Extended reports
Increased expression of integrins on fibroblast-like synoviocytes
from rheumatoid arthritis in vitro correlates with enhanced binding to
extracellular matrix proteins
a University
of Heidelberg, Heidelberg, Germany: Department
of Internal Medicine V , b Institute of
Pathology , c Department of Orthopaedic Surgery
, d University of Dresden,
Dresden, Germany: Department of Internal
Medicine I
Correspondence to: Dr N Rinaldi, Department of Internal Medicine V, Hospitalstrasse, D-69115 Heidelberg, Germany.
Accepted for publication 24 October 1996
OBJECTIVE
To compare in vitro expression of
1,
3, and
4 integrins in normal fibroblast-like synoviocytes (FBS)
and in FBS from rheumatoid arthritis (RA) synovium and to investigate
the adhesion of normal FBS and RA-FBS to the integrin binding
extracellular matrix (ECM) proteins: collagen type IV, fibronectin,
laminin, and tenascin.
METHODS
Expression of integrin receptors of
cultured FBS was detected by flow cytometry. Attachment of FBS to ECM
proteins was quantified by adhesion assays. Inhibition studies were
performed using monoclonal antibodies to the integrin subunits.
RESULTS
Compared with normal FBS, RA-FBS showed
increased expression of
1 to
6,
1, and
4 integrin subunits
and enhanced binding of ECM proteins. Binding to ECM proteins was
partly or completely blocked by an anti-
1 integrin antibody and
antibodies to
3,
5, and
6 integrin subunits. The blocking
efficiency was significantly (P < 0.05) higher in RA-FBS than in
normal FBS.
CONCLUSIONS
The enhanced expression of the
1
integrin receptors on cultured RA-FBS correlated with increased
attachment to ECM proteins. Adhesion of normal and RA-FBS to ECM
proteins is mediated through
1 integrin receptors. Therefore, the
tight binding of rheumatoid FBS to the matrix via
1 integrins might
play a role in ECM remodelling in the rheumatoid process in vivo.
© 1997 by Annals of the Rheumatic Diseases
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