|
|
 Previous Article | Table of Contents | Next Article 
Blood, 1 September 2001, Vol. 98, No. 5, pp. 1561-1566
PHAGOCYTES
A proteolytically truncated form of free CD18, the common chain
of leukocyte integrins, as a novel marker of activated
myeloid cells
Karel Drbal,
Pavla Angelisová,
Ivan Hilgert,
Jan  erný,
Petr Novák, and
Václav Ho ej í
From the Institute of Molecular Genetics and Institute
of Microbiology, Academy of Sciences of the Czech Republic and Faculty
of Sciences, Charles University, Prague, Czech Republic.
An unusual CD18 monoclonal antibody (mAb) MEM-148 binds, in
contrast to standard CD18 mAbs, specifically to peripheral blood monocytes and neutrophils activated by various stimuli such as phorbol
myristate acetate, opsonized zymosan, heat-aggregated immunoglobulin,
and (after priming with lipopolysaccharide, tumor necrosis factor, or
granulocyte-macrophage colony-stimulating factor) also by
formyl-methionyl-leucyl-phenylalanine. In addition, in vivo activated
neutrophils obtained from urine of patients following recent
prostatectomy were also strongly positive for MEM-148. On the activated
myeloid cells the mAb recognized a 65- to 70-kd protein identified
immunochemically and by mass spectrometric peptide sequencing as a
membrane-anchored fragment of CD18 (the common chain of leukocyte
integrins) produced by proteolytic cleavage. The CD18 fragment
originated mainly from integrin molecules stored intracellularly in
resting cells, it was unassociated with CD11 chains, and its formation
was inhibited by several types of protease inhibitors. Thus, the 65- to
70-kd CD18 fragment represents a novel abundant activation marker of
myeloid cells of so far unknown function but possibly involved in
conformational changes in leukocyte integrin molecules resulting in
increased affinity to their ligands.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
G. R. Van de Walle, K. Vanhoorelbeke, Z. Majer, E. Illyes, J. Baert, I. Pareyn, and H. Deckmyn
Two Functional Active Conformations of the Integrin {alpha}2{beta}1, Depending on Activation Condition and Cell Type
J. Biol. Chem.,
November 4, 2005;
280(44):
36873 - 36882.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R.-H. Tang, E. Tng, S. K. A. Law, and S.-M. Tan
Epitope Mapping of Monoclonal Antibody to Integrin {alpha}L {beta}2 Hybrid Domain Suggests Different Requirements of Affinity States for Intercellular Adhesion Molecules (ICAM)-1 and ICAM-3 Binding
J. Biol. Chem.,
August 12, 2005;
280(32):
29208 - 29216.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. D. M. Huq and L.-N. Wei
Post-translational Modification of Nuclear Co-repressor Receptor-interacting Protein 140 by Acetylation
Mol. Cell. Proteomics,
July 1, 2005;
4(7):
975 - 983.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y.-M. Xiong, J. Chen, and L. Zhang
Modulation of CD11b/CD18 Adhesive Activity by Its Extracellular, Membrane-Proximal Regions
J. Immunol.,
July 15, 2003;
171(2):
1042 - 1050.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
