Probable serine carboxypeptidase CPVL, also known as Carboxypeptidase, vitellogenic-like, Vitellogenic carboxypeptidase-like protein, is a member of the peptidase S10 family. It is expressed in macrophages but not in other leukocytes. And specifically, it is abundantly expressed in heart and kidney, also expressed in spleen, leukocytes, and placenta. This enzyme may be involved in the digestion of phagocytosed particles in the lysosome, and also participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.
Cellular retinoic acid-binding protein 2, also known as Cellular retinoic acid-binding protein II, CRABP-II and CRABP2, is a protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The predicted amino acid sequences of human CRABP1 and CRABP2 demonstrated a 99.3% and 93.5% identity to mouse CRABP1 and CRABP2, respectively. CRABP2 forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Expression of CRABP2, but not CRABP1 mRNA, was markedly increased (greater than 15-fold) by retinoic acid treatment of fibroblasts cultured from human skin, whereas no significant induction of CRABP2 mRNA was observed in human lung fibroblasts. CRABP2 transports retinoic acid to the nucleus. It regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is necessary for elastin induction by All-trans retinoic acid (ATRA) in MRC-5 cells. It is expressed at low levels in emphysema fibroblasts. This alteration in the retinoic acid signalling pathway in lung fibroblasts may contribute to the defect of alveolar repair in human pulmonary emphysema.
Death Domain-Containing Protein CRADD (CRADD) is widely expressed in most tissues; with particularly high expression in the adult heart; testis; liver; skeletal muscle; fetal liver; and kidney. CRADD contains one CARD domain that mediates the interaction with caspase-2; and one death domain involved in the binding of RIP protein. CRADD functions as an apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. CRADD induces cell apoptosis/cell death in numerous tissues. Defects in CRADD will result in mental retardation.
Death domain-containing protein CRADD; also known as Caspase and RIP adapter with death domain; RIP-associated protein with a death domain; CRADD and RAIDD; is a protein which is constitutively expressed in most tissues; with particularly high expression in adult heart; testis; liver; skeletal muscle; fetal liver and kidney. CRADD / RAIDD contains oneCARD domain and onedeath domain. CRADD / RAIDD contains a death domain involved in the binding of RIP protein. The CARD domain mediates the interaction with caspase-2. FADD / MORT1 is a death domain (DD)-containing adaptor / signaling molecule that interacts with the intracellular DD of FAS / APO-I ( CD95 ) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 ( Mch5 / MACH / FLICE). CRADD / RAIDD has a dual-domain structure similar to that of FADD. CRADD / RAIDD has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD / RAIDD could play a role in regulating apoptosis in mammalian cells. CRADD / RAIDD is a apoptotic adaptor molecule specific for caspase-2 and FASL / TNF receptor-interacting protein RIP. In the presence of RIP and TRADD; CRADD / RAIDD recruits caspase-2 to the TNFR-1 signalling complex.
Creatine kinase B-type (CKB) belongs to the ATP:guanido phosphotransferase family. It has dimer of identical or non-identical chains with MM being the major form in skeletal muscle and myocardium. MB exists in myocardium, and BB exists in many tissues, especially brain. CKB reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. Clinically, creatine kinase is assayed in blood tests as a marker of myocardial infarction (heart attack), rhabdomyolysis (severe muscle breakdown), muscular dystrophy, autoimmune myositides and acute renal failure.
Creatine kinase M-type is also known as Creatine kinase M chain,M-CK. It is a protein that in humans is encoded by the CKM gene. It belongs to the ATP:guanido phosphotransferase family,containing 1 phosphagen kinase C-terminal domain and 1 phosphagen kinase N-terminal domain. Creatine kinase M-type can reversibly catalyzes the transfer of phosphate between ATP and various phosphogens. It plays a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
CREB3L1, also known as OASIS, is a cellular transcription factor synthesized as a membrane-bound precursor. It is a putative endoplasmic reticulum (ER) stress sensor in astrocytes with a mechanism of activation. OASIS mRNA expression was detected in pancreatic β-cell lines and rodent islets, and the expression level was up-regulated by ER stress-inducing compounds. CREB3L1 may have a role in pancreas development. CREB3L1 may also play an important role in limiting virus spread by inhibiting proliferation of virus-infected cells. In vitro, CREB3L1 binds to box-B element, cAMP response element (CRE) and CRE-like sequences, and activates transcription through box-B element but not through CRE. It may play a role in gliosis.
The cyclic AMP responsive element-binding protein 3-like 4 (CREB3L4) is a transcription factor highly expressed in multiple human cancers. This study aimed to investigate the regulatory effects of CREB3L4 on GC progression and angiogenesis. CREB3L4 was overexpressed in GC tissues and cell lines, and was positively correlated with advanced tumor stage and poor survival in GC patients. The upregulation of CREB3L4 in GC cells increased cell viability, promoted cell proliferation, reduced apoptosis, enhanced cell migration and invasion, and induced the formation of tubule-like endothelial structures, whereas CREB3L4 knockdown impeded tumor cell growth, attenuated cell motility, and prevented human umbilical vein endothelial cells from forming tubule-like structures. In addition, mice inoculated with CREB3L4-deficient GC cells showed significantly suppressed tumor growth compared to the group harboring wild-type tumors.
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