54782 Results for: "Kwas+6-aminopikolinowy&pageNo=48"

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Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Expression of this gene is regulated by steroid hormones and may be useful as a marker for breast cancer. An additional transcript variant has been identified, but its full length sequence has not been determined. [provided by RefSeq, Jul 2008].

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Cytokine with a wide variety of biological functions. It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig-secreting cells Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Required for the generation of T(H)17 cells. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation.

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Fanconi Anemia (FANC) is a human autosomal-recessive cancer susceptibility disorder characterized by congenital defects, progressive bone marrow failure, and cellular hypersensitivity to mitomycin C (MMC). The FANC subunit D2 protein is vital for cellular resistance to DNA cross-linking and the arrest of DNA synthesis after ionizing radiation. DNA damage activates the monoubiquitination of FANC D2, targeting nuclear foci containing the BRCA 1 protein.

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Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF1B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response.

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The family of insulin receptor substrates (IRSs) has been reported to play important roles for signal transduction of various hormones. Four members of the IRS family have been described. Each IRS is believed to have different functions; however, the distinct physiological roles of each IRS are unclear. Summary: This gene encodes the insulin receptor substrate 2, a cytoplasmic signaling molecule that mediates effects of insulin, insulin-like growth factor 1, and other cytokines by acting as a molecular adaptor between diverse receptor tyrosine kinases and downstream effectors. The product of this gene is phosphorylated by the insulin receptor tyrosine kinase upon receptor stimulation, as well as by an interleukin 4 receptor-associated kinase in response to IL4 treatment.

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Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines residing in the dinucleotide CpG motif, and this methylation results in transcriptional repression of the target gene. The Dnmt enzymes are encoded by independent genes. Dnmt1 is the most abundant, and it preferentially methylates hemimethylated DNA and coordinates gene expression during development. Additional mammalian Dnmt proteins include Dnmt2 and Dnmt3. Dnmt2 lacks the large N-terminal regulator domain of Dnmt1, is expressed at substantially lower levels in adult tissues, and is likely involved in methylating newly integrated retroviral DNA. Dnmt3a and Dnmt3b are encoded by two distinct genes, but both are abundantly expressed in embryonic stem cells, where they also methylate CpG motifs on DNA.

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FAM82A2, or family with sequence similarity 82, member C, may participate in differentiation and apoptosis of keratinocytes. Overexpression of FAM82A2 induces apoptosis.

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Equilibrative nucleoside transporters (ENTs) regulate many physiological processes and are widely distributed in mammals, plants, yeasts, insects, nematodes and protozoans. They enable facilitated diffusion of hydrophilic nucleosides, such as adenosine and nucleoside analogs, across cell membranes. ENTs are required for uptake of antiviral and anticancer nucleoside drugs and influence a variety of physiological processes, such as neurotransmission and platelet aggregation, by regulating the amount of adenoside available to cell surface receptors. Equilibrative nucleoside transporter 1 (ENT1), also designated solute carrier family 29 (nucleoside transporters), member 1, belongs to the SLC29A transporter family and is a mammalian ENT isoform. ENT1, along with ENT3, mediates the majority of influx and efflux of nucleosides across the plasma membrane.

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c-Kit is a transmembrane tyrosine kinase encoded by the cKit proto oncogene. c-Kit acts to regulate a variety of biological responses including cell proliferation, apoptosis, chemotaxis and adhesion. Ligand binding to the extracellular domain leads to autophosphorylation on several tyrosine residues within the cytoplasmic domain, and activation. Mutations in c-Kit have been found to be important for tumor growth and progression in a variety of cancers including mast cell diseases, gastrointestinal stromal tumor, acute myeloid leukemia, Ewing sarcoma and lung cancer. Phosphorylation at tyrosine 721 of c-Kit allows binding and activation of PI3 kinase.

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c-Kit is a transmembrane tyrosine kinase encoded by the cKit proto oncogene. c-Kit acts to regulate a variety of biological responses including cell proliferation, apoptosis, chemotaxis and adhesion. Ligand binding to the extracellular domain leads to autophosphorylation on several tyrosine residues within the cytoplasmic domain, and activation. Mutations in c-Kit have been found to be important for tumor growth and progression in a variety of cancers including mast cell diseases, gastrointestinal stromal tumor, acute myeloid leukemia, Ewing sarcoma and lung cancer. Phosphorylation at tyrosine 721 of c-Kit allows binding and activation of PI3 kinase.

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Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying protein. ZBTB44 is a 570 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.

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E2 EPF is a member of the ubiquitin conjugating enzyme family. It is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme dependent manner, a characteristic property of ubiquitin carrier proteins.

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TORC3 is a 619 amino acid protein that localizes to both the cytoplasm and the nucleus and belongs to the TORC family. Expressed in lung tissue and B and T lymphocytes, as well as in colon, brain, ovary, kidney, prostate, colon and heart, TORC3 functions as a transcriptional coactivator for CREB-1, thereby regulating the expression of CREB-activated genes, and is also thought to activate the SIK/TORC signaling pathway. TORC3 exists as multiple alternatively spliced isoforms and, in addition to its role in transcriptional activation, is thought to induce mitochondrial biogenesis, specifically in muscle cells.

