Disease relevance of Fbln2

• In this study, we cloned the extreme 5' end of the mouse fibulin-2 cDNA, isolated phage and cosmid clones encoding the entire gene, and functionally characterized the promoter [1].

High impact information on Fbln2

• Fragments alpha2LG1-3 and alpha2LG4-5 also bound to fibulin-1, fibulin-2 and nidogen-2 with Kd = 13-150 nM [2].
• Endostatins and NC1 showed a comparable binding activity for the microfibrillar fibulin-1 and fibulin-2, and for heparin [3].
• Furthermore, a Cys574-Ser mutation abolished disulfide connection but not non-covalent dimerization of fibulin-2 [4].
• Production of the fibulin-2 was demonstrated by Northern blots and radioimmunoassay in fibroblasts but not in several tumor cell lines [5].
• The latter studies also demonstrated an extracellular localization for fibulin-2 in basement membranes and other connective tissue compartments [5].

Biological context of Fbln2

• We also show that fibulin-2 mRNA and protein remained highly expressed during organogenesis in tissues derived from neural crest mesenchyme [6].
• A very prominent expression of fibulin-2 was seen during early stages of chondrogenesis in all cartilages analyzed [6].
• We used in situ hybridization and immunofluorescence staining to examine the expression of fibulin-1 and fibulin-2 during mouse embryogenesis [6].
• The NH2-terminal 408 residues, unique to fibulin-2, showed no sequence homology to other known proteins and presumably form two additional domains that differ in their cysteine content [5].
• No significant immunological cross-reaction could be detected between fibulin-1 and fibulin-2 [5].

Anatomical context of Fbln2

• Fibulin-2 and fibulin-5 alterations in tsk mice associated with disorganized hypodermal elastic fibers and skin tethering [7].
• The increased elastic fibers in Tsk hypodermal connective tissue was associated with increased fibrillin-1 and fibulin-2 matrices [7].
• In addition, a locally restricted expression pattern of fibulin-1 and fibulin-2 mRNA and protein at sites of epithelial-mesenchymal interactions was detected in two tissues, the developing tooth and hair follicles [6].
• A similar proteolysis was also observed for fibulin-2 deposited by cultured fibroblasts into a dense fibrillar network [8].
• Fibulin-1 and fibulin-2 are two novel rod-like proteins which occur either in basement membranes or in interstitial fibrils in close association with fibronectin [8].

Associations of Fbln2 with chemical compounds

• Synthetic SVPRGDLDG peptide, corresponding to the single RGD site of mouse fibulin-2, was a strong antagonist of alpha IIb beta 3 integrin binding [9].
• Dexamethasone treatment led to a decreased expression of tenascin-C in healing wounds but had no effect on fibulin-2 expression [10].
• Metabolic labelling and pulse-chase studies demonstrated fibulin-2 oligomers in detergent extracts of cells and their rapid translocation to extracellular EDTA-sensitive assembly forms [11].
• Most of the fibroblast fibulin-2 is deposited into a dense fibrillar meshwork which requires treatment with EDTA and/or 6 M urea for solubilization [11].

Other interactions of Fbln2

• Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by matrix metalloproteinases and other tissue proteases [8].
• Fibulin-1 and fibulin-2 are extracellular matrix proteins with unique structural features [6].
• During healing of cutaneous wounds, deposition of collagen I, fibulin-2, and nidogen is identical in mutant and wild-type mice [12].

Analytical, diagnostic and therapeutic context of Fbln2

• By Northern blots we confirm that expression of fibulin-2 is particularly high in the developing and newborn heart [6].
• A new protein, fibulin-2, was predicted from sequence analysis of cDNA clones obtained from a mouse fibroblast library [5].
• Fibulin-2 protein levels were also studied by Western blotting during rat aortic SMC phenotypic modulation in vitro [13].
• METHODS: Presence of fibulin-2 was analysed by immunohistochemistry in atherosclerotic aortas and in mechanically injured carotid arteries from mice [13].
• Unlike for fibronectin and fibulin-1 only a little fibulin-2 was found in the cell culture medium [11].

References