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Human endothelial cells express integrin receptors on the luminal aspect of
their membrane
G Conforti, C Dominguez-Jimenez, A Zanetti, MA Gimbrone , O Cremona, PC Marchisio and E Dejana
Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy.
Endothelial cells (EC) form a dynamic interface between blood and the rest
of the body. EC surface properties promoting adhesion of reactive plasma
proteins and/or circulating cells might be of pivotal importance for the
homeostasis of blood and tissues. EC express multiple integrin receptors
that promote their attachment to the subendothelial matrix proteins. Among
these receptors, alpha v beta 3 is of particular relevance on EC, since it
is abundantly expressed and can bind many different matrix and plasma
proteins. It is still unknown whether integrin receptors are selectively
located to the basal side of EC membrane or may also be exposed on the cell
surface in contact with blood. This issue was addressed using different
experimental approaches. First, selective surface radioiodination using
lactoperoxidase (LPO)-latex beads and immunoprecipitation analysis were
performed. We found that cultured EC, similarly to human skin fibroblasts
(HSF), expose alpha v beta 3 on both their apical (free) and basal
(substratum-attached) surfaces. This held also for other integrins such as
alpha 2 beta 1, alpha 3 beta 1, alpha 5 beta 1, and alpha 6 beta 1.
Immunoprecipitation data were verified by morphological techniques.
Immunofluorescence and immunogold-staining of EC with alpha v beta 3, as
well as with beta 1 subfamily antibodies, showed a diffuse and granular
distribution of these integrins on EC surface. alpha v beta 3 and beta 1
integrins were also detected on the apical membrane of EC at higher
magnification by scanning electron microscopy (SEM). Finally, data obtained
on cultured EC were confirmed in vivo on immunogold-labeled ultrathin
cryosections of human vessels by transmission electron microscopy (TEM).
Data indicate, that in addition to their role in promoting EC attachment to
extracellular matrix proteins, integrin receptors of EC can be exposed to
blood-stream and eventually be available for binding of plasma proteins and
circulating cells.
Volume 80,
Issue 2,
pp. 437-446,
07/15/1992
Copyright © 1992 by The American Society of Hematology

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