Coagulation factor IX, also known as Christmas factor, Plasma thromboplastin component and PTC, is a secreted protein which belongs to the peptidase S1 family. Coagulation factor IX / F9 contains two EGF-like domains, one Gla (gamma-carboxy-glutamate) domain and one peptidase S1 domain. Coagulation factor IX / F9 is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ons, phospholipids, and factor VIIIa. Defects in Coagulation factor IX / F9 are the cause of thrombophilia due to factor IX defect which is a hemostatic disorder characterized by a tendency to thrombosis. Defects in Coagulation factor IX / F9 are also the cause of recessive X-linked hemophilia B ( HEMB ) which also known as Christmas disease.
Mouse coagulation factor X / F10 a member of the peptidase S1 family. The mature F10 is composed mostly of two EGF-like domains, one Gla gamma-carboxy-glutamate domain and one peptidase S1 domain. Factor Xa is a vitamin K-dependent plasma protease that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. The two chains of F10 are formed from a single-chain precursor by the excision of two Arg residues. A single-chain precursor is initially synthesized in the liver. The light and heavy chains are linked together by disulfide bonds. The light chain contains a Gla and two EGF-like domains. The heavy chain corresponds to the serine protease domain. It can form a heterodimer with SERPINA5.
Endostatin, an endogenous non-glycosylated inhibitor of endothelial cell proliferation and angiogenesis. It is produced and/or trimmed by metalloproteinases such as MMP-2 and MMP-9, and cathepsins S, B and L. The N-terminal ~27 aa of Endostatin appear to contain the majority of its activity. This region contains zinc binding sites that are thought to be critical for its anti-endothelial and anti-tumor effects, as well as multiple cleavage sites that, when used, can modify its activity. Mouse Endostatin shares 96% aa sequence identity with rat and 85-87% with human, bovine and equine Endostatin. It is predominantly expressed in liver, kidney, lung, skeletal muscle and testis. Endostatin inhibits endothelial cell growth by inducing cell cycle arrest in G1 phase and initiating apoptosis. It is also thought to down-regulate angiogenesis by blocking VEGF-induced endothelial cell migration. Endostatin may also be involved with down-regulation of angiogenesis after establishment of placental circulation in the pregnant uterus.
Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.
COLEC10 is a member of the C-lectin family. Members of this family possess collagen-like sequences and carbohydrate recognition domains. The other members of this family are secreted proteins and bind to carbohydrate antigens on microorganisms facilitating their recognition and removal. This gene product is a cytosolic protein, a characteristic that suggests that it may have different biological functions than other C-lectins.
Collagen alpha-1(III) chain（Col3a1） is a secreted protein and belongs to the fibrillar collagen family.It contains 1 fibrillar collagen NC1 domain and 1 VWFC domain. Collagen alpha-1(III) chain is a fibrillar collagen that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. The COL3A1 gene produces the components of type III collagen, called pro-alpha1(III) chains. Three copies of this chain combine to make a molecule of type III procollagen. These triple-stranded, rope-like procollagen molecules must be processed by enzymes outside the cell to remove extra protein segments from their ends. Once these molecules are processed, the collagen molecules arrange themselves into long, thin fibrils. Within these fibrils, the individual collagen molecules are cross-linked to one another. These cross-links result in the formation of very strong mature type III collagen fibrils, which are found in the spaces around cells.
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