EC Number   |
General Information |
Reference |
|---|
   1.14.11.7 | malfunction |
silencing PHD3 leads to a significant decrease in TNF-alpha-induced expression of catabolic markers that include ADAMTS5, syndecan4, MMP13, and COX2, and at the same time, there is restoration of aggrecan and collagen type II expression |
727931 |
| 1.14.11.7 | malfunction |
type I collagen extracted from tendon, skin, and bone of wild type and prolyl 3-hydroxylase 1 (P3H1) null mice show distinct patterns of 3-hydroxylation and glycosylation of hydroxylysine residues. The D-period of collagen fibrils is not affected by the lack of 3-hydroxyproline or increasing amounts of hydroxylysine glycosylation. Only small differences are seen in the fibril diameter of newborn mice tail tendons as compared with the severe disorganization found in adult P3H1 null mice, implicating the lateral growth of fibrils in the phenotype |
727956 |
| 1.14.11.7 | more |
importance of P3H1 to bone structure and development. Mutations in the gene encoding for prolyl 3-hydroxylase 1 can cause a severe, recessive form of osteogenesis imperfecta, a skeletal disorder, minimal 3-hydroxylation of key proline residues in type I collagen as a result of P3H1 deficiency. Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones, e.g. abnormalities in collagen fibril ultrastructure in tendons, and alterations in skin architecture, as well as in developing limbs, phenotypes, detailed overview. Collagen secretion rate is decreased in P3H1 null fibroblasts |
712433 |
| 1.14.11.7 | more |
PHD3 upregulation contributes to doxorubicin-induced apoptosis in H9c2 cells. Overexpression of PHD3 counteracts the formation of the BaxBcl-2 complex, the BH4 domain of anti-apoptosis protein Bcl-2 is required for its interaction with PHD3. BaxBcl-2 complex formation is significantly reduced in apoptotic H9c2 cells in which PHD3 is overexpressed compared to the apoptotic H9c2 cells with native PHD3 levels |
711115 |
| 1.14.11.7 | physiological function |
by positively controlling NF-kappaB signaling activity, PHD3 promotes the catabolic effects of the inflammatory cytokines on nucleus pulposus cells |
727931 |
| 1.14.11.7 | physiological function |
cartilage associated protein (CRTAP) and prolyl 3-hydroxylase 1 (P3H1) , together with cyclophilin B, form a complex that 3-hydroxylates a single proline residue on the alpha1(I) chain (Pro986) and has cis/trans isomerase (PPIase) activity essential for proper collagen folding. Prolyl 3-hydroxylation of Pro986 is not required for the structural stability of collagen. P3H1 and CRTAP stabilize each other and absence of one results in degradation of the other |
746168 |
| 1.14.11.7 | physiological function |
P3H2 is involved in formation of new vessels. The enzyme catalyzes the post-translational formation of 3-hydroxyproline on collagens, mainly on type IV. Through its activity on type IV collagen, the enzyme is essential for angiogenesis properties of endothelial cells in vitro by performing experiments of gain- and loss-of-function. Overexpression of P3H2 induces a more condensed status of Collagen IV, accompanied by an alignment of the cells along the Collagen IV bundles, so towards an evident pro-angiogenic status |
764921 |
| 1.14.11.7 | physiological function |
role for prolyl 3-hydroxylase-2, P3H2, in collagen IV prolyl 3-hydroxylation. Collagen IV is found in many tissues in the eye, including lens capsule, epidermal and endodermal membranes of the cornea, and the inner limiting membrane and Bruchs membrane of the retina |
745337 |
| 1.14.11.7 | physiological function |
role of PHD3 in the apoptosis of cardiac myocytes. PHD3 promotes the apoptosis of H9c2 cells via an interaction with the BH4 domain of Bcl-2, it affects the formation of the BaxBcl-2 complex |
711115 |
| 1.14.11.7 | physiological function |
role of prolyl 3-hydroxylation in type IV collagen. Subendothelial collagens bear platelet-specific glycoprotein VI, GPVI, binding sites that initiate platelet aggregation upon blood exposure during injuries. In type IV collagen, these sites are normally 3-hydroxylated. Prolyl 3-hydroxylation of type IV collagen has an important function preventing maternal platelet aggregation in response to the early developing embryo. 3-Hydroxylation of type IV collagen is indispensable for embryonic development in mice |
746295 |
