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FEBS Journal

Cover image for Vol. 278 Issue 11

June 2011

Volume 278, Issue 11

Pages 1791–1968

  1. Minireview Series

    1. Top of page
    2. Minireview Series
    3. Minireview
    4. Original Articles
    5. Author Index
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      Natriuretic peptides and their receptors (page 1791)

      Kunio S. Misono

      Article first published online: 9 MAY 2011 | DOI: 10.1111/j.1742-4658.2011.08114.x

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      Natriuretic peptides secreted by the heart play a major role in the regulation of cardiovascular homeostasis and remodeling. This minireview series discusses physiological and pathophysiological roles of natriuretic peptides studied in animals and in humans, the structure and signaling mechanism of the receptors mediating peptides’ activities, and the metabolism of natriuretic peptides.

  2. Minireview

    1. Top of page
    2. Minireview Series
    3. Minireview
    4. Original Articles
    5. Author Index
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      The functional genomics of guanylyl cyclase/natriuretic peptide receptor-A: Perspectives and paradigms (pages 1792–1807)

      Kailash N. Pandey

      Article first published online: 7 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08081.x

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      Molecular approaches to delineate the functional roles of guanylyl cyclase/natriuretic peptide receptor-A (GC-A/NPRA) gene (Npr1) in physiological and pathophysiological disease states including high blood pressure, cardiac hypertrophy, and congestive heart failure are described here. Comparative analyses of biochemical properties and physiological genomics of Npr1 gene should provide enormous potentials in understanding the biological functions of GC-A/NPRA signaling in hypertension and cardiovascular regulation at the molecular level.

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      Natriuretic peptide metabolism, clearance and degradation (pages 1808–1817)

      Lincoln R. Potter

      Article first published online: 7 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08082.x

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      Natriuretic peptides are a family of three related pleiotropic signaling factors that bind and activate transmembrane guanylyl cyclases. This review initially discusses the general characteristics of natriuretic peptides and their receptors. The tissue specific metabolism of natriuretic peptides and their degradation by individual proteases and natriuretic peptide receptor C-mediated internalization are then more specifically discussed.

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      Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase (pages 1818–1829)

      Kunio S. Misono, John S. Philo, Tsutomu Arakawa, Craig M. Ogata, Yue Qiu, Haruo Ogawa and Howard S. Young

      Article first published online: 7 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08083.x

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      Atrial natriuretic peptide plays a central role in cardiovascular homeostasis through their natriuretic, vasorelaxant, and anti-hypertrophic activities. Such activities are mediated by the guanylate cyclase-linked, single transmembrane segment receptor functioning as a homodimer. Studies have revealed the structural mechanisms of transmembrane signaling and possible chloride-dependent allosteric control of the receptor activity in the kidney.

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      Natriuretic peptide system: an overview of studies using genetically engineered animal models (pages 1830–1841)

      Ichiro Kishimoto, Takeshi Tokudome, Kazuwa Nakao and Kenji Kangawa

      Article first published online: 9 MAY 2011 | DOI: 10.1111/j.1742-4658.2011.08116.x

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      In addition to the effects of their actions as circulating hormones, current evidence suggests that natriuretic peptides exert local effects by acting as autocrine/paracrine hormones. The present review focuses on the new insights in the in vivo significance of the natriuretic peptide system in cardiovascular, renal and skeletal homeostasis, which have been recently revealed by genetically engineered animal models.

  3. Original Articles

    1. Top of page
    2. Minireview Series
    3. Minireview
    4. Original Articles
    5. Author Index
    1. You have free access to this content
      Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae (pages 1842–1853)

      Malea M. Kneen, Razvan Stan, Alejandra Yep, Ryan P. Tyler, Choedchai Saehuan and Michael J. McLeish

      Article first published online: 18 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08103.x

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      The S. cerevisiae ARO10 gene product was shown to be an efficient aromatic 2-ketoacid decarboxylase. Its substrate spectrum suggests that it is unlikely to play any significant role in the catabolism of methionine or branched-chain amino acids. Homology modeling and site-directed mutagenesis were used to identify residues involved in substrate specificity, with the E545L variant unexpectedly exhibiting allosteric activation.

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      Binding of cGMP to the transducin-activated cGMP phosphodiesterase, PDE6, initiates a large conformational change involved in its deactivation (pages 1854–1872)

      Akio Yamazaki, Fumio Hayashi, Isao Matsuura and Vladimir A. Bondarenko

      Article first published online: 20 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08104.x

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      Pαβγ slowly changes its conformation after cGMP binding, i.e., after formation of Pαβγ containing two cGMPs. Binding of Pγ accelerates the conformational change caused by cGMP, but does not add another change. Pαβγ changes its conformation during its inactivation and that the binding of cGMP and Pγ is crucial for this change.

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      Increased expression of c-Fos by extracellular signal-regulated kinase activation under sustained oxidative stress elicits BimEL upregulation and hepatocyte apoptosis (pages 1873–1881)

      Yasuhiro Ishihara, Fumiaki Ito and Norio Shimamoto

      Article first published online: 28 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08105.x

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      We previously showed that BimEL was deeply involved in hepatocyte apoptosis under oxidative stress conditions. The Bim promoter region includes an AP-1 binding site, a FOXO binding site, and three myb binding sites. In this study, we found that a component of AP-1, c-Fos is critical for BimEL upregulation and apoptosis.

