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.
Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe2+ to Fe3+ without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu2+ ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense. Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:604290]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
Chitinase-3-like protein 1 (CHI3L1) is a secreted heparin-binding glycoprotein whose expression is associated with vascular smooth muscle cell migration. CHI3L1 is expressed at high levels in postconfluent nodular VSMC cultures and at low levels in subconfluent proliferating cultures. CHI3L1 is a tissue-restricted, chitin-binding lectin and member of glycosyl hydrolase family 18. In contrast to many other monocyto / macrophage markers, its expression is absent in monocytes and strong induced during late stages of human macrophage differentiation. Elevated levels of CHI3L1 are associated with disorders exhibiting increased connective tissue turnover, such as rheum atoid, arthritis, osteoarthritis, scleroderma, and cirrhosis of liver, but is produced in cartilage from old donors or patiens with osteoarthritis. CHI3L1 is abnormally expressed in the hippocampus of subjects with schizophrenia and may be involved in the cellular response to various environmental events that are reported to increase the risk of schizophrenia.
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