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4
1
1)1
*
Microbiology and Tumor Biology Center, and
Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden;
Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia; and
Institute of Biomedicine, Department of Anatomy, University of Helsinki, Helsinki, Finland
Laminins, a growing family of large heterotrimeric proteins with
cell adhesive and signaling properties, are major components of
vascular and other basement membranes. Expression, recognition, and use
of laminin isoforms by leukocytes are poorly understood. In monoblastic
THP-1 cells, transcripts for laminin 
1-,
1-, and 
4-chains were detected by RT-PCR.
Following immunoaffinity purification on a laminin 1
Ab-Sepharose column, laminin 1- (220 kDa),
1- (200 kDa), and 4- (180/200 kDa) chains
were detected by Western blotting in THP-1 cells and in two other
monoblastic cell lines, U-937 and Mono Mac 6. After cell
permeabilization, a mAb to laminin 1-chain reacted with
practically all blood monocytes by immunofluorescence flow cytometry,
and laminin-8 (411) could
be isolated also from these cells. Monoblastic JOSK-I cells adhered
constitutively to immobilized recombinant laminin-8, less than to
laminin-10/11
(511/521)
but to a higher level than to laminin-1
(111). Compared with the
other laminin isoforms, adhesion to laminin-8 was preferentially
mediated by 61 and 2
integrins. Laminin-8 and, to a lower extent, laminin-1 promoted
spontaneous and chemokine-induced migration of blood monocytes, whereas
laminin-10/11 was inhibitory. Altogether, the results indicate that
leukocytes, as other cell types, are able to synthesize complete
laminin molecules. Expression, recognition, and use of laminin-8 by
leukocytes suggest a major role of this laminin isoform in leukocyte
physiology.
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