This Article
Right arrow Full Text
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 Wang, Z.
Right arrow Articles by Clinkenbeard, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, Z.
Right arrow Articles by Clinkenbeard, K.

 Previous Article  |  Next Article 

Infect Immun, May 1998, p. 1885-1890, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Pasteurella haemolytica Leukotoxin-Induced Increase in Phospholipase A2 Activity in Bovine Neutrophils

Zuncai Wang, Cyril Clarke,* and Kenneth Clinkenbeard

Department of Anatomy, Pathology, and Pharmacology, College of Veterinary Medicine, Oklahoma State University, Stillwater, Oklahoma 74078

Received 10 November 1997/Returned for modification 9 December 1997/Accepted 2 February 1998

Exposure of bovine neutrophils to Pasteurella haemolytica leukotoxin (LKT) stimulates the production of leukotriene B4 (LTB4), which is believed to be an important chemotactic agent in the development of acute fibrinopurulent pneumonic infection in cattle. The involvement of phospholipase A2 (PLA2) in LKT-induced synthesis of LTB4 was studied by using bovine neutrophils labeled with 3H-arachidonate ([3H]AA). Incubation of isolated neutrophils with [3H]AA resulted in incorporation of radioactivity in the PLA2 substrates phosphatidylcholine, phosphatidylinositol, and phosphatidylethanolamine. Exposure of radiolabeled neutrophils to LKT caused concentration- and time-dependent release of radioactivity and redistribution of radioactivity in neutrophil membranes consistent with utilization of phosphoglyceride substrate and release of free fatty acid and eicosanoid products. These LKT-induced effects could be inhibited by pretreatment with arachidonyl trifluoromethyl ketone, an inhibitor of type IV cytoplasmic PLA2, and were dependent on extracellular calcium. These results support the conclusion that LKT-induced synthesis of LTB4 involves a calcium-mediated increase in PLA2 activity.

* Corresponding author. Mailing address: Department of Anatomy, Pathology, and Pharmacology, College of Veterinary Medicine, Oklahoma State University, Stillwater, OK 74078. Phone: (405) 744-8093. Fax: (405) 744-5275. E-mail: clarke{at}okway.okstate.edu.

Infect Immun, May 1998, p. 1885-1890, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Kirschnek, S., Gulbins, E. (2006). Phospholipase A2 Functions in Pseudomonas aeruginosa- Induced Apoptosis. Infect. Immun. 74: 850-860 [Abstract] [Full Text]  
  • McKerral, L. J., Lo, R. Y. C. (2002). Construction and Characterization of an Acapsular Mutant of Mannheimia haemolytica A1. Infect. Immun. 70: 2622-2629 [Abstract] [Full Text]  
  • Borgquist, J. D., Quinn, M. T., Swain, S. D. (2002). Adhesion to extracellular matrix proteins modulates bovine neutrophil responses to inflammatory mediators. J. Leukoc. Biol. 71: 764-774 [Abstract] [Full Text]  
  • Wang, Z., Clarke, C. R., Clinkenbeard, K. D. (1999). Role of Phospholipase D in Pasteurella haemolytica Leukotoxin-Induced Increase in Phospholipase A2 Activity in Bovine Neutrophils. Infect. Immun. 67: 3768-3772 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»