JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Remaley, A. T.
Right arrow Articles by Kaplan, S. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Remaley, A. T.
Right arrow Articles by Kaplan, S. S.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 259, Issue 18, 11173-11175, 09, 1984

Leishmanial phosphatase blocks neutrophil O-2 production

AT Remaley, DB Kuhns, RE Basford, RH Glew and SS Kaplan

Leishmania donovani, the causative agent in kala-azar or visceral leishmaniasis, infects cells of the macrophage system. We show that a purified preparation of the tartrate-resistant acid phosphatase, isolated from the external surface of L. donovani promastigotes, inhibits superoxide anion production by human neutrophils. Preincubation of neutrophils for 15-30 min at 37 degrees C with 240 units (1 unit equals 1 nmol of 4-methylumbelliferyl phosphate cleaved per h) of the acid phosphatase decreases both the rate and extent of superoxide generation by 90% upon stimulation with the chemoattractant peptide fMet-Leu-Phe. The ability of the phosphatase to suppress superoxide anion production is abolished by heat inactivation of the enzyme or by incorporation of an acid phosphatase inhibitor in the preincubation medium, indicating that the effect is dependent on the catalytic activity of the enzyme. These results suggest a possible pathophysiologic role for the acid phosphatase of L. donovani promastigotes.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
E. Aga, D. M. Katschinski, G. van Zandbergen, H. Laufs, B. Hansen, K. Muller, W. Solbach, and T. Laskay
Inhibition of the Spontaneous Apoptosis of Neutrophil Granulocytes by the Intracellular Parasite Leishmania major
J. Immunol., July 15, 2002; 169(2): 898 - 905.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
V. Aragon, S. Kurtz, and N. P. Cianciotto
Legionella pneumophila Major Acid Phosphatase and Its Role in Intracellular Infection
Infect. Immun., January 1, 2001; 69(1): 177 - 185.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
T. J. Reilly, D. L. Chance, and A. L. Smith
Outer Membrane Lipoprotein e (P4) of Haemophilus influenzae Is a Novel Phosphomonoesterase
J. Bacteriol., November 1, 1999; 181(21): 6797 - 6805.
[Abstract] [Full Text]

Home page
 Infect. Immun.Home page
H. Jungnitz, N. P. West, M. J. Walker, G. S. Chhatwal, and C. A. Guzman
A Second Two-Component Regulatory System of Bordetella bronchiseptica Required for Bacterial Resistance to Oxidative Stress, Production of Acid Phosphatase, and In Vivo Persistence
Infect. Immun., October 1, 1998; 66(10): 4640 - 4650.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.