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knockdown of LTBP2 inhibits invasion and tumorigenesis in thyroid carcinoma cells.
We identified one nonsense mutation (c.2421G>A, p.W807X) in LTBP2 in eight Indian families. Among the mutations identified W807X in LTBP2 represent novel mutations.
LTBP-1 (show LTBP1 Proteins) and LTBP-2 are involved in the keratinization of oral epithelium.
The results showed that no deleterious mutations were found in coding regions of LTBP2 in patients with PCG, suggesting that it is not a causal gene for primary congenital glaucoma in the Han Chinese population.
LTBP-2 and FGF-2 (show FGF2 Proteins) are co-localized in fibrotic human keloid and hypertrophic scar.
LTBP-2 is a potent inhibitor of FGF-2 (show FGF2 Proteins) that may influence FGF-2 (show FGF2 Proteins) bioactivity during wound repair particularly in fibrotic tissues.
LTBP2 was able to reduce phosphorylation of p65 (show GORASP1 Proteins) at Serine 536, inhibit nuclear localization of active phosphorylated p65 (show GORASP1 Proteins), and impair the p65 (show GORASP1 Proteins) DNA-binding ability. This results in a consequential down-regulation of p65 (show GORASP1 Proteins)-related gene expression.
LTBP-2 is an essential component for the formation of microfibril bundles in ciliary zonules.
perlecan (show HSPG2 Proteins) HS was not essential for latent transforming growth factor-beta-1 (show TGFB1 Proteins) binding protein-2 deposition
Overall the results indicate that LTBP-2 may have a negative regulatory role during elastic fiber assembly, perhaps in displacing elastin (show ELN Proteins) microassemblies from complexes with fibulin-5 (show FBLN5 Proteins) and/or cell surface heparan sulfate proteoglycans.
Latent transforming growth factor beta-binding proteins-2 and -3 inhibit the proprotein convertase 5 (show PCSK5 Proteins)/6A.
These results suggest a novel regulatory mechanism of elastic fiber assembly in which LTBP-2 regulates targeting of DANCE on suitable microfibrils to form elastic fibers.
This is the first study to investigate the expression and localization of fibrillin proteins and latent TGF-beta (show TGFB1 Proteins) binding proteins affecting TGFbeta (show TGFB1 Proteins) bioavailability in the ovary.
The protein encoded by this gene belongs to the family of latent transforming growth factor (TGF)-beta binding proteins (LTBP), which are extracellular matrix proteins with multi-domain structure. This protein is the largest member of the LTBP family possessing unique regions and with most similarity to the fibrillins. It has thus been suggested that it may have multiple functions: as a member of the TGF-beta latent complex, as a structural component of microfibrils, and a role in cell adhesion.
latent transforming growth factor beta binding protein 2
, latent transforming growth factor beta binding protein 3
, latent transforming growth factor-beta binding protein 3
, latent-transforming growth factor beta-binding protein 2-like
, latent-transforming growth factor beta-binding protein 2
, LTBP-2 like protein
, latent-transforming growth factor beta-binding protein 3