IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rubins, J B
Right arrow Articles by Niewoehner, D E
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rubins, J B
Right arrow Articles by Niewoehner, D E

 Previous Article  |  Next Article 

Infection and Immunity, September 1994, p. 3829-3836, Vol. 62, No. 9
0019-9567/1994/$04.00+0     DOI:

research-article

Pneumolysin activates phospholipase A in pulmonary artery endothelial cells.

J B Rubins, T J Mitchell, P W Andrew, and D E Niewoehner

Department of Medicine, Veterans Affairs Medical Center, Minneapolis, Minnesota.

ABSTRACT

Pneumolysin has been identified as a virulence factor in Streptococcus pneumoniae disease. In addition to producing tissue injury through its cytolytic effect, pneumolysin might injure tissues indirectly by eliciting an inflammatory response. We demonstrate for the first time that pneumolysin is a rapid and potent activator of cellular phospholipase A in bovine pulmonary artery endothelial cells. In contrast to other toxin-activated phospholipases, pneumolysin-stimulated phospholipase A showed no substrate specificity among major cellular membrane phospholipids. Phospholipase A activation required the formation of functional transmembrane pores by pneumolysin rather than membrane lipid perturbation. Pneumolysin stimulation of phospholipase A was calcium dependent; however, pneumolysin did not appear to function simply as a calcium ionophore. Pneumolysin was capable of stimulating purified bee and snake venom phospholipase A2s against a phospholipid substrate isolated from endothelial cells. Thus, pneumolysin stimulates cellular phospholipase A and the resulting products might further injure tissues by direct cytolytic effect or by evoking inflammatory responses.


Infection and Immunity, September 1994, p. 3829-3836, Vol. 62, No. 9
0019-9567/1994/$04.00+0     DOI:




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 1994 by the American Society for Microbiology. All rights reserved.