Recent Advances in Transthyretin Evolution, Structure and Biological Functions
There is a strong interest in transthyretin (TTR) in connection with protein evolution, medical and clinical research. Thus, this is an exciting time for experts in TTR research to come together to write a monograph covering both the basic and the clinica
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Samantha J. Richardson
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Vivian Cody
Recent Advances in Transthyretin Evolution, Structure and Biological Functions
Dr. Samantha J. Richardson RMIT University School of Medical Sciences Bundoora VIC 3083 Bundoora West Campus Australia [email protected]
Dr. Vivian Cody Hauptman-Woodward Medical Research Institute 700 Elliott Street Buffalo NY 14203 USA [email protected]
ISBN 978-3-642-00645-6 e-ISBN 978-3-642-00646-3 DOI: 10.1007/978-3-642-00646-3 Springer Dordrecht Heidelberg London New York Library of Congress Control Number: 2009926025 # 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, and 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, and 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 and regulations and 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 and 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 and other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal fluid barrier), retinal pigment epithelium of the eye, pancreas, intestine and 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, and 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, and 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 and human) has not changed in its overall structure. Despite this, TTRs i
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