CDB15:0000557 FBLN2 — ITGB3
Experimentally validated in Human, Mixed species, Mouse; Orthology-inferred in Human, Mouse, Rat, Frog, Zebrafish, Chicken, Macaque, Pig, Dog, Cow, Chimp, Horse, Marmoset, Sheep
Title
Journal:; Year Published:
Abstract
Association of extracellular matrix proteins fibulin-1 and fibulin-2 with fibronectin in bone marrow stroma.
British journal of haematology, 2000; PubMed, Mus Musculus Fbln2 — Mus Musculus Itgb3
ABSTRACT: Extracellular matrix (ECM) molecules, together with growth factors and stromal cells, regulate haematopoietic cell development in bone marrow (BM). We report here expression of ECM proteins fibulin-1 and fibulin-2 in mouse BM. In other tissues, fibulin-1 and fibulin-2 associate with fibronectin and other ECM proteins. Fibulin-2 has also been found to adhere to cells via beta3 integrins. We studied the association of fibulins with fibronectin in BM stroma. By confocal microscopy, fibulin-1 and fibulin-2 immunostainings were co-localized with fibronectin in the adherent layer of long-term BM cultures. In cell adhesion assays using recombinant proteins, mouse fibulin-2 adhered to human erythroid-megakaryocytic leukaemia cell line HEL. This adhesion was mediated by beta3 integrins. However, HEL cells did not adhere to human fibulin-2. We therefore studied a possible species-specific cell-adhesive activity of mouse fibulin-2 by using mouse megakaryocytes, obtained by culture of BM cells in the presence of thrombopoietin. These megakaryocytes did not adhere to mouse fibulin-2. Our findings suggested that the functional role of fibulin-1 and fibulin-2 in BM stroma is related to binding to the major cell adhesion protein fibronectin, whereas adhesion of mouse fibulin-2 to human cells containing the integrin beta3 chain is not related to an apparent physiological function of the protein.
Integrin-binding and cell-adhesion studies of fibulins reveal a particular affinity for alpha IIb beta 3.
Experimental cell research, 1995; PubMed, Homo sapiens FBLN2 — Homo sapiens ITGB3
ABSTRACT: The extracellular matrix proteins fibulin-1 (variants C and D) and fibulin-2 occur in basement membranes and in vessel walls and are thus potential candidates for cellular interactions. Recombinant forms of these proteins were obtained from stably transfected kidney cell clones and examined for cell-adhesion activity and binding to five different purified integrins. The two variants of mouse fibulin-1 were inactive in all these assays. Mouse fibulin-2, however, bound to alpha IIb beta 3 integrin almost as strongly as fibrinogen, while a lower activity was found for alpha V beta 3 and almost none for alpha 5 beta 1 integrin. Synthetic SVPRGDLDG peptide, corresponding to the single RGD site of mouse fibulin-2, was a strong antagonist of alpha IIb beta 3 integrin binding. Its affinity for alpha V beta 3 and alpha 5 beta 1 integrins was, however, 10- to 50-fold lower compared to GRGDS. Mouse fibulin-2 also promoted adhesion of thrombin-stimulated platelets and of some established cell lines which could be inhibited by RGD peptides. Human fibulin-2, in which the RGD sequence is changed to RSS, bound less strongly to alpha IIb beta 3 integrin and showed no cell-adhesion activity. Together these data suggest a potential role in hemostatic control for mouse fibulin-2 and possibly also for human fibulin-2.