced in vitro by snake venom serine proteinase.
AuthorsI A Sokolova, A T Vaughan, N N Khodarev
JournalImmunology and cell biology (Immunol Cell Biol) Vol. 76 Issue 6 Pg. 526-34 (Dec 1998) ISSN: 0818-9641 [Print] United States
PMID9893030 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Snake Venoms
  • Sulfonamides
  • 1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione
  • Endonucleases
  • Serine Endopeptidases
Topics
  • Animals
  • Apoptosis (genetics, physiology)
  • Cell Line
  • DNA Fragmentation
  • Electrophoresis, Gel, Two-Dimensional
  • Endonucleases (analysis, drug effects, metabolism)
  • Humans
  • Jurkat Cells
  • Mice
  • Mycoplasma (enzymology, pathogenicity)
  • Mycoplasma Infections (enzymology, physiopathology)
  • Serine Endopeptidases (pharmacology)
  • Snake Venoms (enzymology)
  • Species Specificity
  • Sulfonamides (pharmacology)

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