40406 Results for: "2-Methoxypyrimidine-4-carbaldehyde&pageNo=68"

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Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing.

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Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins.

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Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.

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Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo. Plays a role in central nevous system development. Required for proper formation of motor neuron axons.

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FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

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Lysosome associated membrane protein (LAMP1), also known as lgp120 or lgpA, is a type 1 integral membrane protein that is transported from trans Golgi networks to endosomes and then lysosomes. Upon cell activation, LAMP1 transfer to the plasma membrane is dependent on a carboxyl terminal tyrosine based motif (YXXI). Perturbation in the spacing between the tyrosine based motif relative to the membrane abolishes lysosome localisation of LAMP1. This mutant protein then cycles between the plasma membrane and the endosome. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.

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Alpha-1-antitrypsin is a protease inhibitor, deficiency of which is associated with emphysema and liver disease. The protein is encoded by a gene (PI) located on the distal long arm of chromosome 14.

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Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

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Forms a channel with a broad specificity. Mediates passage of a wide variety of non-charged solutes including carbamides, polyols, purines, and pyrimidines in a phloretin- and mercury-sensitive manner, whereas amino acids, cyclic sugars, Na(+), K(+), Cl(-), and deprotonated monocarboxylates are excluded. Also permeable to urea and glycerol.

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Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

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Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity).

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Heamachrome.

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Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2. Seems to have an immune potentiation function.

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Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.

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Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.

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Insulin is a pancreatic hormone that regulates glucose and is involved in the synthesis of protein and fat. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Heterodimer of a B chain and an A chain linked by two disulfide bonds.Belongs to the insulin family. The insulin-link growth factors, IGF-I and IGF-II (also desinated somatomedin C and multiplication stimulating activator, respectvely), share approximatly 76% sequence identity and are 50% related to pro-insulin.IGF-I and IGF-II are nonglycosylated, single chain proteins of 70 and 76 amino acids in length, respectivelly. IGF-I functions as an autocrine regulator of growth in vaious, whereas the function of IGF-II is less well defined.

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The glycine cleavage system is comprised of AMT (known as Protein T), GCSH (known as Protein H), DLD (known as Protein L) and GLDC (known as Protein P), all of which work together to catalyze the cleavage and degradation of glycine. GLDC (glycine dehydrogenase ), also known as GCE, GCSP (glycine cleavage system P protein) or HYGN1, is a 1,020 amino acid protein that localizes to the mitochondria and belongs to the gcvP family. GLDC binds to glycine and enables the methylamine group from glycine to be transferred to the Protein T. GLDC exists as a homodimer and utilizes pyridoxal phosphate as a cofactor. Mutations in the gene encoding GLDC leads to nonketotic hyperglycinemia (NKH), also known as glycine encephalopathy (GCE), an autosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms.

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This gene encodes a transmembrane protein containing six epidermal growth factor repeats. The protein is involved in the differentiation of several cell types, including adipocytes; it is also thought to be a tumor suppressor. It is one of several imprinted genes located in a region of on chr 14q32. Certain mutations in this imprinted region can cause phenotypes similar to maternal and paternal uniparental disomy of chromosome 14 (UPD14). This gene is expressed from the paternal allele. A polymorphism within this gene has been associated with child and adolescent obesity. The mode of inheritance for this polymorphism is polar overdominance; this non-Mendelian inheritance pattern was first described in sheep with the callipyge phenotype, which is characterised by muscle hypertrophy and decreased fat mass.

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This gene encodes a mitochondrial outer membrane protein. It has a potential role in tumorigenesis, which may result from negative regulation of the p53 tumor suppressor gene. Alternatively spliced transcript variants have been noted for this gene.

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Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 chequepoint and progression to cytokinesis during mitosis. Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F() activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. Isoform Bcl-X(S) promotes apoptosis.

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Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.

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Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. May be involved in normal development or differentiation as well as in carcinogenesis.

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Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ).

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Tenascin, also known as hexabrachion and cytotactin, is an extracellular matrix protein with a spatially and temporally restricted tissue distribution. It is a hexameric, multidomain protein with disulfide linked subunits of 190 to 240 kD, originally characterised as 'myotendinous antigen.' In the embryo it is present in dense mesenchyme surrounding developing epithelia and in developing cartilage and bone. In the adult, tenascin remains present in tendons and myotendinous junctions in the perichondrium and periosteum, as well as in smooth muscle.

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The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.

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DNAJC3 may act as an inhibitor of both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2/PKR to catalyse phosphorylation of the EIF2A. It also functions as a Co-chaperone of HSPA8/HSC70 and is involved in the unfolded protein response (UPR) during ER stress. It has been reported that this protein stimulates the ATPase activity of HSPA8/HSC70.DNAJC3 is also involved in ativiral defense - it is activated in response to infection by influenza virus through the dissociation of DNAJB1. DNAJC3 is widely expressed and can be found at high levels in the testis and pancreas (expression in cell lines is variable).

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Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

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Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.

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AMAP-1 (AMY-1-binding protein 1), also known as AMAM-1 or MYCBPAP (MYCBP associated protein), is a 947 amino acid protein that is expressed specifically in testis and is involved in spermatogenesis and synaptic processes. AMAP-1 colocalizes with MYCBP (AMY-1) in cytoplasm and also localizes to membrane. The gene encoding AMAP-1 maps to human chromosome 17, which comprises over 2.5% of the human genome and encodes over 1,200 genes. Two key tumor suppressor genes are associated with chromosome 17, namely, p53 and BRCA1. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. Malfunction or loss of p53 expression is associated with malignant cell growth and Li-Fraumeni syndrome. Like p53, BRCA1 is directly involved in DNA repair, though specifically it is recognized as a genetic determinant of early onset breast cancer and predisposition to cancers of the ovary, colon, prostate gland and fallopian tubes.

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ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.