Disease relevance of LTBP2

• Antibodies were generated against recombinant fragment of hLTBP-3 and used to detect the protein and its secretion from cultured COS-7 and osteosarcoma cells [1].
• Additionally, a specific positive immunostaining of LTBP2 was found in the smooth muscle cells of both leiomyomas and myometrium [2].
• Bowes melanoma cells bound most efficiently to LTBP-2 and were used for further characterization [3].

High impact information on LTBP2

• Fibroblasts plated on LTBP-2 and FN substratum exhibited less adherent morphology and displayed clearly decreased actin stress fibers than cells plated on FN [4].
• Quantitative cell adhesion assays indicated that fibroblasts do not adhere to full-length LTBP-2 [4].
• We have analyzed the effects of latent TGF-beta binding protein 2 (LTBP-2) and its fragments on lung fibroblast adhesion [4].
• LTBP-2 had no effects on cells adhering to collagen type I. Fibroblasts adhered weakly to the NH2-terminal fragment of LTBP-2 [4].
• Interestingly, the adhesion-mediating and cytoskeleton-disrupting effects were localized to the same NH2-terminal proline-rich region of LTBP-2 [4].

Chemical compound and disease context of LTBP2

• The attachment of melanoma cells to LTBP-2 was prevented with monoclonal antibody against beta1 integrin in a concentration-dependent manner, suggesting an important role for beta1 integrin in the process [3].

Biological context of LTBP2

• A novel gene, isolated because of structural similarities to fibrillin, was called LTBP2 when its 4.6-kb transcript was found to encode a protein sequence related to the latent TGF-beta binding protein (LTBP1), which is encoded on human chromosome (Chr) 2, region p12-q22 [5].
• We have assigned the human and murine LTBP2 loci to regions of conserved synteny on human Chr 11 and mouse Chr 19 [5].
• The hLTBP-3 gene consists of 28 exons, including one alternatively spliced exon [1].
• We established the identity of the cDNA by sequence comparison (80% identity with human LTBP-2) and by chromosome localization (mouse chromosome 12, band D, a region of conserved synteny with the human LTBP-2 gene) [6].
• We found for the first time that LTBP-2 gene expression in mouse embryos was restricted to cartilage perichondrium and blood vessels, a somewhat surprising result since other LTBP genes are widely expressed in rodent tissues [6].

Anatomical context of LTBP2

• By PCR analysis of somatic cell hybrid DNA and fluorescence in situ hybridization, LTBP2 was mapped to human Chr band 11q12 and Ltbp2 to mouse Chr band 19B [5].
• Human fibroblast libraries were used to isolate cDNA encoding LTBP-2 which was then used to identify LTBP-2 transcripts and to isolate the corresponding LTBP-2 gene [7].
• LTBP-2 may have dual functions as a member of the TGF-beta latent complex and as a structural component of microfibrils [7].
• LTBP-2 is synthesized as a 240-kDa protein by human foreskin fibroblasts and also by COS cells transfected with the isolated LTBP-2 cDNA [8].
• This gene encodes a fish orthologue of the latent transforming growth factor beta binding protein 3 (LTBP-3) and was identified through a differential display approach from a rainbow trout gonad cell line (RTG-2-ERalpha) [9].

Associations of LTBP2 with chemical compounds

• LTBP-2 contains an RGD putative integrin recognition site, suggesting a role in cell adhesion [3].

Other interactions of LTBP2

• While the domain structure of LTBP-2 is similar to that of the other LTBPs, LTBP-2 possesses unique regions that make it the largest member of the LTBP family [7].
• Recombinant latent transforming growth factor beta-binding protein 2 assembles to fibroblast extracellular matrix and is susceptible to proteolytic processing and release [10].
• LTBP-2 also supported Bowes cell migration in modified Boyden chamber assays in a manner similar to the migration on fibronectin [3].

Analytical, diagnostic and therapeutic context of LTBP2

• Expression analyses by real time RT-PCR indicated that the slow appearance of LTBP-3 and -4 was due to the low expression levels soon after subculture [11].
• Immunoblotting analyses of isolated insoluble matrices as well as immunofluorescence analyses and confocal microscopy indicated that both LTBP-3 and -4 get assembled into the ECM [11].

References