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[PMID]: 23344948 [Au] Autor: Amigo I; Traba J; González-Barroso MM; Rueda CB; Fernández M; Rial E; Sánchez A; Satrústegui J; Del Arco A [Ad] Dirección: Departmento de Biología Molecular, Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid-CSIC, Madrid, Spain. [Ti] Título: Glucagon regulation of oxidative phosphorylation requires an increase in matrix adenine nucleotide content through Ca2+ activation of the mitochondrial ATP-Mg/Pi carrier SCaMC-3. [So] Fuente: J Biol Chem;288(11):7791-802, 2013 Mar 15. [Is] ISSN: 1083-351X [Cp] País de publicación: United States [La] Idioma: eng [Ab] Resumen: It has been known for a long time that mitochondria isolated from hepatocytes treated with glucagon or Ca(2+)-mobilizing agents such as phenylephrine show an increase in their adenine nucleotide (AdN) content, respiratory activity, and calcium retention capacity (CRC). Here, we have studied the role of SCaMC-3/slc25a23, the mitochondrial ATP-Mg/Pi carrier present in adult mouse liver, in the control of mitochondrial AdN levels and respiration in response to Ca(2+) signals as a candidate target of glucagon actions. With the use of SCaMC-3 knock-out (KO) mice, we have found that the carrier is responsible for the accumulation of AdNs in liver mitochondria in a strictly Ca(2+)-dependent way with an S0.5 for Ca(2+) activation of 3.3 ± 0.9 µm. Accumulation of matrix AdNs allows a SCaMC-3-dependent increase in CRC. In addition, SCaMC-3-dependent accumulation of AdNs is required to acquire a fully active state 3 respiration in AdN-depleted liver mitochondria, although further accumulation of AdNs is not followed by increases in respiration. Moreover, glucagon addition to isolated hepatocytes increases oligomycin-sensitive oxygen consumption and maximal respiratory rates in cells derived from wild type, but not SCaMC-3-KO mice and glucagon administration in vivo results in an increase in AdN content, state 3 respiration and CRC in liver mitochondria in wild type but not in SCaMC-3-KO mice. These results show that SCaMC-3 is required for the increase in oxidative phosphorylation observed in liver mitochondria in response to glucagon and Ca(2+)-mobilizing agents, possibly by allowing a Ca(2+)-dependent accumulation of mitochondrial AdNs and matrix Ca(2+), events permissive for other glucagon actions. [Mh] Términos MeSH primario: Nucleótidos de Adenina/metabolismo Antiportadores/metabolismo Calcio/metabolismo Regulación de la Expresión Génica Glucagón/metabolismo Mitocondrias/metabolismo Proteínas Mitocondriales/metabolismo Oxígeno/metabolismo [Mh] Términos MeSH secundario: Adenosina Difosfato/química Adenosina Trifosfato/química Animales Glucosa/metabolismo Cinética Ratones Ratones Consanguíneos C57BL Ratones Transgénicos Mitocondrias Hepáticas/metabolismo Modelos Biológicos Fosforilación Oxidativa Consumo de Oxígeno [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nombre de substancia: 0 (ATP-Mg-Pi carrier proteins, mitochondria); 0 (Adenine Nucleotides); 0 (Antiporters); 0 (Mitochondrial Proteins); 50-99-7 (Glucose); 56-65-5 (Adenosine Triphosphate); 58-64-0 (Adenosine Diphosphate); 7440-70-2 (Calcium); 7782-44-7 (Oxygen); 9007-92-5 (Glucagon) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 130318 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M112.409144

