Am J Physiol Cell Physiol Journal of Neurophysiology
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Am J Physiol Cell Physiol 267: C1112-C1118, 1994;
0363-6143/94 $5.00
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AJP - Cell Physiology, Vol 267, Issue 4 C1112-C1118, Copyright © 1994 by American Physiological Society

ARTICLES

MCP-1-stimulated monocyte attachment to laminin is mediated by beta 2-integrins

Y. Jiang, J. F. Zhu, F. W. Luscinskas and D. T. Graves
Department of Oral Biology, Boston University School of Graduate Dentistry, Boston University School of Medicine 02118.

Migration of monocytes to sites of inflammation involves a series of attachments and detachments to extracellular matrix proteins. We examined the capacity of a chemokine, monocyte chemoattractant protein-1 (MCP-1), to regulate attachment of human monocytes to laminin, collagen I, collagen IV, or fibronectin. MCP-1 increased monocyte attachment to laminin in a dose- and time-dependent manner and stimulated a lesser increase to the other matrix proteins. Function-blocking monoclonal antibodies (MAbs) to the integrin beta 2-subunit (CD18), including Fab' fragments and alpha M (CD11b) blocked > 70% of attachment, whereas MAbs to the beta 1-integrin subunit reduced attachment by < 30%. This suggests that the CD11b/CD18 integrin is the predominant molecule involved in adhesion of MCP-1-stimulated monocytes to laminin. The association of CD11b with F-actin illustrated by confocal microscopy further supports this concept. In contrast, when monocytes were stimulated with the beta 1-stimulatory MAb TS2/16, monocyte adhesion to laminin occurred through beta 1-integrins. Thus MCP-1 can stimulate monocyte attachment to laminin, and this process is mediated through beta 2-integrins, principally CD11b/CD18.


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