EC Number   |
General Information |
Reference |
|---|
   1.14.11.4 | drug target |
normalizing the cross-link pattern by selectively inhibiting LH2 (and thus hydroxy-alpha-aminoadipic acid-delta-semialdehyde cross-linking) alters the balance of collagen degradation. It is expected that this results in reversible fibrosis. Since the up-regulation of LH2 is seen in all organs, a drug that specifically inhibits LH2 activity can be used in a wide range of fibrotic disorders. Since LH2 catalyzes only a single reaction downstream in the fibrogenic cascade (namely the formation of unwanted cross-links in collagen of the fibrotic lesions), little (if any) side-effects are expected, as the deposited collagen in the wound area is expected to be normally modified, and thus have the properties (e.g. with respect to tensile strength) required for a normal function of the repaired tissue |
764615 |
| 1.14.11.4 | drug target |
PLOD2 is a gene of clinical relevance with implications in glioblastoma invasion and treatment strategies. PLOD2 expression is positively correlated with tumor grade and inversely associated with glioblastoma patient prognosis |
765490 |
| 1.14.11.4 | drug target |
the expression level of the procollagen-lysine, 2-oxoglutarate 5-dioxygenase (PLOD) might become a novel biomarker for prognosis and is a potential target for individual treatment decisions in lower-grade glioma (LGG) |
764722 |
| 1.14.11.4 | evolution |
LH3 belongs to the lysyl hydroxylase family of enzymes that has important roles in the biosynthesis of collagen |
725092 |
| 1.14.11.4 | evolution |
the enzyme belongs to the 2-oxoglutarate/Fe2+-dependent oxygenase family |
744168 |
| 1.14.11.4 | evolution |
whereas in animals from sponges to humans the transfer of galactose to hydroxylysine in collagen is conserved, the mimivirus L230 enzyme transfers glucose to hydroxylysine, thereby defining another type of collagen glycosylation in nature. Utilization of glucose instead of the galactose found throughout animals as well as a bifunctional enzyme rather than two separate enzymes may represent a parallel evolutionary track in collagen biology |
-, 725453 |
| 1.14.11.4 | malfunction |
although differential expression of LH2 (long) is associated with fibrotic conditions, there is no direct evidence that the increased Pyr cross-links in the overaccumulated collagen contribute definitively to fibrosis |
699401 |
| 1.14.11.4 | malfunction |
disorders of LH3 with a unique phenotype causing severe morbidity as a result of feauters that overlap with collagen disorders |
695440 |
| 1.14.11.4 | malfunction |
enzyme LH3 downregulation decreases MMP-9 recruitment to MRC-5 and thus MMP-9/LH3 interaction |
745323 |
| 1.14.11.4 | malfunction |
impairment of LH3 function significantly affects type I collagen fibrillogenesis |
-, 725464 |
