Recent Advances in Transthyretin Evolution, Structure and Biological Functions

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Recent Advances in Transthyretin Evolution, Structure Biological Functions Samantha J. Richardson l Vivian Cody Recent Advances in Transthyretin Evolution, Structure Biological Functions Dr. Samantha J.
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Recent Advances in Transthyretin Evolution, Structure Biological Functions Samantha J. Richardson l Vivian Cody Recent Advances in Transthyretin Evolution, Structure Biological Functions Dr. Samantha J. Richardson RMIT University School of Medical Sciences Bundoora VIC 3083 Bundoora West Campus Australia Dr. Vivian Cody Hauptman-Woodward Medical Research Institute 700 Elliott Street Buffalo NY USA ISBN e-isbn DOI: / Springer Dordrecht Heidelberg London New York Library of Congress Control Number: # Springer-Verlag Berlin Heidelberg 2009 This work is subject to copyright. All rights are reserved, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilm or in any other way, storage in data banks. Duplication of this publication or parts thereof is permitted only under the provisions of the German Copyright Law of September 9, 1965, in its current version, permission for use must always be obtained from Springer. Violations are liable to prosecution under the German Copyright Law. The use of general descriptive names, registered names, trademarks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws regulations therefore free for general use. Cover design: WMXDesign GmbH, Heidelberg, Germany Printed on acid-free paper Springer is part of Springer Science+Business Media (www.springer.com) Preface Since its first description in 1942 in both serum cerebrospinal fluid, transthyretin (TTR) has had an eventful history, including changes in name from prealbumin to thyroxine-binding prealbumin to transthyretin as knowledge increased about its functions. TTR is synthesised in a wide range of tissues in humans other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal fluid barrier), retinal pigment epithelium of the eye, pancreas, intestine meninges. However, its sites of synthesis are more restricted in other vertebrates. This implies that the number of tissues synthesising TTR during vertebrate evolution has increased, raises questions about the selection pressures governing TTR synthesis. TTR is most widely known as a distributor of thyroid hormones. In addition, TTR binds retinol-binding protein, which binds retinol. In this way, TTR is also involved with retinoid distribution. More recently, TTR has been demonstrated to bind a wide variety of endocrine disruptors including drugs, pollutants, industrial compounds, heavy metals, some naturally occurring plant flavonoids. These not only interfere with thyroid hormone delivery in the body, but also transport such endocrine disruptors into the brain, where they have the potential to accumulate. The X-ray crystal structure of TTR from vertebrates (fish, chicken, rat, mouse human) has not changed in its overall structure. Despite this, TTRs in fish, amphibians, reptiles birds bind T3 with higher affinity than T4, whereas in mammals, while maintaining the same three-dimensional structure in the binding site, TTR binds T4 with higher affinity than T3. The high conservation of quaternary, tertiary, secondary primary structure, in combination with the sequencing of many non-vertebrate genomes, has allowed the identification of genes coding for TTR-Like Proteins (TLPs) in microbes, plants non-vertebrate animals. TLPs studied to date do not bind thyroid hormones, but have 5-hydroxyisourate hydrolase activity. The change in function from 5-HIUase in bacteria to distributor of T3 in fish, amphibians, reptiles birds, to distributor of T4 in mammals, yet maintaining the same overall three-dimensional structure, renders TLP/TTR an excellent model for the study of protein evolution. The function of TTR is still considered controversial by some researchers, as TTR null mice were originally reported to be without an overt phenotype. There exists the possibility that the lack of phenotype is due to redundancies in thyroid v vi Preface hormone retinoid metabolism, also that mice living in animal houses in laboratories are not subjected to the same stresses as those in the wild; thus the phenotype is not seen under laboratory conditions. Intriguingly, there are no reports of humans lacking TTR. However, more recent studies have revealed a variety of phenotypes in TTR null mice, shedding light on previously unknown roles of TTR in development