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Prepublished online as a Blood First Edition Paper on September 19, 2002; DOI 10.1182/blood-2002-03-0796.
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Blood, 1 February 2003, Vol. 101, No. 3, pp. 877-885
HEMATOPOIESIS
Laminin isoform-specific promotion of adhesion and migration
of human bone marrow progenitor cells
Yu-Chen Gu,
Jarkko Kortesmaa,
Karl Tryggvason,
Jenny Persson,
Peter Ekblom,
Sten-Eirik Jacobsen, and
Marja Ekblom
From the Department of Medical Biochemistry and
Biophysics, Karolinska Institute and BioStratum AB, Stockholm,
Sweden; Department of Cell and Molecular Biology; Stem
Cell Laboratory, Department of Laboratory Medicine; both of University
of Lund, Sweden; and Department of Hematology, University
Hospital, Lund, Sweden.
Laminins are    heterotrimeric extracellular proteins that
regulate cellular functions by adhesion to integrin and nonintegrin receptors. Laminins containing 4 and 5 chains are expressed in
bone marrow, but their interactions with hematopoietic progenitors are
unknown. We studied human bone marrow cell adhesion to laminin-10/11 (511/521), laminin-8 (411), laminin-1
(111), and fibronectin. About 35% to 40% of
CD34+ and CD34+CD38 stem and
progenitor cells adhered to laminin-10/11, and 45% to 50% adhered to
fibronectin, whereas they adhered less to laminin-8 and laminin-1.
Adhesion of CD34+CD38 cells to laminin-10/11
was maximal without integrin activation, whereas adhesion to other
proteins was dependent on protein kinase C activation by
12-tetradecanoyl phorbol-13-acetate (TPA). Fluorescence-activated cell-sorting (FACS) analysis showed expression of integrin 6 chain
on most CD34+ and CD34+CD38
cells. Integrin 6 and 1 chains were involved in binding of both
cell fractions to laminin-10/11 and laminin-8. Laminin-10/11 was highly
adhesive to lineage-committed myelomonocytic and erythroid progenitor
cells and most lymphoid and myeloid cell lines studied, whereas
laminin-8 was less adhesive. In functional assays, both laminin-8 and
laminin-10/11 facilitated stromal-derived factor-1 (SDF-1)-stimulated transmigration of CD34+ cells, by an
integrin 6 receptor-mediated mechanism. In conclusion, we
demonstrate laminin isoform-specific adhesive interactions with human
bone marrow stem, progenitor, and more differentiated cells. The
cell-adhesive laminins affected migration of hematopoietic progenitors,
suggesting a physiologic role for laminins during hematopoiesis.
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