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[PMID]: 23192020 [Au] Autor: Zhang J; Shapiro P; Pozharski E [Ad] Dirección: Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, 20 Penn Street, Baltimore, MD 21201, USA. [Ti] Título: Structure of extracellular signal-regulated kinase 2 in complex with ATP and ADP. [So] Fuente: Acta Crystallogr Sect F Struct Biol Cryst Commun;68(Pt 12):1434-9, 2012 Dec 1. [Is] ISSN: 1744-3091 [Cp] País de publicación: England [La] Idioma: eng [Ab] Resumen: Extracellular signal-regulated kinases 1 and 2 (ERK1 and ERK2) are members of the mitogen-activated protein (MAP) kinase family. Constitutive activation of the ERK proteins contributes to the development and progression of numerous human tumors. Thus, ERK1 and ERK2 are promising targets for the design and the development of anticancer drugs. The detailed structural analysis of ERK complexed with ATP can provide valuable information for the design of new ligands that can bind in the ATP-binding pocket and inhibit ERK activity. In this study, the structures of apo-form ERK2 and of its complexes with the substrate ATP and the product ADP were determined. Comparison with the structural homolog cyclin-dependent kinase 2 reveals differences in the way that the ATP binding to the protein is mediated by magnesium. Only minor conformational changes are identified that occur upon substrate binding, and these are limited to the active-site residues. [Mh] Términos MeSH primario: Adenosina Difosfato/metabolismo Adenosina Trifosfato/metabolismo Proteína Quinasa 1 Activada por Mitógenos/química [Mh] Términos MeSH secundario: Adenosina Difosfato/química Adenosina Trifosfato/química Animales Apoproteínas/química Apoproteínas/metabolismo Sitios de Unión Cristalografía por Rayos X Proteína Quinasa 1 Activada por Mitógenos/antagonistas & inhibidores Proteína Quinasa 1 Activada por Mitógenos/metabolismo Modelos Biológicos Conformación Proteica Ratas [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S. [Nm] Nombre de substancia: 0 (Apoproteins); 56-65-5 (Adenosine Triphosphate); 58-64-0 (Adenosine Diphosphate); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 121129 [St] Status: MEDLINE [do] DOI: 10.1107/S1744309112042972

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[PMID]: 23022874 [Au] Autor: Tretter L; Adam-Vizi V [Ad] Dirección: Department of Medical Biochemistry, Semmelweis University, Budapest H-1444, Hungary. [Ti] Título: High Ca2+ load promotes hydrogen peroxide generation via activation of α-glycerophosphate dehydrogenase in brain mitochondria. [So] Fuente: Free Radic Biol Med;53(11):2119-30, 2012 Dec 1. [Is] ISSN: 1873-4596 [Cp] País de publicación: United States [La] Idioma: eng [Ab] Resumen: H(2)O(2) generation associated with α-glycerophosphate (α-GP) oxidation was addressed in guinea pig brain mitochondria challenged with high Ca(2+) load (10 µM). Exposure to 10 µM Ca(2+) induced an abrupt 2.5-fold increase in H(2)O(2) release compared to that measured in the presence of a physiological cytosolic Ca(2+) concentration (100 nM) from mitochondria respiring on 5 mM α-GP in the presence of ADP (2 mM). The Ca(2+)-induced stimulation of H(2)O(2) generation was reversible and unaltered by the uniporter blocker Ru 360, indicating that it did not require Ca(2+) uptake into mitochondria. Enhanced H(2)O(2) generation by Ca(2+) was also observed in the absence of ADP when mitochondria exhibited permeability transition pore opening with a decrease in the NAD(P)H level, dissipation of membrane potential, and mitochondrial swelling. Furthermore, mitochondria treated with the pore-forming peptide alamethicin also responded with an elevated H(2)O(2) generation to a challenge with 10 µM Ca(2+). Ca(2+)-induced promotion of H(2)O(2) formation was further enhanced by the complex III inhibitor myxothiazol. With 20 mM α-GP concentration, stimulation of H(2)O(2) formation by Ca(2+) was detected only in the presence, not in the absence, of ADP. It is concluded that α-glycerophosphate dehydrogenase, which is accessible to and could be activated by a rise in the level of cytosolic Ca(2+), makes a major contribution to Ca(2+)-stimulated H(2)O(2) generation. This work highlights a unique high-Ca(2+)-stimulated reactive oxygen species-forming mechanism in association with oxidation of α-GP, which is largely independent of the bioenergetic state and can proceed even in damaged, functionally