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Laminin γ2 chain as a stromal cell marker of the human bone marrow microenvironment
Author(s) -
Siler Ulrich,
Rousselle Patricia,
Müller Claudia A.,
Klein Gerd
Publication year - 2002
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.2002.03800.x
Subject(s) - bone marrow , stromal cell , laminin , haematopoiesis , peripheral blood mononuclear cell , cell adhesion molecule , microbiology and biotechnology , chemistry , biology , immunology , cancer research , stem cell , in vitro , biochemistry , extracellular matrix
Summary. Laminins are large heterotrimeric molecules consisting of α, β and γ chains. At present, five α chains, three β chains and three γ chains have been characterized. Laminin‐5 (α3β3γ2) is the only isoform known to date which contains a γ2 chain. In human bone marrow, non‐haematopoietic stromal cells expressed the laminin γ2 chain, whereas bone marrow mononuclear cells did not. Co‐localization of the γ2 chain was detected with the laminin α4 and α5 chains, and co‐immunoprecipitation studies revealed a new isoform consisting of α5, β2 and γ2 chains. The laminin γ2 chain was also co‐localized with α‐sm‐actin in bone marrow, but it was not expressed in endothelial cells or megakaryocytes, indicating that the γ2 chain is exclusively expressed in vivo in bone marrow stromal cells. The laminin γ2 chain containing isoform LN‐5 was shown to be an adhesive substrate for a small subpopulation of bone marrow mononuclear cells and also for peripheral blood platelets. Taken together, these results indicate that (I) laminin isoforms containing the γ2 chain can act as adhesive substrates for human haematopoietic cells, and (II) the laminin γ2 chain can be used as a specific marker molecule for human bone‐marrow‐derived stromal cells.