|
|
 Previous Article | Table of Contents | Next Article 
Distribution of integrins on human peripheral blood mononuclear cells
HG Klingemann and S Dedhar
Terry Fox Laboratory, B.C. Cancer Research Center, Vancouver, Canada.
The receptors for fibronectin (FN-R) and vitronectin (VN-R) belong to a
family of integral membrane glycoproteins known to be involved in cell-
extracellular matrix and cell-cell interactions named integrins (FN-R =
beta 1 integrin and VN-R = beta 3 integrin). Adhesion studies using FN-
coated plastic dishes and highly purified subpopulations of peripheral
blood mononuclear cells (PBMCs) showed a strong binding of monocytes and T
lymphocytes to FN but virtually no binding of B cells to FN. Binding of
monocytes and T cells to FN could be partially inhibited by a hexapeptide
(GRGDSP) containing the adhesive peptide sequence Arg-Gly- Asp (RGD) as
well as by an anti-FN-R antibody. The distribution of beta 1 and beta 3
integrin complexes on PBMCs was characterized by immunoprecipitation of
detergent extracts of 125I-labeled cells using polyclonal antibodies
against these two receptors. Two surface polypeptides corresponding to the
alpha and beta chains of FN-R and VN- R were found on all three cell types.
To characterize these receptors further, monoclonal antibodies (MoAbs)
against the very late antigens (VLAs) 1, 3, and 5 were used for
immunoprecipitation studies. Monocytes and T cells reacted with VLA 5 that
was previously identified as the human FN receptor, whereas no labeling
with anti-VLA 5 could be shown for B cells. When cell populations were
cultured in 10% human serum for 24 hours, an increase in beta 1-integrin+
monocytes and T cells was observed. The number of beta 3-integrin+ cells
remained essentially unchanged. The presence of beta 1 and beta 3 integrins
on monocytes as well as on T and B lymphocytes may be of significance in
the ability of these cells to interact with each other and participate in
hematopoiesis and certain immune reactions.
Volume 74,
Issue 4,
pp. 1348-1354,
09/01/1989
Copyright © 1989 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
A. D. Ricart, A. W. Tolcher, G. Liu, K. Holen, G. Schwartz, M. Albertini, G. Weiss, S. Yazji, C. Ng, and G. Wilding
Volociximab, a Chimeric Monoclonal Antibody that Specifically Binds {alpha}5{beta}1 Integrin: A Phase I, Pharmacokinetic, and Biological Correlative Study
Clin. Cancer Res.,
December 1, 2008;
14(23):
7924 - 7929.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. Bei, Y. Lu, S. L. Bellis, W. Zhou, E. Horvath, and E. A. Eklund
Identification of a HoxA10 Activation Domain Necessary for Transcription of the Gene Encoding beta3 Integrin during Myeloid Differentiation
J. Biol. Chem.,
June 8, 2007;
282(23):
16846 - 16859.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. D. Loike, L. Cao, S. Budhu, S. Hoffman, and S. C. Silverstein
Blockade of {{alpha}}5{{beta}}1 Integrins Reverses the Inhibitory Effect of Tenascin on Chemotaxis of Human Monocytes and Polymorphonuclear Leukocytes Through Three-Dimensional Gels of Extracellular Matrix Proteins
J. Immunol.,
June 15, 2001;
166(12):
7534 - 7542.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Rich, F. George 4th, J. Law, and W. Martin
Cell-adhesive motif in region II of malarial circumsporozoite protein
Science,
September 28, 1990;
249(4976):
1574 - 1577.
[Abstract]
[PDF]
|
|
|
|
|
