Cerebral Dopamine Neurotrophic Factor (CDNF), also known as ARMETL1 (ARMET-like protein 1), is a secreted protein with eight conserved cysteine residues, predicting a unique protein fold and defining a new, evolutionarily conserved protein family. CDNF is a novel neurotrophic factor with strong trophic activity on dopaminergic neurons comparable to that of glial cell line-derived neurotrophic factor (GDNF). CDNF/ARMETL1 is a evolutionary conserved protein which can protect and restore the function of dopaminergic neurons in the rat model of Parkinson's disease, suggesting that CDNF might be beneficial for the treatment of Parkinson's disease. CDNF is widely expressed in neurons in several brain regions including cerebral cortex, hippocampus, substantia nigra, striatum and cerebellum. Human CDNF is glycosylated and secreted from transiently transfected cells. CDNF promotes the survival, growth, and function of dopamine-specific neurons and is expressed in brain regions that undergo cocaine-induced neuroplasticity.
Cysteine Dioxygenase Type 1 (CDO1) is a mammalian non-heme iron enzyme that belongs to the cysteine dioxygenase family. CDO1 is highly expressed in the liver and placenta, and has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels.
CDO (CAMrelated/down-regulatedby oncogenes) is a member of the Immunoglubulin (Ig) superfamily, Ig/Fibronectin (FN)type III repeat family of cell surface proteins. Human CDO is a type I transmembrane (TM) glycoprotein. It is synthesized as a 1287 amino acid (aa) precursorthat contains a 25 aa signal sequence, a 938 aa extracellular domain (ECD), a 21 aa TM segment and a 303 aa cytoplasmic region. The ECD contains five C2-typeIglikedomains, followed by three FN type III repeats. The ECD of human CDO is 85% aa identical to mouse CDO ECD.CDO is found on muscle precursor and neural progenitor cells of the embryo. It likely promotes muscle differentiation, and contributes to axon guidance andneuronal patterning.
The carcinoembryonic-antigen-related cell-adhesion molecule (CEACAM) family of proteins has been implicated in various intercellular-adhesion and intracellular-signalling-mediated effects that govern the growth and differentiation of normal and cancerous cells. CEACAM1 , also known as biliary glycoprotein I (BGP I) and CD66a , is a member of the carcinoembryonic antigen (CEA) gene family which belongs to the immunoglobulin superfamily. The highly glycosylated CEACAM1 contains one N-terminal V-type Ig-like domain and three C2-type Ig-like domains within its ECD , and one ITIM motif and a calmodulin binding site in the cytoplasmic region. CEACAM1 is a surface glycoprotein expressed on various blood cells , epithelial cells , and vascular cells. It was described as an adhesion molecule mediating cell adhesion via both homophilic and heterophilic manners , and was detected on leukocytes , epithelia , and endothelia. Studies have revealed that CEACAM1 performs actions in multiple cellular processes including tissue differentiation , angiogenesis , apoptosis , metastasis , as well as the modulation of innate and adaptive immune responses.
The carcinoembryonic-antigen-related cell-adhesion molecule (CEACAM) family of proteins has been implicated in various intercellular-adhesion and intracellular-signalling-mediated effects that govern the growth and differentiation of normal and cancerous cells. CEACAM1, also known as biliary glycoprotein I (BGP I) and CD66a, is a member of the carcinoembryonic antigen (CEA) gene family which belongs to the immunoglobulin superfamily. The highly glycosylated CEACAM1 contains one N-terminal V-type Ig-like domain and three C2-type Ig-like domains within its ECD, and one ITIM motif and a calmodulin binding site in the cytoplasmic region. CEACAM1 is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. It was described as an adhesion molecule mediating cell adhesion via both homophilic and heterophilic manners, and was detected on leukocytes, epithelia, and endothelia. Studies have revealed that CEACAM1 performs actions in multiple cellular processes including tissue differentiation, angiogenesis, apoptosis, metastasis, as well as the modulation of innate and adaptive immune responses.
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 (CEACAM1) is a member of the Carcinoembryonic Antigen (CEA) family, which belongs to the immunoglobulin superfamily. CEACAM1 is originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it is found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. CEACAM1 mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. In addition, CEACAM1 plays a important role in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses.
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