118489 Results for: "jodek+potasu&pageNo=30"

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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. Acts as a receptor for Listeria internalin inlB, mediating entry of the pathogen into cells.

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Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis process by modulating PP2A activity.Tissue specificityExpressed in peripheral blood leukocytes, colon, small intestine, prostate, thymus, spleen, skeletal muscle, liver and kidney.

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Myotilin, a sarcomeric protein that is encoded by the gene mapping to human chromosome 5q31, binds to a-actinin and is localized in the Z-line of myofibrils. Myotilin is expressed in skeletal and cardiac muscle, and it co-localizes with a-actinin in the sarcomeric I-bands where it directly interacts with a-actinin. Defects in the myotilin gene are reported to cause a form of autosomal dominant limb-girdle muscular dystrophy (LGMD). Symptoms of adult onset LGMD are progressive weakness of the hip and shoulder girdles as well as a distinctive dysarthric pattern of speech. The muscle of affected individuals with LGMD shows degeneration of myofibers, variations in fiber size, fiber splitting, centrally located myonuclei and an enhanced number of autophagic vesicles.

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Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL.

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MP21 is a member of the EMP24/GP25L/p24 cargo family of proteins that regulates vesicular trafficking in the early secretory pathway. TMP21 is a ubiquitously expressed single-pass type I membrane protein localizing to the Golgi cisternae and the plasma membrane. It contains one GOLD (Golgi dynamics) domain and participates in protein transport and quality control between the endoplasmic reticulum (ER) and the Golgi complex. In addition, TMP21 is a component of the heteromeric secretase complex (or Presenilin complex) and functions to regulate the ?secretase activity. Two isoforms, namely TMP21-I and TMP21-II, exist for this protein.

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Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity. [SUBCELLULAR LOCATION] Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Constituent of focal adhesions.

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Neuromedin U is a neuropeptide with high activity on smooth muscle. It is widely expressed in gastrointestinal systems and central nervous system (CNS). Peripheral activities of neuromedin U include smooth muscle stimulation, ion transport alterations in the gut and the regulation of local blood flow and adrenocortical function. Neuromedin U receptors 1 and 2 (NMUR1 and NMUR2) are multi-pass membrane proteins that belong to the G-protein coupled receptor 1 family of proteins. Both NMUR1 and NMUR2 act as receptors for the neuromedin U neuropeptide. NMUR1 is detected in peripheral organs, particularly in urogenital and gastrointestinal systems, with highest levels in testis. It’s expression in CNS is low, but the protein has been detected in cerebellum, hippocampus, dorsal root ganglia and spinal cord. NMUR2 is predominantly detected in central nervous system with highest levels detected in medulla oblongata, spinal cord and thalamus. It may also be detected in testis but has low levels of expression in peripheral tissues.

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Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane, known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through the formation of disulfide bonds and gamma-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are Ca2+-dependent enzymes, which catalyze the formation of isopeptide bonds by transferring an amine to a glutaminyl residue, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. TGase6 (transglutaminase 6), also known as TGM6, TGY or TGM3L, is a 706 amino acid protein that catalyzes the cross-linking of proteins and the conjugation of proteins to polyamines. As a result of alternative splicing, two TGase6 isoforms exist.

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Members of the GATA family share a conserved zinc finger DNA-binding domain and are capable of binding the WGATAR consensus sequence. GATA-1 is erythroid-specific and is responsible for the regulated transcription of erythroid genes. It is an essential component in the generation of the erythroid lineage. GATA-2 is expressed in embryonic brain and liver, HeLa and endothelial cells, as well as in erythroid cells. Studies with a modified GATA consensus sequence, AGATCTTA, have shown that GATA-2 and GATA-3 recognize this mutated consensus while GATA-1 has poor recognition of this sequence. This indicates broader regulatory capabilities of GATA-2 and GATA-3 than GATA-1. GATA-3 is highly expressed in T lymphocytes. GATA-4, GATA-5 and GATA-6 comprise a subfamily of transcription factors. Both GATA-4 and GATA-6 are found in heart, pancreas and ovary; lung and liver tissues exhibit GATA-6, but not GATA-4 expression. GATA-5 expression has been observed in differentiated heart and gut tissues and is present throughout the course of development in the heart. Although expression patterns of the various GATA transcription factors may overlap, it is not yet apparent how the GATA factors are able to discriminate in binding their appropriate target sites.

