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Blood, Vol. 93 No. 8 (April 15), 1999:
pp. 2533-2542
Characterization of Bone Marrow Laminins and Identification of
 5-Containing Laminins as Adhesive Proteins for Multipotent
Hematopoietic FDCP-Mix Cells
Yuchen Gu,
Lydia Sorokin,
Madeleine Durbeej,
Tord Hjalt,
Jan-Ingvar Jönsson, and
Marja Ekblom
From the Department of Animal Physiology, Biomedical Center, Uppsala,
Sweden; the Department of Experimental Medicine, University of
Erlangen, Erlangen, Germany; the Department of Laboratory Medicine,
Lund University Hospital, Malmö, Sweden; and the Department of
Internal Medicine, Uppsala Academic Hospital, Uppsala, Sweden.
Laminins are extracellular matrix glycoproteins that influence the
phenotype and functions of many types of cells. Laminins are
heterotrimers composed of  ,  , and  polypeptides. So far five
, three , and two polypeptide chains, and 11 variants of
laminins have been proposed. Laminins interact in vitro with mature
blood cells and malignant hematopoietic cells. Most studies have been
performed with laminin-1 (111), and its expression in bone
marrow is unclear. Employing an antiserum reacting with most laminin
isoforms, we found laminins widely expressed in mouse bone marrow.
However, no laminin 1 chain but rather laminin 2, 4, and 5
polypeptides were found in bone marrow. Our data suggest presence of
laminin-2 (211), laminin-8 (411), and laminin-10 (511) in bone marrow. Northern blot analysis showed expression of laminin 1, 2, 4, and 5 chains in long-term bone marrow cultures, indicating upregulation of laminin 1 chain expression in
vitro. Laminins containing 5 chain, in contrast to laminin-1, were
strongly adhesive for multipotent hematopoietic FDCP-mix cells.
Integrin 6 and 1 chains mediated this adhesion, as shown by
antibody perturbation experiments. Our findings indicate that laminins
other than laminin-1 are functional in adhesive interactions in bone marrow.
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