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Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity).

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The protein encoded by this gene is a nuclear encoded endonuclease that is localized in the mitochondrion. The encoded protein is widely distributed among animals and cleaves DNA at GC tracts. This protein is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA. [provided by RefSeq, Jul 2008].

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Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity).

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Src is the human homolog of the v-Src gene of the rous sarcoma virus, also designated avian sarcoma virus or ASV. Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family, which has common structural motifs, is composed of nine members in vertebrates, including Src, Yes, Fgr, Frk, Fyn, Lyn, Hck, Lck and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility and adhesion. Src-family ki-nases contain an amino-terminal cell membrane anchor followed by an SH3 domain and an SH2 domain, which are involved in modular association and activation, respectively. Src-family kinases, which are normally maintained in an inactive state and can be activated transiently during cellular events such as mitosis. Different subcellular localizations of Src-family kinases may be important for the regulation of specific cellular processes such as mitogenesis, cytoskeletal organization and membrane trafficking. c-Fgr is a human non-receptor tyrosine kinase family member that was discovered by using a probe toward the v-Fgr portion of the cell-derived domain of Gardner-Rasheed feline sarcoma virus. The human c-Fgr gene encodes a 529 amino acid protein.

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Nuclear Marker.The protein encoded by this gene is a negative regulator of the cell cycle and was the first tumor suppressor gene found. The encoded protein also stabilizes constitutive heterochromatin to maintain the overall chromatin structure. The active, hypophosphorylated form of the protein binds transcription factor E2F1. Defects in this gene are a cause of childhood cancer retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.

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Electron-transferring-flavoprotein dehydrogenase in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The protein is synthesized as a 67-kDa precursor which is targeted to mitochondria and processed in a single step to a 64-kDa mature form located in the mitochondrial membrane. Deficiency in electron-transferring-flavoprotein dehydrogenase have been demonstrated in some patients with type II glutaricacidemia. [provided by RefSeq, Jul 2008].

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Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III.

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Heamachrome

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Protocadherins are a large family of cadherin-like cell adhesion proteins that are involved in the establishment and maintenance of neuronal connections in the brain. There are three protocadherin gene clusters, designated a, b and g, all of which contain multiple tandemly-arranged genes. PCDHB10 (protocadherin b10), also known as PCHB10 or PCDH-b10, is an 800 amino acid protein that is one of 16 proteins in the protocadherin b cluster. Unlike the a and g gene clusters, whose genes are spliced to downstream constant-region exons during transcription, members of the b cluster (such as PCDHB10) do not use constant-region exons to produce mRNAs. As a result, each protocadherin b gene encodes the transmembrane, extracellular and short cytoplasmic domains of the protein. Localized to the cell membrane, PCDHB10 is a single-pass type I membrane protein that contains six cadherin domains.

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Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. May limit beta-amyloid peptide accumulation in brain. May also have methyltransferase activity.

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Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). May associate with and regulate the cell adhesion properties of both C- and E-cadherins. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage.

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Protocadherins are a large family of cadherin-like cell adhesion proteins that are involved in the establishment and maintenance of neuronal connections in the brain. There are three protocadherin gene clusters, designated alpha, beta and gamma, all of which contain multiple tandemly arranged genes. PCDHB1 (Protocadherin beta 1) is an 818 amino acid protein that is one of 16 proteins in the protocadherin beta cluster. Unlike the alpha and gamma gene clusters whose genes are spliced to downstream constant region exons during transcription, members of the beta cluster (such as PCDHB1) do not use constant-region exons to produce mRNAs. As a result, each protocadherin beta gene encodes the transmembrane, extracellular and short cytoplasmic domains of the protein. PCDHB1 is a single-pass type I membrane protein containing six cadherin domains.

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Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.

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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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Glucose and insulin are anabolic signals which upregulate the transcriptions of a series of lipogenic enzymes to convert excess carbohydrate into triglycerides for efficient energy storage. Acyl-coenzyme A:diacylglycerol acyltransferase, also known as DGAT1 and ARGP1, is a microsomal enzyme that assists in the synthesis of fatty acids into triglycerides. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol (DAG) and fatty acyl CoA as substrates. DGAT1 plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eukaryotes for physiologic processes involving triacylglycerol metabolism, such as intestinal fat absorption, lipoprotein assembly, adipose tissue form-ation and lactation. DGAT2, which has no homology to DGAT1, differs from DGAT1 in that its activity has been shown to be inhibited by MgCl in an in vitro assay. DGAT2 is expressed primarily in liver and white adipose tissue, which suggests that it plays an important role in mammalian triglyceride metabolism.

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This gene encodes a GTP-binding protein that belongs to the small GTPase superfamily and Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors.

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In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.