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Phosphorylated upon DNA damage, probably by ATM or ATR.

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Inositol polyphosphate multikinase (IPMK) belongs to the inositol phosphokinase (IPK) family and is characterized as having a broad substrate specificity. However, IPMK displays a preference for inositol-1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4). IPMK is ubiquitously expressed with the highest expression in skeletal muscle, liver, placenta, lung, peripheral blood leukocytes, kidney, spleen and colon. IPMK is localized to the nucleus, where it may play a role in the regulation of calcium release from intracellular stores and has been implicated as a drug target for cancer therapies. The gene encoding IPMK maps to human chromosome 10, which contains over 800 genes. Notably, disorders linked to genes on chromosome 10 include Cowden syndrome, Cockayne syndrome and Tetrahydrobiopterin deficiency.

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Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis.

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Potentiates but cannot initiate FAS-induced apoptosis.

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Integrins are heterodimeric cell surface receptors composed of alpha and beta subunits, which mediate cell-cell and cell-extracellular matrix attachments. Aberrant integrin expression has been found in many epithelial tumours. Changes in integrin expression have been shown to be important for the growth and early metastatic capacity of melanoma cells. Integrin alpha-v beta-6 is upregulated in cancers and during tissue remodelling but is absent from resting adult tissues. Integrin alpha-v beta-6 promotes invasion and correlates with poor survival and therefore makes a promising therapeutic target.

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Transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation which has different mechanisms of action specific to the lineage and biological functions. Forms complexes with different corepressors and histone deacetylases to repress the transcriptional expression of different subsets of target genes. Represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by repressing the transcriptional activity of transcription factors. In GC B-cells, represses genes that function in differentiation, inflammation, apoptosis and cell cycle control, also autoregulates its transcriptional expression and up-regulates, indirectly, the expression of some genes important for GC reactions, such as AICDA, through the repression of microRNAs expression, like miR155. An important function is to allow GC B-cells to proliferate very rapidly in response to T-cell dependent antigens and tolerate the physiological DNA breaks required for immunglobulin class switch recombination and somatic hypermutation without inducing a p53/TP53-dependent apoptotic response. In follicular helper CD4(+) T-cells (T(FH) cells), promotes the expression of T(FH)-related genes but inhibits the differentiation of T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and maintenance of immunological memory for both T- and B-cells. Suppresses macrophage proliferation through competition with STAT5 for STAT-binding motifs binding on certain target genes, such as CCL2 and CCND2. In response to genotoxic stress, controls cell cycle arrest in GC B-cells in both p53/TP53-dependedent and -independent manners. Besides, also controls neurogenesis through the alteration of the composition of NOTCH-dependent transcriptional complexes at selective NOTCH targets, such as HES5, including the recruitment of the deacetylase SIRT1 and resulting in an epigenetic silencing leading to neuronal differentiation.

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CRISP3

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When present in a hybrid receptor with INSR, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.

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AHNAK is a 5,890 amino acid protein encoded by the human gene AHNAK. The intronless AHNAK gene is located on human chromosome 11q12 and has three main structural regions: the 251 amino acid N-terminus, a large central region of 4390 amino acids with multiple repeated units of about 128 amino acids in length, and the 1002 amino acid C-terminus. The central region seems to have antiparallel beta-strands connected by intervening loops. Several putative regulatory elements are clustered within the C-terminal region, including nuclear export localization signals, a leucine zipper, and potential phosphorylation sites for Akt1 and PKC. AHNAK is believed to be an important signalling molecule involved in a wide range of physiological activities and may be required for neuronal cell differentiation.. AHNAK also appears to influence b-adrenergic regulation of cardiac L-type Ca2+ channel function.

