OBJECTIVE: The mechanisms used by @entity1 lymphoproliferative diseases to invade locally and @entity3 are thought to be similar to those developed by solid @entity5 , including cell proliferation and secretion of extracellular matrix-degrading enzymes following adhesion to extracellular matrix proteins. Hence, the ability of Namalwa ( @entity2109 ), @entity1 ( @entity1582 ), and @entity11511 ( @entity11511 ) cells to interact with the extracellular matrix components @entity4732 and fibronectin was determined. Fresh bone marrow plasma cells from @entity1 with @entity1582 also were studied. MATERIALS AND METHODS: Engagement of alpha(v)beta(3) integrin, formation and protein composition of focal adhesion contacts on the cell surface, phosphorylation of several signal transduction proteins in the contacts, cell proliferation, and enzyme secretion were studied following adhesion to @entity4732 and fibronectin. RESULTS: All three lines adhered to immobilized @entity4732 and fibronectin. Adhesion was fully prevented by neutralizing monoclonal anti-alpha(v)beta(3) integrin antibody. Integrin engagement caused the formation of phosphorylated pp60( @entity7242 )/focal adhesion kinase complexes and the aggregation of focal adhesion plaques containing the beta(3) integrin subunit, the cytoskeletal proteins @entity10274 , @entity5263 , and paxillin, the @entity669 kinases focal adhesion kinase and pp60( @entity7242 ), the adapter protein @entity10240 , and the mitogen-activated protein kinase @entity3963 . Free and immobilized @entity4732 and fibronectin stimulated the proliferation of cells under serum-free conditions and the production and release of @entity2290 , and increased the release of the activated forms of @entity5379 in an alpha(v)beta(3) integrin-dependent manner. Similar results were obtained in @entity1582 plasma cells. CONCLUSIONS: The demonstrated ability of @entity5 cells to interact with the extracellular matrix components @entity4732 and fibronectin via alpha(v)beta(3) integrin can be interpreted as evidence of a novel mechanism for their invasion and spreading. This interaction allows them to adhere to the substratum and enhances their proliferation and protease secretion.

alpha(v)beta(3) integrin engagement modulates cell adhesion, proliferation, and protease secretion in XXXX @entity5 cells.

@entity1 :: ('9606', 'Species') :: ['human', 'patients', 'U266'] @entity5263 :: ('2017', 'Gene') :: ['cortactin'] @entity5379 :: ('4313;4318', 'Gene') :: ['matrix metalloproteinase-2 and matrix metalloproteinase-9'] @entity7242 :: ('6714', 'Gene') :: ['src'] @entity5 :: ('MESH:D009369', 'Disease') :: ['lymphoid tumor', 'tumors'] @entity10274 :: ('7414', 'Gene') :: ['vinculin'] @entity3963 :: ('5594', 'Gene') :: ['ERK-2'] @entity2109 :: ('MESH:D002051', 'Disease') :: ["Burkitt's lymphoma"] @entity1582 :: ('MESH:D009101', 'Disease') :: ['multiple myeloma', 'myeloma'] @entity10240 :: ('2885', 'Gene') :: ['Grb-2'] @entity3 :: ('MESH:D009362', 'Disease') :: ['metastasize'] @entity669 :: ('CHEBI:18186', 'Chemical') :: ['tyrosine'] @entity11511 :: ('MESH:D054218', 'Disease') :: ['T-cell lymphoblastic leukemia', 'CEM'] @entity4732 :: ('7448', 'Gene') :: ['vitronectin'] @entity2290 :: ('5328', 'Gene') :: ['urokinase-type plasminogen activator']
@entity1 :: (9606,Species) :: ['human']