incompetent mitochondria. [Mh] Términos MeSH primario: Encéfalo/enzimología Calcio/fisiología Glicerolfosfato Deshidrogenasa/metabolismo Peróxido de Hidrógeno/metabolismo Mitocondrias/enzimología [Mh] Términos MeSH secundario: Adenosina Difosfato/metabolismo Adenosina Difosfato/fisiología Alameticina/farmacología Animales Encéfalo/metabolismo Complejo III de Transporte de Electrones/antagonistas & inhibidores Complejo III de Transporte de Electrones/metabolismo Metabolismo Energético Activación Enzimática Glicerofosfatos/metabolismo Glicerofosfatos/fisiología Cobayas Masculino Potencial de la Membrana Mitocondrial Metacrilatos/farmacología Mitocondrias/efectos de drogas Mitocondrias/metabolismo Consumo de Oxígeno Tiazoles/farmacología Desacopladores/farmacología [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nombre de substancia: 0 (Glycerophosphates); 0 (Methacrylates); 0 (Thiazoles); 0 (Uncoupling Agents); 27061-78-5 (Alamethicin); 58-64-0 (Adenosine Diphosphate); 7440-70-2 (Calcium); 76706-55-3 (myxothiazol); 7722-84-1 (Hydrogen Peroxide); 9NTI6P3O4X (alpha-glycerophosphoric acid); EC 1.1.- (Glycerolphosphate Dehydrogenase); EC 1.10.2.2 (Electron Transport Complex III) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 121127 [St] Status: MEDLINE

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[PMID]: 23322773 [Au] Autor: Ravilious GE; Westfall CS; Jez JM [Ad] Dirección: Department of Biology, Washington University, St Louis, Missouri 63130, USA. [Ti] Título: Redox-linked gating of nucleotide binding by the N-terminal domain of adenosine 5'-phosphosulfate kinase. [So] Fuente: J Biol Chem;288(9):6107-15, 2013 Mar 1. [Is] ISSN: 1083-351X [Cp] País de publicación: United States [La] Idioma: eng [Ab] Resumen: Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Crystallographic studies of APSK from Arabidopsis thaliana revealed the presence of a regulatory intersubunit disulfide bond (Cys(86)-Cys(119)). The reduced enzyme displayed improved catalytic efficiency and decreased effectiveness of substrate inhibition by APS compared with the oxidized form. Here we examine the effect of disulfide formation and the role of the N-terminal domain on nucleotide binding using isothermal titration calorimetry (ITC) and steady-state kinetics. Formation of the disulfide bond in A. thaliana APSK (AtAPSK) inverts the binding affinities at the ATP/ADP and APS/PAPS sites from those observed in the reduced enzyme, consistent with initial binding of APS as inhibitory, and suggests a role for the N-terminal domain in guiding nucleotide binding order. To test this, an N-terminal truncation variant (AtAPSKΔ96) was generated. The resulting protein was completely insensitive to substrate inhibition by APS. ITC analysis of AtAPSKΔ96 showed decreased affinity for APS binding, although the N-terminal domain does not directly interact with this ligand. Moreover, AtAPSKΔ96 displayed reduced affinity for ADP, which corresponds to a loss of substrate inhibition by formation of an E·ADP·APS dead end complex. Examination of the AtAPSK crystal structure suggested Arg(93) as important for positioning of the N-terminal domain. ITC and kinetic analysis of the R93A mutant also showed a complete loss of substrate inhibition and altered nucleotide binding affinities, which mimics the effect of the N-terminal deletion. These results show how thiol-linked changes in AtAPSK alter the energetics of binding equilibria to control its activity. [Mh] Términos MeSH primario: Arabidopsis/enzimología Fosfotransferasas (Aceptor de Grupo Alcohol)/química [Mh] Términos MeSH secundario: Adenosina Difosfato/química Adenosina Difosfato/genética Adenosina Difosfato/metabolismo Adenosina Trifosfato/química Adenosina Trifosfato/genética Adenosina Trifosfato/metabolismo Arabidopsis/genética Proteínas de Arabidopsis Catálisis Cinética Oxidación-Reducción Fosfotransferasas (Aceptor de Grupo Alcohol)/genética Fosfotransferasas (Aceptor de Grupo Alcohol)/metabolismo Unión Proteica Estructura Terciaria de Proteína Compuestos de Sulfhidrilo/química Compuestos de Sulfhidrilo/metabolismo [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S. [Nm] Nombre de substancia: 0 (Arabidopsis Proteins); 0 (Sulfhydryl Compounds); 56-65-5 (Adenosine Triphosphate); 58-64-0 (Adenosine Diphosphate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.25 (adenylylsulfate kinase) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 130304 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M112.439414

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[PMID]: 23598340 [Au] Autor: Vieira-Pires RS; Szollosi A; Morais-Cabral JH [Ad] Dirección: Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal. [Ti] Título: The structure of the KtrAB potassium transporter. [So] Fuente: Nature;496(7445):323-8, 2013 Apr 18. [Is] ISSN: 1476-4687 [Cp] País de publicación: England [La] Idioma: eng [Ab] Resumen: In bacteria, archaea, fungi and plants the Trk, Ktr and HKT ion transporters are key components of osmotic regulation, pH homeostasis and resistance to drought and high salinity. These ion transporters are functionally diverse: they can function as Na(+) or K(+) channels and possibly as cation/K(+) symporters. They are closely related to potassium channels both at the level of the membrane protein and at the level of the cytosolic regulatory domains. Here we describe the crystal structure of a Ktr K(+) transporter, the KtrAB complex from Bacillus subtilis. The structure shows the dimeric membrane protein KtrB assembled with a cytosolic octameric KtrA ring bound to ATP, an activating ligand. A comparison between the structure of KtrAB-ATP and the structures of the isolated full-length KtrA protein with ATP or ADP reveals a ligand-dependent conformational change in the octameric ring, raising new ideas about the mechanism of activation in these transporters. [Mh] Términos MeSH primario: Bacillus subtilis/química Proteínas Bacterianas/química Proteínas Bacterianas/metabolismo Proteínas de Transporte de Catión/química Proteínas de Transporte de Catión/metabolismo Potasio/metabolismo [Mh] Términos MeSH secundario: Adenosina Difosfato/metabolismo Adenosina Trifosfato/metabolismo Cristalografía por Rayos X Transporte Iónico Modelos Biológicos Modelos Moleculares Conformación Proteica Subunidades de Proteína/química Subunidades de Proteína/metabolismo Relación Estructura-Actividad [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nombre de substancia: 0 (Bacterial Proteins); 0 (Cation Transport Proteins); 0 (KtrB protein, Bacteria); 0 (Protein Subunits); 56-65-5 (Adenosine Triphosphate); 58-64-0 (Adenosine Diphosphate); 7440-09-7 (Potassium) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 130419 [St] Status: MEDLINE [do] DOI: 10.1038/nature12055

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[PMID]: 23598339 [Au] Autor: Cao Y; Pan Y; Huang H; Jin X; Levin EJ; Kloss B; Zhou M [Ad] Dirección: Department of Physiology & Cellular Biophysics, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, New York 10032, USA. [Ti] Título: Gating of the TrkH ion channel by its associated RCK protein TrkA. [So] Fuente: Nature;496(7445):317-22, 2013 Apr 18. [Is] ISSN: 1476-4687 [Cp] País de publicación: England [La] Idioma: eng [Ab] Resumen: TrkH belongs to a superfamily of K(+) transport proteins required for growth of bacteria in low external K(+) concentrations. The crystal structure of TrkH from Vibrio parahaemolyticus showed that TrkH resembles a K(+) channel and may have a gating mechanism substantially different from K(+) channels. TrkH assembles with TrkA, a cytosolic protein comprising two RCK (regulate the conductance of K(+)) domains, which are found in certain K(+) channels and control their gating. However, fundamental questions