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Published online before print June 12, 2008
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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.0108048

Received for publication January 18, 2008.
Revised May 5, 2008.
Accepted for publication May 5, 2008.

Article

Laminin isoforms of lymph nodes and predominant role of {alpha}5-laminin(s) in adhesion and migration of blood lymphocytes

Gezahegn Gorfu *, Ismo Virtanen {dagger}, Mika Hukkanen {dagger}, Veli-Pekka Lehto {ddagger}, Patricia Rousselle {sect}, Ellinor Kenne ||, Lennart Lindbom ||, Randall Kramer , Karl Tryggvason #, and Manuel Patarroyo *@

Departments of *Odontology, ||Physiology and Pharmacology, and #Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden; {dagger}Institute of Biomedicine/Anatomy and {ddagger}Haartman Institute, University of Helsinki, Finland; {sect}Institut de Biologie et Chimie des Protéines, Université Lyon I, Lyon, France; and Department of Cell and Tissue Biology, University of California, San Francisco, California, USA

@ To whom correspondence should be addressed. E-mail: manuel.patarroyo{at}ki.se.


  Abstract

During extravasation and within lymph nodes (LNs), blood lymphocytes interact with laminins (Lms), major components of vascular basement membranes (BMs) and of reticular fibers (RFs), a fibrillar extracellular matrix. However, the identity and role of these laminin isoform(s) are poorly known. By using confocal microscopy examination of human LNs, we show that BMs of high endothelial venules (HEVs) express laminin {alpha}3, {alpha}4, {alpha}5, {beta}1, {beta}2, and {gamma}1 chains and that the same chains, in addition to {alpha}2, are found in RFs. In functional studies with laminin isoforms covering all Lm {alpha} chains, {alpha}5-laminin (Lm-511) was the most adhesion- and migration-promoting isoform for human blood lymphocytes, followed by {alpha}3- (Lm-332) and {alpha}4- (Lm-411) laminins, and the lymphocytes used the {alpha}6{beta}1 integrin as the primary receptor for the {alpha}5-laminin. Moreover, Lm-511 strongly costimulated T cell proliferation, and blood lymphocytes were able to secrete {alpha}4- and {alpha}5-laminins following stimulation. The LN cell number in laminin {alpha}4-deficient mice compared with wild-type did not differ significantly. This study demonstrates a predominant role for {alpha}5-laminin(s) in blood lymphocyte biology and identifies LN laminins and their integrin receptors in blood lymphocytes.

Key Words: leukocyte • extracellular matrix • basement membrane • chemotaxis






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