neurobiology. TTR is also widely implicated in human health disease. TTR is used as a nutritional marker, also as an indicator of recovery following some diseases surgery. Perhaps the most prolific area of TTR research concerns human TTR amyloid formation. There are two main types of TTR amyloid: familial amyloidotic polyneuropathy (FAP) is an autosomal dominant inherited mutation in the TTR gene causing polyneuropathy, whereas senile systemic amyloidosis (SSA; also known as senile cardiac amyloidosis, SCA) is age-dependent the amyloid fibrils contain wild type TTR. Of the 127 amino acids in the polypeptide, there are at least 100 point mutations that result in FAP. Therefore, there is an urgent need for continued research into the mechanisms of TTR amyloid formation, for the development of therapeutics including drugs, gene therapy organ transplants. Thus, progress in medical research into TTR is fundamental to human health. TTR is a fascinating protein from the st point of protein evolution, also in medicine. Thus, this is an exciting time for experts in TTR research to come together to write this monograph that covers both the basic the clinical research in TTR. This monograph describes each of the above-mentioned aspects of TTR brings the reader up to date on the latest developments discoveries. March 2009 Samantha J. Richardson Vivian Cody Contents 1 Mechanisms of Molecular Recognition: Structural Characteristics of Transthyretin Lig Interactions... 1 Vivian Cody Andrzej Wojtczak 2 Transthyretin Synthesis During Development Evolution: What the Marsupials Revealed Samantha J. Richardson 3 Evolution of Transthyretin Gene Structure Porntip Prapunpoj 4 Evolutionary Insights from Fish Transthyretin Deborah M. Power, Isabel Morgado, João C.R. Cardoso 5 The Salmonella sp. TLP: A Periplasmic 5-Hydroxyisourate Hydrolase Sarah Hennebry 6 Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, Evolutionary Relationship with Transthyretin Giuseppe Zanotti, Ileana Ramazzina, Laura Cendron, Claudia Folli, Riccardo Percudani, Rodolfo Berni 7 Transthyretin-Related Transthyretin-like Proteins A. Elisabeth Sauer-Eriksson, Anna Linusson, Erik Lundberg 8 The Transthyretin Retinol-Binding Protein Complex Hugo L. Monaco 9 Transthyretin Retinol-Binding Protein: Implications in Fish Physiology Sancia Gaetani Diana Bellovino vii viii Contents 10 Transthyretin Endocrine Disruptors Kiyoshi Yamauchi Akinori Ishihara 11 Genetics: Clinical Implications of Transthyretin Amyloidosis Merrill D. Benson 12 Molecular Pathogenesis Associated with Familial Amyloidotic Polyneuropathy Maria João Saraiva 13 Histidine 31: The Achilles Heel of Human Transthyretin. Microheterogeneity is Not Enough to Underst the Molecular Causes of Amyloidogenicity Klaus Altl Samantha J. Richardson 14 New Therapeutic Approaches for Familial Amyloidotic Polyneuropathy (FAP) Yukio Ando, Masaaki Nakamura, Mistuharu Ueda, Hirofumi Jono 15 Liver Transplantation for Transthyretin Amyloidosis Bo-Goran Ericzon, Erik Lundgren, Ole B. Suhr 16 Mouse Models of Transthyretin Amyloidosis Sadahiro Ito Shuichiro Maeda 17 What Have We Learned from Transthyretin-Null Mice: Novel Functions for Transthyretin? João Carlos Sousa Joana Almeida Palha 18 Transthyretin Null Mice: Developmental Phenotypes Julie A. Monk Samantha J. Richardson 19 Transthyretin Null Mice as a Model to Study the Involvement of Transthyretin in Neurobiology: From Neuropeptide Processing to Nerve Regeneration Carolina Estima Fleming, Ana Filipa Nunes, Márcia Almeida Liz, Mónica Mendes Sousa 20 Plasma Transthyretin Reflects the Fluctuations of Lean Body Mass in Health Disease Yves Ingenbleek Index Contributors Klaus Altl Justus-Liebig-University, Institute of Human Genetics Schlangenzahl 14, Giessen, Germany Yukio Ando Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Honjo, Kumamoto , Japan Diana Bellovino National Research Institute on Food Nutrition, Via Ardeatina 546, Rome, Italy Merrill D. Benson Indiana University School of Medicine, 635 Barnhill Drive, MS-128, Indianapolis, IN , USA Rodolfo Berni Department of Biochemistry Molecular Biology, University of Parma, Viale delle Scienze 23/A, Parma, Italy João C.R. Cardoso Comparative Molecular Endocrinology Group, Centre for Marine Sciences (CCMAR), Universidade do Algarve, Campus do Gambelas, Faro, Portugal Laura Cendron Department of Chemistry, University of Padua, ICB-CNR, Section of Padua, Via Marzolo 1, Padova, Italy Venetian Institute of Molecular Medicine, Via Orus 2, Padua, Italy Vivian Cody Structural Biology Department, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, NY 14203, USA ix x