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Biomedical subjects

T W Penberthy

Publications and source records attributed to T W Penberthy.

2 recordsLinked to original sources

Leukocyte adhesion molecules.

Recruitment of leukocytes is critical to many of the processes studied in oral biology. With the development of new tools such as monoclonal antibody production and transgenic mice, the specific adhesion molecules thought to be important in leukocyte recruitment have been identified and their function examined. These molecules can be divided into three major classes: selectins, members of the immunoglobulin superfamily, and integrins. They mediate interactions between leukocytes and endothelial cells, facilitating the initial process of leukocyte rolling, firm attachment to endothelium, transendothelial migration, diapedesis, and migration along connective tissue. The goal of this paper is to provide an understanding of which molecules are involved in the above processes by discussing their cellular distribution, counter-receptors, and physiologic function.

Animals↗

MCP-1-stimulated monocytes preferentially utilize beta 2-integrins to migrate on laminin and fibronectin.

Recruitment of monocytes to inflammatory sites involves a series of sequential attachments and detachments to extracellular matrix proteins in response to a chemoattractant gradient. In this study we compared the migration of human peripheral blood monocytes on different extracellular matrix proteins in response to monocyte chemoattractant protein-1 (MCP-1) and N-formylmethionyl-leucyl-phenylalanine. Monocytes migrated more effectively on laminin compared with other extracellular matrix proteins. In contrast, this preference was not observed with neutrophils, suggesting that the monocytes and neutrophils may have differences in their migration on extracellular matrix proteins. To study this further, function-blocking monoclonal antibodies were used to examine mechanistically whether beta 1- and beta 2-integrins were involved in monocyte migration on fibronectin or laminin in response to MCP-1. Monocyte migration on both laminin and fibronectin was blocked 100% (P < 0.05) by intact monoclonal antibody, F(ab') fragments, and F(ab')2 fragments to beta 2-integrins. We also determined that antibodies to beta 2-integrins block monocyte migration that has already been initiated. In contrast, antibody to the beta 1-integrins inhibited monocyte migration by approximately 40% (P < 0.05). Thus monocytes that express both beta 1- and beta 2-integrins require utilization of beta 2-integrins in migration on extracellular matrix proteins. The results also suggest that beta 1-integrins facilitate monocyte migration but that monocyte migration is not absolutely dependent on the interaction of beta 1-integrins with extracellular matrix proteins. In contrast, neutrophil migration is beta 2-integrin dependent and is not facilitated by beta 1-integrins.

CD18 Antigens↗