title: Laminin and fibronectin promote the chemotaxis of human malignant plasma cell lines.
abstract: We examined chemotaxis of human plasma cells (PCs) in response to extracellular matrix proteins (ECMs) in the human PC cell lines FR4ds and OPM-1ds. The FR4ds cells expressed beta 1+, beta 3-, alpha 2-, alpha 3-, alpha 4+, alpha 5+, alpha 6+, and alpha v+ integrins, whereas the OPM-1ds cells expressed beta 1+, beta 3-, alpha 2-, alpha 3+, alpha 4+, alpha 5-, alpha 6+, and alpha v+. Fibronectin (FN) and laminin (LN) promoted the chemotaxis of the PCs. An inhibitory assay with anti-integrin monoclonal antibodies (MoAbs) showed that anti-alpha 4 MoAb partially inhibited the chemotaxis of FR4ds and completely inhibited the chemotaxis of OPM-1ds. Anti-alpha 5 MoAb alone had no effect on either of these two lines. Nevertheless, anti-alpha 5 MoAb completely inhibited chemotaxis when it was added with anti-alpha 4 in FR4ds, demonstrating a novel complementary role of VLA-5 toward VLA-4 in the chemotaxis induced by FN. LN facilitated chemotaxis both in OPM-1ds expressing alpha 3 and alpha 6 integrins and in FR4ds expressing alpha 6 integrin alone. Anti-alpha 6 MoAb completely inhibited FR4ds chemotaxis, whereas anti-alpha 3 and -alpha 6 MoAb had synergistic inhibitory effects on the chemotaxis of OPM-1ds. These results indicated that the distribution of PCs in human tissue are determined by at least two factors: the concentration of the ECM proteins FN and LN and the expression of integrins.
authors.affiliation: Department of Hematology and Oncology, Osaka University Medical School, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Shibayama
authors.forename: S
authors.initials: S
authors.lastname: Tagawa
authors.forename: H
authors.initials: H
authors.lastname: Hattori
authors.forename: R
authors.initials: R
authors.lastname: Inoue
authors.forename: S
authors.initials: S
authors.lastname: Katagiri
authors.forename: T
authors.initials: T
authors.lastname: Kitani
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology / Q000494:pharmacology; D002448:Cell Adhesion / Q000187:drug effects; D048429:Cell Size / Q000187:drug effects; D002633:Chemotaxis / Q000187:drug effects*; D005353:Fibronectins / Q000494:pharmacology*; D006801:Humans; D007797:Laminin / Q000494:pharmacology*; D009363:Neoplasm Proteins / Q000378:metabolism; D014411:Neoplastic Stem Cells / Q000187:drug effects* / Q000502:physiology; D009842:Oligopeptides / Q000494:pharmacology; D010950:Plasma Cells / Q000187:drug effects* / Q000502:physiology; D010954:Plasmacytoma / Q000473:pathology*; D017469:Receptors, Fibronectin / Q000037:antagonists & inhibitors / Q000276:immunology / Q000378:metabolism; D017474:Receptors, Laminin / Q000037:antagonists & inhibitors / Q000276:immunology; D016029:Receptors, Very Late Antigen / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: D000911:Antibodies, Monoclonal; D005353:Fibronectins; D007797:Laminin; D009363:Neoplasm Proteins; D009842:Oligopeptides; D017469:Receptors, Fibronectin; D017474:Receptors, Laminin; D016029:Receptors, Very Late Antigen; C047981:arginyl-glycyl-aspartic acid; C058161:glycyl-arginyl-glycyl-aspartyl-seryl-proline