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Mß2 (CD11b/CD18)1
*
The La Jolla Institute for Experimental Medicine, La Jolla, CA 92037;
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037
The work presented here demonstrates that human complement factor H
is an adhesion ligand for human neutrophils but not for eosinophils.
The adherence of polymorphonuclear leukocytes (PMNs) to plastic wells
coated with factor H depended on divalent metal ions and was augmented
by C5a and TNF-
. PMN adhesion to factor H in the presence or absence
of C5a was blocked specifically by mAbs against CD11b or CD18. Affinity
purification using factor H Sepharose followed by immunoprecipitation
using mAbs to various integrin chains identified Mac-1 (CD11b/CD18) as
a factor H binding receptor. The presence of surface bound factor H
enhanced neutrophil activation resulting in a two- to fivefold increase
in the generation of hydrogen peroxide by PMNs stimulated by C5a or
TNF-. When factor H was mixed with PMNs, 1.4 to 3.8-fold more cells
adhered to immobilized heparin or chondroitin A. In addition, augmented
adhesion of PMNs was measured when factor H, but not HSA or C9, was
absorbed to wells that were first coated with heparin or chondroitin A.
The adhesion of PMNs to glycosaminoglycan-factor H was blocked by mAbs
to CD11b and CD18. These studies demonstrate that factor H is an
adhesion molecule for human neutrophils and suggest that the
interaction of factor H with glycosaminoglycans may facilitate the
tethering of this protein in tissues allowing factor H to serve as a
neutrophil adhesion ligand in vivo.
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