on whether TrkH is an ion channel and how it is regulated by TrkA remain unresolved. Here we show single-channel activity of TrkH that is upregulated by ATP via TrkA. We report two structures of the tetrameric TrkA ring, one in complex with TrkH and one in isolation, in which the ring assumes two markedly different conformations. These results suggest a mechanism for how ATP increases TrkH activity by inducing conformational changes in TrkA. [Mh] Términos MeSH primario: Proteínas Bacterianas/química Proteínas Bacterianas/metabolismo Activación del Canal Iónico [Mh] Términos MeSH secundario: Adenosina Difosfato/metabolismo Adenosina Trifosfato/metabolismo Cristalografía por Rayos X Conductividad Eléctrica Transporte Iónico Modelos Moleculares Pliegue de Proteína Estructura Cuaternaria de Proteína Estructura Terciaria de Proteína Vibrio parahaemolyticus [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nombre de substancia: 0 (Bacterial Proteins); 56-65-5 (Adenosine Triphosphate); 58-64-0 (Adenosine Diphosphate) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 130419 [St] Status: MEDLINE [do] DOI: 10.1038/nature12056

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[PMID]: 22193232 [Au] Autor: Ellabban AS; Kamel SR; Omar HA; El-Sherif AM; Abdel-Magied RA [Ad] Dirección: Rheumatology and Rehabilitation Department, Minia University, Minia, Egypt. [Ti] Título: Ultrasonographic diagnosis of articular chondrocalcinosis. [So] Fuente: Rheumatol Int;32(12):3863-8, 2012 Dec. [Is] ISSN: 1437-160X [Cp] País de publicación: Germany [La] Idioma: eng [Ab] Resumen: To investigate the role of high-frequency ultrasonography in the diagnosis of calcium pyrophosphate dihydrate (CPPD) calcifications, in the most commonly affected joints in CPPD disease. Sixty patients with knee effusion were included in the study. All patients underwent musculoskeletal ultrasonography (on the shoulder, elbow, wrist, and knee joints), radiological examination of the sites examined by US, and synovial fluid analysis (using polarized light microscopy). Out of 60 patients with knee effusion, ultrasonographic calcifications (knees, shoulders, and wrists) were present in 38 patients (63.3%) and out of those patients; 32 had calcification characteristic of CPPD crystals deposition (hyperechoic deposits) in the knee and wrist joints. Pattern II (punctate pattern) was the most common pattern of calcification. It was present in all patients who had wrist calcification (18 patients) and in the knee in either alone (21 patients) or in association with pattern I (hyperechoic band) and/or pattern III (hyperechoic nodular or oval deposits) (9 patients). The sensitivity of ultrasonography for the detection of calcification was 84.2% while that of plain radiography was 13.2%, the specificity of both ultrasonography and plain radiography for the detection of calcification was 100%, and ultrasonography is valuable for diagnosing articular chondrocalcinosis via the detection of calcifications within the joint cartilage and fibrocartilage. Both sensitivity and specificity are high for detecting CPPD deposits. [Mh] Términos MeSH primario: Cartílago Articular/ultrasonografía Condrocalcinosis/ultrasonografía Articulación de la Rodilla/ultrasonografía Articulación del Hombro/ultrasonografía Articulación de la Muñeca/ultrasonografía [Mh] Términos MeSH secundario: Adulto Anciano Cartílago Articular/radiografía Condrocalcinosis/radiografía Femenino Humanos Articulación de la Rodilla/radiografía Masculino Mediana Edad Sensibilidad y Especificidad Articulación del Hombro/radiografía Articulación de la Muñeca/radiografía [Pt] Tipo de publicación: JOURNAL ARTICLE [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 121126 [St] Status: MEDLINE [do] DOI: 10.1007/s00296-011-2320-1

