The JI PBL Intereron Source
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 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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ueda, E.
Right arrow Articles by Kitani, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ueda, E.
Right arrow Articles by Kitani, T.

The Journal of Immunology, Vol 143, Issue 4 1274-1277, Copyright © 1989 by American Association of Immunologists

ARTICLES

Different membrane anchors of Fc gamma RIII (CD16) on K/NK-lymphocytes and neutrophils. Protein- vs lipid-anchor

E Ueda, T Kinoshita, J Nojima, K Inoue and T Kitani
Department of Clinical Research, Osaka University, Japan.

Fc gamma RIII (CD16), the type three receptor for the Fc portion of IgG, is expressed on neutrophils, killer (K)/NK lymphocytes and macrophages. K/NK lymphocyte Fc gamma RIII, which plays a role in antibody-dependent cellular cytotoxicity, is an efficient signal transducing molecule, whereas neutrophil Fc gamma RIII, which plays a role in immune-complex clearance, seems less efficient in signal transduction. Neutrophil Fc gamma RIII has been reported to be a glycan- phosphatidylinositol-anchored membrane protein. Our studies suggest that K/NK lymphocyte Fc gamma RIII is protein-anchored rather than glycan-phosphatidylinositol-anchored. That is, K/NK lymphocyte Fc gamma RIII was resistant to phosphatidylinositol-specific phospholipase C and surface expression of Fc gamma RIII was not affected on K/NK lymphocytes from patients with paroxysmal nocturnal hemoglobinuria, a disorder of hemopoietic stem cells resulting in deficient expression of glycan-phosphatidylinositol-anchored proteins. Different membrane anchoring mechanisms of the Fc gamma RIII may account for different consequences of the ligand binding to two cell types.


This article has been cited by other articles:


Home page
 J. Immunol.Home page
S. E. Sweeney and Y. B. Kim
Identification of a Novel Fc{gamma}RIIIa{alpha}-Associated Molecule That Contains Significant Homology to Porcine Cathelin
J. Immunol., January 15, 2004; 172(2): 1203 - 1212.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. E. Chesla, P. Li, S. Nagarajan, P. Selvaraj, and C. Zhu
The Membrane Anchor Influences Ligand Binding Two-dimensional Kinetic Rates and Three-dimensional Affinity of Fcgamma RIII (CD16)
J. Biol. Chem., March 31, 2000; 275(14): 10235 - 10246.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Nagarajan, S. Chesla, L. Cobern, P. Anderson, C. Zhu, and P. Selvaraj
Ligand Binding and Phagocytosis by CD16 (Fc [IMAGE] Receptor III) Isoforms
J. Biol. Chem., October 27, 1995; 270(43): 25762 - 25770.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
M. Hibbs, P Selvaraj, O Carpen, T. Springer, H Kuster, M. Jouvin, and J. Kinet
Mechanisms for regulating expression of membrane isoforms of Fc gamma RIII (CD16)
Science, December 22, 1989; 246(4937): 1608 - 1611.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1989 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1989 by The American Association of Immunologists, Inc. All rights reserved.