PeproTech Inc.

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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Berenson, C. S.
Right arrow Articles by Rasp, R. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Berenson, C. S.
Right arrow Articles by Rasp, R. H.
(Journal of Leukocyte Biology. 2002;72:492-502.)
© 2002 by Society for Leukocyte Biology

The role of ceramide of human macrophage gangliosides in activation of human macrophages

Charles S. Berenson, Melissa A. Gallery, Jane M. Smigiera and Robin H. Rasp

Infectious Diseases Section, Department of Veterans Affairs Western New York Healthcare System, State University of New York at Buffalo, School of Medicine

Correspondence: Charles S. Berenson, Division of Infectious Diseases (151), VA Western NY Healthcare System, 3495 Bailey Avenue, Buffalo, NY 14215. E-mail: berenson{at}acsu.buffalo.edu

Gangliosides of macrophages have immunoregulatory and structural attributes, distinct from neural gangliosides. We previously produced a monoclonal antibody to human macrophage gangliosides (HMG; mAb25F4), which inhibited macrophage migration and recognized a surface-accessible epitope. We investigated expanded immunoregulatory properties and molecular domains for antibody recognition. mAb25F4 directly induced human macrophage production of proinflammatory cytokines, interleukin-1ß, and tumor necrosis factor {alpha}. Conditions were established for selective, reversible depletion of HMG with D-threo-(R,R)-1-phenyl-2-decanoyl-amino-3-morpholine-1-propa-nol. mAb25F4 had diminished recognition for ganglioside-depleted macrophages, which was restored with regeneration of gangliosides. Although desialylation of HMG did not impair mAb25F4 recognition, enzymatic cleavage of ceramide abolished antibody binding. Antibody recognition was specific for the ceramide fraction, with preferential recognition for ceramide of HMG and murine macrophage gangliosides and limited recognition for neural tissue ceramide and gangliosides. This study underscores the importance of structurally distinct ceramide of macrophage gangliosides as a critical domain for ganglioside-mediated activation of human macrophages.

Key Words: glycosphingolipids • mononuclear phagocytes • cytokines • PDMP




This article has been cited by other articles:


Home page
 Infect. Immun.Home page
C. S. Berenson, T. F. Murphy, C. T. Wrona, and S. Sethi
Outer Membrane Protein P6 of Nontypeable Haemophilus influenzae Is a Potent and Selective Inducer of Human Macrophage Proinflammatory Cytokines
Infect. Immun., May 1, 2005; 73(5): 2728 - 2735.
[Abstract] [Full Text] [PDF]