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xß2 Integrin (CD11c-CD18, gp150-95)1


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Laboratoire de Biochimie Médicale et Biologie Moléculaire, Centre National de la Recherche Scientifique, UPRESA 6021, Institut Fedératif de Recherche 53-Biomolécules, Faculté de Médecine, Université de Reims Champagne-Ardenne, Reims, France; and
Laboratoire Central dHématologie, Centre Hospitalier Universitaire de Reims, rue du Général Koenig, Reims, France
Human blood monocytes are attracted into connective tissues during
early steps of inflammation and wound healing, and locally interact
with resident cells and extracellular matrix proteins. We studied the
effects of type I collagen on monocyte adhesion and superoxide anion
production, using human monocytes elutriated from peripheral blood and
type I collagen obtained from rat tail tendon. Both acid-soluble and
pepsin-digested type I collagens promoted the adhesion of monocytes,
whereas only acid-soluble collagen with intact telopeptides induced the
production of superoxide. Adhesion and activation of monocytes on
acid-soluble type I collagen depended on the presence of divalent
cations. mAbs directed against integrin subunits CD11c and CD18
specifically inhibited adhesion and activation of monocytes on type I
collagen. Protein membrane extracts obtained from monocytes were
submitted to affinity chromatography on collagen I-Sepharose 4B, and
analyzed by Western blotting using specific anti-integrin subunit
Abs. In the case of both acid-soluble and pepsin-digested collagens,
two bands were revealed with mAbs against CD11c and CD18 integrin
subunits. Our results demonstrate that monocytes interact with type I
collagen through CD11c-CD18 (
xß2)
integrins, which promote their adhesion and activation. For monocyte
activation, specific domains of the type I collagen telopeptides are
necessary. Interactions between monocytes and collagen are most likely
involved in the cascade of events that characterize the initial phases
of inflammation.
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