Overview
- Editors:
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Samantha J. Richardson
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School of Medical Sciences, RMIT University, Bundoora, Australia
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Vivian Cody
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Medical Research Institute, Hauptman-Woodward, Buffalo, USA
Transthyretin is a most exciting example for the study of the evolution of protein structure-function relationships
Covers both the basic and the clinical research into transthyretin
Brings the reader up to date on the latest developments and discoveries
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Table of contents (21 chapters)
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Front Matter
Pages i-xiii
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- Vivian Cody, Andrzej Wojtczak
Pages 1-21
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- Deborah M. Power, Isabel Morgado, João C. R. Cardoso
Pages 59-75
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- Giuseppe Zanotti, Ileana Ramazzina, Laura Cendron, Claudia Folli, Riccardo Percudani, Rodolfo Berni
Pages 95-108
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- A. Elisabeth Sauer-Eriksson, Anna Linusson, Erik Lundberg
Pages 109-122
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- Sancia Gaetani, Diana Bellovino
Pages 143-157
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- Kiyoshi Yamauchi, Akinori Ishihara
Pages 159-171
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- Klaus Altland, Samantha J. Richardson
Pages 201-214
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- Yukio Ando, Masaaki Nakamura, Mistuharu Ueda, Hirofumi Jono
Pages 215-238
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- Bo-Göran Ericzon, Erik Lundgren, Ole B. Suhr
Pages 239-260
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- Sadahiro Ito, Shuichiro Maeda
Pages 261-280
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- João Carlos Sousa, Joana Almeida Palha
Pages 281-295
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- Julie A. Monk, Samantha J. Richardson
Pages 297-310
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- Carolina Estima Fleming, Ana Filipa Nunes, Márcia Almeida Liz, Mónica Mendes Sousa
Pages 311-328
About this book
Since its ?rst description in 1942 in both serum and cerebrospinal ?uid, 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 ?uid 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 ?avonoids. 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.
Reviews
From the reviews:
“Transthyretin (TTR) is a relatively abundant thyroid hormone carrier protein found in the blood of vertebrates. … The authors of the book Recent Advances in Transthyretin Evolution, Structure and Biological Functions have produced a comprehensive reference text that does much to reconcile the evolutionary biology, structure-function relationships and pathophysiology of this remarkable protein. … In summary, this … text will prove to be essential reading for both expert and non-expert researchers in the field of TTR biology.” (Rob Gasperini, Australian Biochemist, Vol. 41 (1), April, 2010)
Editors and Affiliations
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School of Medical Sciences, RMIT University, Bundoora, Australia
Samantha J. Richardson
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Medical Research Institute, Hauptman-Woodward, Buffalo, USA
Vivian Cody
