Murine platelet endothelial cell adhesion molecule (PECAM‐1)/CD31 modulates β2 integrins on lymphokine‐activated killer cells

European Journal of Immunology - Tập 23 Số 10 - Trang 2464-2471 - 1993
Luca Piali1, Steven Μ. Albelda2, H. Scott Baldwin3, Philippe Hammel1, Roland H. Gisler1, Sussan Nourshargh1
1Basel Institute for Immunology, Basel
2University of Pennsylvania Medical Center, Philadelphia
3Children's Hospital of Philadelphia and the Wistar Institute, Philadelphia

Tóm tắt

AbstractLymphokine‐activated killer (LAK) cells are able to colonize sites of tumor lesions in mouse and man. The molecular mechanisms of homing in on tumors are largely unknown. However, before LAK cells can reach the tumor, they must adhere to the vascular endothelia within the lesion and then extravasate. We developed a novel mAb, EA‐3, which recognizes the murine homologue of the human adhesion molecule CD31. It is present on a subpopulation of murine LAK cells and all endothelial cells. CD31 was also involved in the adhesion of LAK cells to endothelium. Since CD31 can initiate integrin activation by inside‐out signaling after binding to its ligand, EA‐3 was used to minimic this in adhesion assays. It induces modifications in the β2 integrin LFA‐1, leading to increased binding capacities of the cells to endothelium. In contrast, β1 integrins and RGD‐binding integrins were not affected. These results suggest that expression of CD31 might confer adhesive advantages for LAK cells prone to tumor infiltration.

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Tài liệu tham khảo

10.1084/jem.155.6.1823

10.1084/jem.159.2.495

10.1056/NEJM198704093161501

Schwarz R. E., 1989, Cancer Res., 49, 1441

10.1093/jnci/85.8.622

Yokoyama W. M., 1993, Curr. Opin. Cell Biol., 5, 67

10.1146/annurev.iy.08.040190.001431

10.1093/jnci/83.13.944

10.1084/jem.174.2.479

10.1126/science.1690453

Ohto H., 1985, Blood, 66, 873, 10.1182/blood.V66.4.873.873

Stockinger H., 1990, J. Immunol., 145, 3889, 10.4049/jimmunol.145.11.3889

10.1083/jcb.110.4.1227

Torimoto Y., 1992, J Immunol., 148, 388, 10.4049/jimmunol.148.2.388

10.1084/jem.176.1.245

10.1002/eji.1830190804

10.1083/jcb.114.5.1059

10.1084/jem.175.5.1401

DeLisser H. M., 1991, J. Cell Biol., 115, 70

10.1016/0955-0674(92)90099-X

10.1038/341619a0

10.1038/342811a0

10.1038/309629a0

10.1016/0092-8674(88)90536-3

Ralph P., 1978, Cancer Res., 38, 1414

Gunji Y., 1989, J Immunol., 142, 1748, 10.4049/jimmunol.142.5.1748

10.1084/jem.172.3.969

Bogen S. A., 1992, Am. J. Pathol., 141, 843

10.1083/jcb.107.1.321

10.1038/361079a0

10.1016/0092-8674(92)90115-S

10.1084/jem.177.1.185

10.1016/0167-5699(92)90151-V

10.1016/0955-0674(92)90106-M

10.1016/0167-5699(93)90205-Y

Jain R. K., 1988, Cancer Res., 48, 2641

10.1093/jnci/83.6.433

Muller W. A., 1993, FASEB J., 7, A640

10.1083/jcb.119.6.1387

10.1038/346425a0

10.1146/annurev.iy.10.040192.003021