GlyCAM-1, a Physiologic Ligand for L-selectin, Activates Beta 2 Integrins on Naive Peripheral Lymphocytes

Overview

Journal J Exp Med

Specialties Allergy & Immunology
General Medicine

Date 1996 Oct 1

PMID 8879206

Citations 39

Authors

S T Hwang

M S Singer

P A Giblin

T A Yednock

K B Bacon

S I Simon

S D Rosen

Affiliations

Soon will be listed here.

Abstract

Naive T cells are selectively recruited from the blood into peripheral lymph nodes during lymphocyte recirculation. L-selectin, a lectin-like receptor, mediates the initial attachment of lymphocytes to high endothelial venules (HEV) in lymph nodes. A subsequent step involving the activation of beta 2 integrins has been proposed to facilitate firm adhesion, but the activating signals are poorly understood. We report here that either antibody-mediated cross-linking of L-selectin on human lymphocytes or treatment of the cells with GlyCAM-1, an HEV-derived, secreted ligand for L-selectin, stimulates their binding to ICAM-1 through the beta 2 integrin pathway. Furthermore, GlyCAM-1 causes the rapid expression of a neoepitope on beta 2 integrins associated with a high-avidity state. Naive (CD45RA+), but not memory (CD45R0+) lymphocytes, respond to L-selectin cross-linking or GlyCAM-1 treatment. Thus, the complexing of L-selectin by specific ligands may provide key signals to naive lymphocytes, contributing to their selective recruitment into peripheral lymphoid organs.

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