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[PMID]: 22497853 [Au] Autor: Bartolini M; Wainer IW; Bertucci C; Andrisano V [Ad] Dirección: Department of Pharmaceutical Sciences, University of Bologna, via Belmeloro 6, 40126 Bologna, Italy. manuela.bartolini3@unibo.it [Ti] Título: The rapid and direct determination of ATPase activity by ion exchange chromatography and the application to the activity of heat shock protein-90. [So] Fuente: J Pharm Biomed Anal;73:77-81, 2013 Jan 25. [Is] ISSN: 1873-264X [Cp] País de publicación: England [La] Idioma: eng [Ab] Resumen: Adenosine nucleotides are involved as substrates or co-factors in several biochemical reactions, catalyzed by enzymes, which modulate energy production, signal transduction and cell proliferation. We here report the development and optimization of an ion exchange liquid chromatography (LC) method for the determination of ATP, ADP and AMP. This method is specifically aimed at the determination of the ATP-ase activity of human heat shock protein 90 (Hsp90), a molecular chaperone that has emerged as target enzyme in cancer therapy. Separation of the three nucleotides was achieved in a 15-min run by using a disk shaped monolithic ethylene diamine stationary phase of small dimensions (2mm×6mm i.d.), under a three-solvent gradient elution mode and UV detection at 256nm. The described direct LC method resulted highly specific as a consequence of the baseline separation of the three adenosine nucleotides and could be applied to the determination of the enzymatic activity of ADP/ATP generating or consuming enzymes (such as kinases). Furthermore, comparison of the LOD and LOQ values of the LC method with those obtained with the malachite green assay, which is one of the most used indirect screening methodologies for ATP-ase activity, showed that the LC method has a similar range of application without presenting the drawbacks related to contamination by inorganic phosphate ions and glycerol, which are present in Hsp90 commercial samples. [Mh] Términos MeSH primario: Adenosin-Trifosfatasas/metabolismo Proteínas HSP90 de Choque Térmico/metabolismo [Mh] Términos MeSH secundario: Adenosina Difosfato/análisis Adenosina Monofosfato/análisis Adenosin-Trifosfatasas/química Adenosina Trifosfato/análisis Calibración Cromatografía por Intercambio Iónico Dicroismo Circular Activación Enzimática Proteínas HSP90 de Choque Térmico/química Ensayos Analíticos de Alto Rendimiento Humanos Hidrólisis Límite de Detección [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nombre de substancia: 0 (HSP90 Heat-Shock Proteins); 0 (HSP90alpha protein, human); 56-65-5 (Adenosine Triphosphate); 58-64-0 (Adenosine Diphosphate); 61-19-8 (Adenosine Monophosphate); EC 3.6.1.- (Adenosine Triphosphatases) [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 121120 [St] Status: MEDLINE

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[PMID]: 23091026 [Au] Autor: Barua B; Winkelmann DA; White HD; Hitchcock-DeGregori SE [Ad] Dirección: Department of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA. baruabi@umdnj.edu [Ti] Título: Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin. [So] Fuente: Proc Natl Acad Sci U S A;109(45):18425-30, 2012 Nov 6. [Is] ISSN: 1091-6490 [Cp] País de publicación: United States [La] Idioma: eng [Ab] Resumen: Cooperative activation of actin-myosin interaction by tropomyosin (Tm) is central to regulation of contraction in muscle cells and cellular and intracellular movements in nonmuscle cells. The steric blocking model of muscle regulation proposed 40 y ago has been substantiated at both the kinetic and structural levels. Even with atomic resolution structures of the major players, how Tm binds and is designed for regulatory function has remained a mystery. Here we show that a set of periodically distributed evolutionarily conserved surface residues of Tm is required for cooperative regulation of actomyosin. Based on our results, we propose a model of Tm on a structure