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      Human kynurenine aminotransferase II – reactivity with substrates and inhibitors (pages 1882–1900)

      Elisabetta Passera, Barbara Campanini, Franca Rossi, Valentina Casazza, Menico Rizzi, Roberto Pellicciari and Andrea Mozzarelli

      Article first published online: 28 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08106.x

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      Kynurenine aminotransferase (KAT) is a pyridoxal 5′-phosphate-dependent enzyme catalyzing the formation of kynurenic acid, an antagonist of excitatory receptors in the CNS. KATII is a potential drug target for the treatment of schizophrenia. KATII spectroscopy, transamination and β-lytic activity were characterized with substrate and substrate analogs using novel continuous and high-throughput assays.

      Corrected by:

      Corrigendum: Corrigendum

      Vol. 280, Issue 23, 6274, Article first published online: 20 NOV 2013

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      An alternative mature form of subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis identified in the presence of Ca2+ (pages 1901–1911)

      Nitat Sinsereekul, Tita Foophow, Mai Yamanouchi, Yuichi Koga, Kazufumi Takano and Shigenori Kanaya

      Article first published online: 13 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08107.x

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      A subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis is thought to be matured from its inactive precursor Pro-Tk-SP upon autoprocessing of the N-and C-propeptides. In this study, however, we showed that the Pro-Tk-SP derivative with the N-propeptide removed, ProC-Tk-SP, represents a mature form of Pro-Tk-SP in a natural environment. The C-propeptide contributes to the stabilization of ProC-Tk-SP.

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      On the aggregation properties of FMRP – a link with the FXTAS syndrome? (pages 1912–1921)

      Ljiljana Sjekloća, Kris Pauwels and Annalisa Pastore

      Article first published online: 9 MAY 2011 | DOI: 10.1111/j.1742-4658.2011.08108.x

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      Lack of the Fragile X mental retardation protein (FMRP) causes an inherited mental retardation in humans. We describe here that constructs spanning the conserved N-terminus of FMRP and of the two homologues, FXR1P and FXR2P, have an intrinsic tendency to aggregate and misfold towards beta-rich structures, also under non-destabilizing conditions. These findings suggest a link with FMRP associated pathologies.

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      Germinal center-specific protein human germinal center associated lymphoma directly interacts with both myosin and actin and increases the binding of myosin to actin (pages 1922–1931)

      Xiaoqing Lu, Katarzyna Kazmierczak, Xiaoyu Jiang, Michelle Jones, James Watt, David M. Helfman, Jeffrey R. Moore, Danuta Szczesna-Cordary and Izidore S. Lossos

      Article first published online: 20 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08109.x

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      HGAL is a germinal center-specific gene negatively regulating lymphocyte motility. We demonstrate that HGAL interacts directly and independently with actin and myosin and delineates the HGAL and myosin domains responsible for the interaction, and HGAL increases the binding of myosin to F-actin and inhibits the ability of myosin to translocate actin by reducing the maximal velocity of myosin head/actin movement.

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      Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis – distal effects on dimer stability (pages 1932–1943)

      Moumita Samanta, Mousumi Banerjee, Mathur R. N. Murthy, Hemalatha Balaram and Padmanabhan Balaram

      Article first published online: 28 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08110.x

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      The role of the fully conserved Cys126 residue in triosephosphate isomerase is probed using the engineered mutants, C126S, C126A, C126V, C126M and C126T of the Plasmodium falciparum enzyme. The mutant enzymes exhibited diminished thermal stability at low concentration, suggesting that Cys126 contributes to dimer stability through a crucial network of interactions.

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      Crystal structure of basic 7S globulin, a xyloglucan-specific endo-β-1,4-glucanase inhibitor protein-like protein from soybean lacking inhibitory activity against endo-β-glucanase (pages 1944–1954)

      Takuya Yoshizawa, Toshiyuki Shimizu, Mayuki Yamabe, Misako Taichi, Yuji Nishiuchi, Naoki Shichijo, Satoru Unzai, Hisashi Hirano, Mamoru Sato and Hiroshi Hashimoto

      Article first published online: 28 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08111.x

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      Basic 7S globulin (Bg7S) from soybean is a homologous protein of a proteinaceous inhibitor against endo-β-glucanases from fungi. We reveal that Bg7S lacks inhibition activity against endo-β-glucanases and the structural basis of why Bg7S lacks inhibition activity. Assembly of Bg7S is dynamically altered by pH. The structure provides structural implication of dynamic assembly of Bg7S.

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      The toxicity of bovine α-lactalbumin made lethal to tumor cells is highly dependent on oleic acid and induces killing in cancer cell lines and noncancer-derived primary cells (pages 1955–1967)

      Christel Rothe Brinkmann, Christian Würtz Heegaard, Torben Ellebæk Petersen, Jens Christian Jensenius and Steffen Thiel

      Article first published online: 28 APR 2011 | DOI: 10.1111/j.1742-4658.2011.08112.x

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      A complex between α-lactalbumin and oleic acid has been reported to be cytotoxic to cancer cells. We have prepared such complexes and tested the activity against cancer cell lines and non-cancer-derived primary cells. Interestingly, some primary cell types were more sensitive to treatment than cancer cell lines, and we found the activity to be mediated by the oleic acid.

  4. Author Index

    1. Top of page
    2. Minireview Series
    3. Minireview
    4. Original Articles
    5. Author Index
    1. You have free access to this content
      Author index (page 1968)

      Article first published online: 17 MAY 2011 | DOI: 10.1111/j.1742-4658.2011.07847.x

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