3.4.21.46: complement factor D
This is an abbreviated version!
For detailed information about complement factor D, go to the full flat file.
Word Map on EC 3.4.21.46
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3.4.21.46
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angiogenesis
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angiogenic
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vessel
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metastasis
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neovascularization
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hypoxia
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artery
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hypoxia-inducible
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necrosis
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retinal
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antiangiogenic
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umbilical
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bevacizumab
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microvessels
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vein
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capillary
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factor-1
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huvecs
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vegfr-2
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collagen
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vasculature
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retinopathy
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eyes
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ovarian
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macular
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tumour
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tube
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microvascular
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mesenchymal
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anti-vegf
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lymphatic
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receptor-2
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pro-angiogenic
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bfgf
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intravitreal
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progression-free
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edema
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choroid
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metalloproteinase
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endothelium
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hypertension
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sprout
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matrigel
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paracrine
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lymph
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hif-1alpha
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mmp-9
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sunitinib
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drug development
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sorafenib
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vitreous
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medicine
- 3.4.21.46
- angiogenesis
-
angiogenic
- vessel
- metastasis
- neovascularization
- hypoxia
- artery
-
hypoxia-inducible
- necrosis
- retinal
-
antiangiogenic
-
umbilical
-
bevacizumab
-
microvessels
- vein
- capillary
- factor-1
- huvecs
- vegfr-2
- collagen
- vasculature
- retinopathy
- eyes
- ovarian
-
macular
- tumour
- tube
-
microvascular
- mesenchymal
-
anti-vegf
- lymphatic
- receptor-2
-
pro-angiogenic
- bfgf
-
intravitreal
-
progression-free
- edema
- choroid
- metalloproteinase
- endothelium
- hypertension
-
sprout
- matrigel
-
paracrine
- lymph
- hif-1alpha
- mmp-9
- sunitinib
- drug development
- sorafenib
- vitreous
- medicine
Reaction
selective cleavage of Arg-/-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor =
Synonyms
28 kDa protein, adipocyte, Adipsin, alternative complement pathway component Factor D, C3 convertase activator, C3 proactivator convertase, CFD, complement factor D/adipsin and kallikrein-like serine protease, convertase, C3 proactivator, Df, Df protein, endogenous vascular elastase, esterase, properdin factor D, factor D, factor D (complement), fD, PDGF-D, platelet-derived growth factor D, PoDAK, vascular endothelial growth factor, vascular endothelial growth factor D, VEGF-D
ECTree
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General Information
General Information on EC 3.4.21.46 - complement factor D
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malfunction
metabolism
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in humans neither MASP-1 nor MASP-3 are required for alternative pathway function. During MASP-1/-3 deficiency significant alternative pathway activity remains, indicating that mature factor D is present in the absence of MASP-1/-3
physiological function
additional information
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deficiency of factor D leads to exacerbated liver injury and inflammatory cells. The absence of Factor D and lack of C3b/iC3b/C3c deposition following CCl4-induced injury is associated with more severe and prolonged liver injury
malfunction
knockdown of complement factor D in senescent fibroblasts significantly reduces the increase of matrix metalloproteinase 1 in the co-cultured young fibroblasts
malfunction
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deficiency of factor D leads to exacerbated liver injury and inflammatory cells. The absence of Factor D and lack of C3b/iC3b/C3c deposition following CCl4-induced injury is associated with more severe and prolonged liver injury
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in total 150 gastric cancer patients who underwent radical gastrectomy are analyzed (75 cases presented with hepatic metastases and 75 cases presented without any recurrences). Significant association is shown between VEGF-D expression and hepatic metastasis from gastric cancer after radical gastrectomy
physiological function
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interleukin-7/interleukin-7R induce VEGF-D up-regulation and promote lymphangiogenesis via c-Fos/c-Jun pathway in lung cancer
physiological function
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PDGF-D plays an important role in breast tumor aggressiveness and this process is mechanistically linked with the activation of Notch and NF-kappaB signaling
physiological function
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serum VEGF-D levels are greater in patients with lympangioleiomyomatosis with lymphatic involvement
physiological function
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alternative complement pathway component Factor D contributes to efficient clearance of tissue debris following acute CCl4-induced injury in the liver. Acute toxic injury to the liver results in the death of hepatocytesby necrosis and apoptosis. If removal of damaged tissue is inadequate and injury persists, reorganization of the extracellular matrix is impaired
physiological function
human factor D is a self-inhibited thrombin-like serine proteinase that is critical for amplification of the complement immune response
physiological function
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mature factor D is required for the alternative complement pathway
physiological function
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targeting of the enzyme's exosite causes inhibition of the pathway complement activation
physiological function
targeting of the enzyme's exosite causes inhibition of the pathway complement activation
physiological function
enzyme overexpression promotes adipocyte differentiation, increasesC3a production, and leads to induction of C3a receptor target gene expression
physiological function
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the enzyme is involved in immune responses in rock bream. The enzyme is vital to alternative complement pathway activation in cleaving complement factor B. This catalytic reaction forms the alternative C3 convertase that is crucial for complement-mediated pathogenesis
physiological function
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the enzyme protects mice from ethanol-induced inflammation and liver injury. The enzyme contributes to the maintenance of tissue homeostasis during chronic ethanol by facilitating the clearance of apoptotic cells
physiological function
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the enzyme shows antimicrobial activity against both gram-positive bacteria like Staphylococcus aureus and gram-negative bacteria like Aeromonas hydrophila
physiological function
treatment of young fibroblasts with complement factor D results in increased matrix metalloproteinase 1 gene expression
physiological function
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alternative complement pathway component Factor D contributes to efficient clearance of tissue debris following acute CCl4-induced injury in the liver. Acute toxic injury to the liver results in the death of hepatocytesby necrosis and apoptosis. If removal of damaged tissue is inadequate and injury persists, reorganization of the extracellular matrix is impaired
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influence of buffer composition on the activity of the alternative pathway of complement activation in mice in the presence and the absence of the Masp1 gene products, overview
additional information
the substrate-binding, or exosite, region displays a well defined and rigid conformation. A salt bridge between Arg202 on the self-inhibitory loop and Asp177 locks the S1 pocket and rigidifies the exosite. Asp-His-Ser catalytic site. The enzyme exhibits conformational dynamics like thrombin, but unlike in thrombin a mechanism has evolved in factor D that locks the unbound native state into an ordered inactive conformation via the self-inhibitory loop. The Asp-His-Ser catalytic site of the enzyme is in an enzymatically active conformation induced by substrate binding at the exosite
additional information
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the substrate-binding, or exosite, region displays a well defined and rigid conformation. A salt bridge between Arg202 on the self-inhibitory loop and Asp177 locks the S1 pocket and rigidifies the exosite. Asp-His-Ser catalytic site. The enzyme exhibits conformational dynamics like thrombin, but unlike in thrombin a mechanism has evolved in factor D that locks the unbound native state into an ordered inactive conformation via the self-inhibitory loop. The Asp-His-Ser catalytic site of the enzyme is in an enzymatically active conformation induced by substrate binding at the exosite