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The hepatic sodium/bile acid uptake system exhibits broad substrate specificity and transports various non-bile acid organic compounds as well. It is strictly dependent on the extracellular presence of sodium.

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Protein kinases comprise a large group of encoded factors that regulate cellular processes by catalyzing the transfer of a phosphate group to a hydroxyl acceptor in serine, threonine or tyrosine residues (1,2). Kinases are capable of influencing the oncogenic potential of cell sytems at the level of oncoprotein or tumor suppressor protein phosphorylation states (1,2). STAP-2 is a protein that contains a pleckstrin homology (PH) domain and an SH2 domain, and associates with BRK (3). BRK (breast tumor kinase, Sik) is a 451 amino acid, nonreceptor protein-tyrosine kinase that is overexpressed in breast tumors and metastatic melanoma cell lines (4). Similar to the Src family of intracellular kinses, BRK is comprised of an SH3 domain, an SH2 domain, and a catalytic domain (5). STAP-2 is susceptiple to tyrosine phosphorylation and may be invovled in tyrosine kinase-mediated signaling cascades, whose aberrant function may lead to metastis (3).

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Facilitative glucose transporter. This isoform likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the beta cell. May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney.

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Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.

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Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade.

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Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. Inhibits glycolysis by reducing cellular levels of fructose-2,6-bisphosphate. May protect cells against reactive oxygen species and against apoptosis induced by tp53.

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This gene encodes a member of the Wiskott-Aldrich syndrome protein family. The gene product is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal verprolin homology domain in all family members. The multiprotein complex serves to tranduce signals that involve changes in cell shape, motility or function. The published map location (PMID:10381382) has been changed based on recent genomic sequence comparisons, which indicate that the expressed gene is located on chromosome 1, and a pseudogene may be located on chromosome X. Two transcript variants encoding different isoforms have been found for this gene.

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Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.

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The protein encoded by ZFP91 is a member of the zinc finger family of proteins. This protein contains C2H2 type domains, which are the classical zinc finger domains found in numerous nucleic acid-binding proteins. May be involved in transcriptional regulation. May play an important role in cell proliferation and/or anti-apoptosis Found in all the examined tissues including brain, heart, kidney, lung, liver, spleen, thymus, skeletal muscle, ovary and testis. Belongs to the krueppel C2H2-type zinc-finger protein family.

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MSK1 is a mitogen and stress activated protein kinase 1 which belongs to the AGC family of kinases and is related in structure to the ribosomal p70 S6 kinase subfamily. MSK1 can be activated by ERK1/2 and SAPK2/p38 MAP kinase. It is also known to be required for the phosphorylation of CREB, ATF1 H3 and HMG14 in response to mitogen and stress. Similar to RSK, MSK1 contains two kinase domains (N term and a C term). Once phosphorylated on Thr581 and Ser360 by ERK1/2 and SAPK2/p38, MSK1 autophosphorylate on at least 5 sites. Of these autophosphorylation sites Ser212 and Ser376 get phosphorylated by the C terminal kinase domain of MSK1 which is essential for the catalytic activity of the N terminal kinase domain.

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Representing about 2% of human DNA, chromosome 20 consists of approximately 63 million bases and 600 genes. Chromosome 20 contains a region with numerous genes expressed in the epididymis, which are thought important for seminal production, and some viewed as potential targets for male contraception. The PRNP gene encoding the prion protein associated with spongiform encephalopathies, like Creutzfeldt-Jakob disease, is found on chromosome 20. Amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome are also associated with chromosome 20. The C20orf165 gene product has been provisionally designated C20orf165 pending further characterization.

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Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.