The growth arrest-specific 6 gene (GAS6) is a member of the family of plasma vitamin K-dependent proteins, which are able to bind to phospholipids using an N-terminal gamma-carboxyglutamic acid domain. GAS6 is a vitamin K-dependent protein, plays a role in the survival, proliferation, migration, differentiation, adhesion, and apoptosis of cells. The growth arrest-specific 6 (GAS6) has been implicated in systemic inflammation and coagulation. Growth arrest-specific 6 (GAS6), plays a role in tumor progression by regulating growth in many cancers. GAS6, expressed by osteoblasts in the bone marrow, plays a significant role in the regulation of PCa cell survival during chemotherapy, which will have important implications for targeting metastatic disease. The GAS6/TYRO3-AXL-MERTK (TAM) signaling pathway is essential for full and sustained platelet activation, as well as thrombus stabilization. Inhibition of this pathway decreases platelet aggregation, shape change, clot retraction, aggregate formation under flow conditions, and surface expression of activation markers. It had been show that GAS6 signaling regulates invasion, proliferation, chemotherapy-induced apoptosis of prostate cancer (PCa) cells, and GAS6 secreted from osteoblasts in the bone marrow environment plays a critical role in establishing prostate tumor cell dormancy.
WAP , kazal , immunoglobulin , kunitz and NTR domain-containing protein 2 , also known as Growth and differentiation factor-associated serum protein 1 , WAP , follistatin , immunoglobulin , kunitz and NTR domain-containing-related protein , WFIKKN-related protein , WFIKKN2 and GASP1 , is a secreted protein that belongs to the WFIKKN family. WFIKKN2 contains two BPTI/Kunitz inhibitor domains , one Ig-like C2-type (immunoglobulin-like) domain , one Kazal-like domain , one NTR domain and one WAP domain. WFIKKN2 is primarily expressed in ovary , testis and brain , but not in liver. In fetal tissues , it is primarily expressed in brain , skeletal muscle , thymus and kidney. WFIKKN2 is a protease-inhibitor that contains multiple distinct protease inhibitor domains. It probably has serine protease-and metalloprotease-inhibitor activity. It inhibits the biological activity of mature myostatin , but not activin. WFIKKN2 protein binds mature GDF8/myostatin and myostatin propeptide and inhibits the biological activity of myostatin.
Gastric intrinsic factor, also known as GIF, belongs to the of the cobalamin transport protein family. It is a glycoprotein produced by the parietal cells of the stomach. Gastric intrinsic factor plays a key role in the absorption of vitamin B12 on in the small intestine. Vitamin B12 bounds to haptocorrin after entry into the stomach. The resulting complex enters the duodenum, where pancreatic enzymes digest haptocorrin. In the less acidic environment of the small intestine, B12 can then bind to gastric intrinsic factor. This new complex travels to the ileum, where special epithelial cells endocytose them. Inside the cell, B12 dissociates once again and binds to another protein, transcobalamin II. The new complex can exit the epithelial cells to enter the liver.
This gene encodes gastric lipase, an enzyme involved in the digestion of dietary triglycerides in the gastrointestinal tract, and responsible for 30% of fat digestion processes occurring in human. It is secreted by gastric chief cells in the fundic mucosa of the stomach, and it hydrolyzes the ester bonds of triglycerides under acidic pH conditions. The gene is a member of a conserved gene family of lipases that play distinct roles in neutral lipid metabolism. Several transcript variants encoding different isoforms have been found for this gene.
Gastric Triacylglycerol Lipase (LIPF) belongs to the AB hydrolase superfamily. LIPF is an important lipase during the digestion of dietary lipids in cystic fibrosis. LIPF is involved in the digestion of dietary triglycerides in the gastrointestinal tract, and responsible for 30% of fat digestion processes occurring in human. LIPF is secreted by gastric chief cells in the fundic mucosa of the stomach, and it hydrolyzes the ester bonds of triglycerides under acidic pH conditions. LIPF acts distinct roles in neutral lipid metabolism.
Cytosolic beta-glucosidase, also known as Cytosolic beta-glucosidase-like protein 1, GBA3, CBG and CBGL1 is a cytoplasm protein which belongs to theglycosyl hydrolase 1 family and Klotho subfamily. GBA3 / CBGL1 is a glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. GBA3 / CBGL1 is present in small intestine (at protein level). GBA3 / CBGL1 is expressed in liver, small intestine, colon, spleen and kidney. GBA3 / CBGL1 is down-regulated in renal cell carcinomas and hepatocellular carcinomas. GBA3 / CBGL1 is able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. GBA3 / CBGL1 possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.
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