Contributors Bo-Goran Ericzon Head Division of Transplantation Surgery, CLINTEC, Karolinska Institutet, Karolinska University Hospital Huddinge, F82, Stockholm, Sweden Carolina Estima Fleming Nerve Regeneration Group, Instituto de Biologia Molecular e Celular IBMC, Universidade do Porto, R Campo Alegre 823, 4150 Porto, Portugal Claudia Folli Department of Biochemistry Molecular Biology, University of Parma, Viale delle Scienze 23/A, Parma, Italy Sancia Gaetani National Research Institute on Food Nutrition, Via Ardeatina 546, Rome, Italy Sarah Hennebry Human Neurotransmitters Laboratory, Baker IDI Heart Diabetes Institute, Melbourne, VIC, Australia Yves Ingenbleek Laboratory of Nutrition, Faculty of Pharmacy, University Louis Pasteur, Strasbourg 1, France 15 bis, rue de la Vise, Balaruc-le-Vieux, France Akinori Ishihara Department of Biological Science, Faculty of Science, Shizuoka University, Shizuoka, Japan Sadahiro Ito Department of Biochemistry, Interdisciplinary Graduate School of Medicine Engineering, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi , Japan Center for Life Science Research, Interdisciplinary Graduate School of Medicine Engineering, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi , Japan Hirofumi Jono Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Honjo, Kumamoto , Japan Contributors xi Anna Linusson Department of Chemistry, Umeå University, Umeå, Sweden Márcia Almeida Liz Nerve Regeneration Group, Instituto de Biologia Molecular e Celular IBMC, Universidade do Porto, R Campo Alegre 823, 4150 Porto, Portugal Erik Lundgren Department of Molecular Biology, Umeå University, Umeå, Sweden Department of Chemistry, Umeå University, Umeå, Sweden Shuichiro Maeda Department of Biochemistry, Interdisciplinary Graduate School of Medicine Engineering, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi , Japan Hugo L. Monaco Biocrystallography Laboratory, Department of Biotechnology, University of Verona, Strada Le Grazie 15, Verona, Italy Julie A. Monk ProScribe Medical Communications, 481 Gilbert Rd., Preston, VIC 3072, Australia url: Isabel Morgado Comparative Molecular Endocrinology Group, Centre for Marine Sciences (CCMAR), Universidade do Algarve, Campus do Gambelas, Faro, Portugal Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, Halle (Saale), Germany Masaaki Nakamura Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Honjo, Kumamoto , Japan Ana Filipa Nunes Nerve Regeneration Group, Instituto de Biologia Molecular e Celular IBMC, Universidade do Porto, R Campo Alegre 823, 4150 Porto, Portugal xii Contributors Joana Almeida Palha Life Health Sciences Research Institute (ICVS), School of Health Sciences, University of Minho, Campus de Gualtar, Braga, Portugal Riccardo Percudani Department of Biochemistry Molecular Biology, University of Parma, Viale delle Scienze 23/A, Parma, Italy Deborah M. Power Comparative Molecular Endocrinology Group, Centre for Marine Sciences (CCMAR), Universidade do Algarve, Campus do Gambelas, Faro, Portugal Porntip Prapunpoj Department of Biochemistry, Faculty of Science, Prince of Songkla University, Hat Yai, Songkhla 90112, Thail Ileana Ramazzina Department of Biochemistry Molecular Biology, University of Parma, Viale delle Scienze 23/A, Parma, Italy Samantha J. Richardson School of Medical Sciences, RMIT University, P.O. Box 71, Bundoora, 3083 VIC, Australia Maria João Saraiva Molecular Neurobiology Group, IBMC Instituto de Biologia Molecular e Celular, R Campo Alegre 823, 4150 Porto, Portugal ICBAS Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Porto, Portugal A. Elisabeth Sauer-Eriksson Department of Chemistry, Umeå University, Umeå, Sweden João Carlos Sousa Life Health Sciences Research Institute (ICVS), School of Health Sciences, University of Minho, Campus de Gualtar, Braga, Portugal Mónica Mendes Sousa Nerve Regeneration Group, Instituto de Biologia Molecular e Celular IBMC, Universidade do Porto, R Campo Alegre 823, 4150 Porto, Portugal Contributors xiii Ole B. Suhr Department of Medicine, Section for Gastroenterology Hepatology, Umeå University Hospital, Umeå, Sweden Mistuharu Ueda Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Honjo, Kumamoto , Japan Andrzej Wojtczak Chemistry Department, N. Copernicus University, Torun, Pol Kiyoshi Yamauchi Department of Biological Science, Faculty of Science, Shizuoka University, Shizuoka, Japan Giuseppe Zanotti Department of Chemistry, University of Padua, ICB-CNR, Section of Padua, Via Marzolo 1, Padova, Italy Venetian Institute of Molecular Medicine, Via Orus 2, Padua, Italy
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