Ectonucleotide pyrophosphatase / phosphodiesterase family member 7, also known as Alkaline sphingomyelin phosphodiesterase, Intestinal alkaline sphingomyelinase, Alk-Smase, ENPP7 and NPP-7, is a single-pass type I membrane protein which belongs to thenucleotide pyrophosphatase / phosphodiesterase family. ENPP7 / NPP-7 is expressed in the intestines and human bile. ENPP7 / NPP-7 is localized at the surface of the microvillar membrane in small intestine enterocytes, as well as in endosome-like structures and in Golgi complex. The main function of ENPP7 / NPP-7 is to convert the dietary sphingomyelin into ceramide, the sphingolipid messengers via hydrolyzation. ENPP7 / NPP-7 is also reported to exert a phospholipase C activity toward palmitoyl lyso-phosphocholine. The activity of this enzyme is inhibited in a dose dependent manner by ATP, imidazole, orthovanadate and zinc ion. Further, It has been shown in studies that decreased levels of ENPP7 / NPP-7 may be associated with human colon cancer.
Human enterovirus 71 genome polyprotein is a member of the picornaviruses polyprotein family. It contains twopeptidase C3 domains, oneRdRp catalytic domain, oneSF3 helicase domain. Genome polyprotein is cleaved into the following 12 chains: Protein VP (VP4-VP2), Protein VP4 (P1A), Protein VP2 (P1B), Protein VP3 (P1C), Protein VP1 (P1D), Picornain 2A (P2A), Protein 2B (P2B), Protein 2C (P2C), Protein 3A (P3A), Protein 3B (P3B), Picornain 3C (Protease 3C) and RNA-directed RNA polymerase 3D-POL (P3D-POL). VP precursor is a component of immature procapsids. Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid composed of 6 copies of each VP1, VP2, and VP3, with a diameter of approximately 3 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes.
Ectonucleoside triphosphate diphosphohydrolase 5 (ENTPD5), also known as CD39 antigen-like 4, ER-UDPase, Guanosine-diphosphatase ENTPD5, Nucleoside diphosphatase Uridine-diphosphatase ENTPD5. This hydrolase is expressed in response to phosphoinositide 3-kinase (PI3K) signaling. Activation of PI3K results in FOXO phosphorylation by AKT1 and loss of ENTPD5 transcriptional repression. It is Up-regulated in PTEN-deficient cells. Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation.ENTPD5 promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, ENTPD5 constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. ENTPD5 also hydrolyzes GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. This enzyme Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.
Chemokine Ligand 26 protein (CCL26) is a novel small cytokine belonging to the CC chemokine family which is involved in immunoregulatory and inflammatory processes. CCL26 is constitutively expressed in thymus; but only transiently expressed in phytohemagglutinin-stimulated peripheral blood mononuclear cells. It specifically binds and induces chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. CCL26; along with Eotaxin-1 and Eotaxin-2; selectively activates the CC chemokine receptor 3 (CCR3). The Eotaxin-3-CCR3 interaction may play an important role in allergic diseases such as atopic dermatitis and bronchial asthma. The full-length cDNA for CCL26 encodes a protein of 94 amino acids with a putative signal peptide of either 23 or 26 amino acid residues. Both the 71 and 68 amino acid residue variants of recombinant CCL26 demonstrate equal potency in inducing chemotaxis of a human CCR3-transfected cell line. Unlike most other CC chemokines; CCL26 maps to human chromosome 7q11.2; within 40 kilobases of the Eotaxin-2 loci. CCL26 and Eotaxin-2 are unique in that they are the only chemokines identified to date that map to chromosome 7.
Chemokine (C C Motif) Ligand 26 (CCL26) is a novel small cytokine belonging to the CC chemokine family; which involved in immunoregulatory and inflammatory processes. CCL26 is expressed constitutively in thymus; but only transiently in phytohemagglutinin-stimulated peripheral blood mononuclear cells. It specifically binds and induces chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. Eotaxin-3/CCL26; along with Eotaxin-1 and Eotaxin-2; selectively activates the CC chemokine receptor 3 (CCR3). The Eotaxin-3-CCR3 interaction may play an important role in allergic diseases such as atopic dermatitis and bronchial asthma. The full-length cDNA for Eotaxin-3 encodes a protein of 94 amino acids with a putative signal peptide of either 23 or 26 amino acid residues. Both the 71 and 68 amino acid residue variants of recombinant Eotaxin-3 demonstrate equal potency in inducing chemotaxis of a human CCR3-transfected cell line. Unlike most other CC chemokines; Eotaxin-3 maps to human chromosome 7q11.2; within 40 kilobases of the Eotaxin-2 loci. Eotaxin-3 and Eotaxin-2 are unique in that they are the only chemokines identified to date that map to chromosome 7.
May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E.
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