Hormone regulating the release of corticotropin from pituitary gland. Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile.
Cripto/TDGF1 is a member of the epidermal growth factor (EGF)-Cripto , Frl-1 , and Cryptic (CFC) family. EGF-CFC family member proteins share a variant EGF-like motif , a conserved cysteine-rich domain , and a C-terminal hydrophobic region. Before gastrulation , Cripto is asymmetrically expressed in a proximal–distal gradient in the epiblast , and subsequently is expressed in the primitive streak and newly formed embryonic mesoderm. These proteins play key roles in intercellular signaling pathways during vertebrate embryogenesis. Mutations in Cripto/TDGF1 can cause autosomal visceral heterotaxy. Cripto/TDGF1 is involved in left-right asymmetric morphogenesis during organ development. Cripto signalling is essential for the conversion of a proximal–distal asymmetry into an orthogonal anterior–posterior axis. The mechanism of inhibitory effects of the Cripto includes both cancer cell apoptosis , activation of c-Jun-NH(2)-terminal kinase and p38 kinase signaling pathways and blocking of Akt phosphorylation. Thus , Cripto is a unique target , and Immunohistochemistry to Cripto could be of therapeutic value for Human cancers.
Cysteine-rich secretory protein 3 (CRISP-3) is a secreted protein,containing 1 SCP domain and 1 ShKT domain.It is belongs to the CRISP family. CRISP-3 is a glycoprotein that belongs to the family of cysteine-rich secretory proteins (CRISPs) which was originally discovered in human neutrophilic granulocytes. CRISP-3 is also widely distibuted in exocrine glands (salivary glands, pancreas and prostate), eosinophilic granulocytes and to a lower level in epididymis, ovary, thymus and colon. The presence of CRISP-3 in neutrophils, eosinophils and in exocrine secretions indicates a role in innate host defense. The antibody has been raised against recombinant C-terminally truncated form of CRISP-3 and recognizes both the N-glycosylated and non-glycosylated form of the mature protein.
Carnitine octanoyltransferase (CROT or COT), also known as octanoyl-CoA: L-carnitine O-octanoyltransferase, medium-chain/long-chain carnitine acyltransferase, and carnitine medium-chain acyltransferase, is a carnitine acyltransferase belonging to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. Carnitine octanoyltransferase (CROT or COT) facilitate the transport of medium- and long-chain fatty acids through the peroxisomal and mitochondrial membranes. It is physiologically inhibited by malonyl-CoA. COT also has functions in efficiently converting one of the end products of the peroxisomal beta-oxidation of pristanic acid, 4, 8-dimethylnonanoyl-CoA, to its corresponding carnitine ester.
C-reactive protein (CRP) is synthesized by the liver in response to factors released by fat cells. It is a member of the pentraxin family of proteins. The levels of CRP rise in response to inflammation. Human C-reactive protein (CRP) is the classical acute phase reactant, the circulating concentration of which rises rapidly and extensively in a cytokine-mediated response to tissue injury, infection and inflammation. Serum CRP values are routinely measured, empirically, to detect and monitor many human diseases. However, CRP is likely to have important host defence, scavenging and metabolic functions through its capacity for calcium-dependent binding to exogenous and autologous molecules containing phosphocholine (PC) and then activating the classical complement pathway. CRP may also have pathogenic effects and the recent discovery of a prognostic association between increased CRP production and coronary atherothrombotic events is of particular interest.
Cytotoxic and Regulatory T-Cell Molecule (CRTAM) is a member of Nectin family under the immunoglobulin superfamily that is expressed by activated CD8+ and NK T cells. CRTAM is found in spleen, thymus, small intestine, peripheral blood, and it is highly expressed by Purkinje cells of the cerebellum. CRTAM is a type I transmembrane glycoprotein containing one Ig-like C2-type domain and one Ig-like V-type domain in its extracellular domain, while its cytoplasmic region shows a potential class I PDZ domain. CRTAM is expressed as a homodimer on the cell surface but does not show homotypic binding in trans. The high affinity of CRTAM/IGSF4 adhesion allows CRTAM to disrupt IGSF4 homotypic interactions. IGSF4 and T cell receptor coengagement of CD8+ cells expressiong CRTAM induces increased IFNγ or IL-22 production.
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