of actin-Tm-myosin in the "open" (on) state showing potential electrostatic interactions of the residues with both actin and myosin. The sites alternate with a second set of conserved surface residues that are important for actin binding in the inhibitory state in the absence of myosin. The transition from the closed to open states requires the sites identified here, even when troponin + Ca(2+) is present. The evolutionarily conserved residues are important for actomyosin regulation, a universal function of Tm that has a common structural basis and mechanism. [Mh] Términos MeSH primario: Actinas/metabolismo Secuencia Conservada Miosinas/metabolismo Tropomiosina/metabolismo [Mh] Términos MeSH secundario: Citoesqueleto de Actina/metabolismo Adenosina Difosfato/metabolismo Secuencia de Aminoácidos Animales Sitios de Unión Calcio/metabolismo Evolución Molecular Fluorescencia Yodoacetamida/análogos & derivados Yodoacetamida/metabolismo Cinética Modelos Moleculares Datos de Secuencia Molecular Mutación/genética Fosfatos/metabolismo Unión Proteica Transporte de Proteína Ratas Dispersión de Radiación Tropomiosina/química Tropomiosina/genética Troponina/metabolismo [Pt] Tipo de publicación: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL [Nm] Nombre de substancia: 0 (Actins); 0 (Phosphates); 0 (Tropomyosin); 0 (Troponin); 144-48-9 (Iodoacetamide); 58-64-0 (Adenosine Diphosphate); 7440-70-2 (Calcium); 76936-87-3 (N-(1-pyrenyl)iodoacetamide); EC 3.6.4.1 (Myosins) [Em] Mes de ingreso: 1301 [Cu] Fecha actualización por clase: 130506 [Lr] Fecha última revisión: 130506 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 121107 [St] Status: MEDLINE [do] DOI: 10.1073/pnas.1212754109

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[PMID]: 23463648 [Au] Autor: Seror P; Vuillemin V [Ad] Dirección: 146 Laboratoire d'électromyographie, Av. Ledru Rollin 75011, Paris, France. paulseror@gmail.com [Ti] Título: Ulnar nerve lesion at the wrist related to pisotriquetral joint arthropathy. [So] Fuente: Muscle Nerve;47(4):600-4, 2013 Apr. [Is] ISSN: 1097-4598 [Cp] País de publicación: United States [La] Idioma: eng [Ab] Resumen: INTRODUCTION: Ulnar nerve lesions at the wrist (UNLW) are always difficult to localize clinically and sometimes electrophysiologically. Finding conduction block when studying ulnar motor nerve conduction (CB) across the wrist is sometimes the only way to demonstrate that the ulnar deep motor branch (UDMB) is entrapped. METHODS: An elderly woman who had bilateral carpal tunnel syndrome (CTS) and thumb osteoarthritis for many years experienced worsening of left hand impairment recently. RESULTS: Electrodiagnostic and ultrasound examinations revealed an acute and severe UDMB lesion related to pisotriquetral joint effusion. The patient received a local injection of a corticosteroid that provided rapid recovery. CONCLUSIONS: The diagnosis of UDMB lesion is especially difficult when CTS coexists, but CTS may allow for early diagnosis, if CB at the wrist is not overlooked. Chondrocalcinosis was responsible for the systemic inflammation, the CTS, the pisotriquetral joint effusion, and the UDBM compression, which has not been reported previously. [Mh] Términos MeSH primario: Condrocalcinosis/complicaciones Síndromes de Compresión del Nervio Cubital/diagnóstico [Mh] Términos MeSH secundario: Anciano de 80 o más Años Articulaciones del Carpo Síndrome del Túnel Carpiano/etiología Electromiografía Femenino Humanos Conducción Nerviosa Hueso Pisiforme Hueso Piramidal Síndromes de Compresión del Nervio Cubital/etiología Síndromes de Compresión del Nervio Cubital/fisiopatología [Pt] Tipo de publicación: CASE REPORTS; JOURNAL ARTICLE [Em] Mes de ingreso: 1305 [Sb] Subgrupo de revista: IM [Da] Fecha de ingreso para procesamiento: 130325 [St] Status: MEDLINE [do] DOI: 10.1002/mus.23545

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