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Developmental Immunology
Volume 6 (1998), Issue 3-4, Pages 205-213

L1 Makes Immunological Progress by Expanding Its Relations

1Department of Cellular Immunology 0710, German Cancer Research Centre, Im Neuenheimer Feld 280, Heidelberg D-69120, Germany
2Department of Immunology, The Scripps Research Institute, 10666 North Torrey Pines Rd., La Jolla 92037, California, USA

Received 15 August 1996; Accepted 12 April 1997

Copyright © 1998 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The cell-adhesion molecule L1 was originally described in the nervous system. It has recently been detected in CD4+ T lymphocytes, peripheral B lymphocytes, and granulocytes in the human immune system and in similar leucocyte types in the murine immune system. L mediates neural recognition by Ca+2, Mg+2-independent homophilic binding. In the human and murine immune systems, L1 binds to the “classical” vitronectin receptor, αVβ3, and fibronectin receptor, α5β1, respectively, and abstains from homophilic binding. Homophilic L1 binding probably involves antiparallel alignment of several interactive domains. Integrin binding is mediated by a short segment of immunoglobulinlike domain 6, which includes two RGD repeats in rodent L1 and one RGD motif in human L1. L1 is modulated in activated leucocytes in vitro in parallel to L-selectin, and diverse cell types release intact L in vivo and in vitro. Released L1 can bind to laminin and adheres to the extracellular matrix of sciatic nerve, M21 melanoma, and possibly spleen and other tissues. It can support integrin-dependent cell migration and preliminary data implicate it in tumor development and transnodal lymphocyte migration.