Recent Advances in Transthyretin Evolution, Structure and Biological Functions

1. Front Matter

   Pages i-xiii

   PDF

2. Mechanisms of Molecular Recognition: Structural Characteristics of Transthyretin Ligand Interactions

   • Vivian Cody, Andrzej Wojtczak

   Pages 1-21

3. Transthyretin Synthesis During Development and Evolution: What the Marsupials Revealed

   • Samantha J. Richardson

   Pages 23-43

4. Evolution of Transthyretin Gene Structure

   • Porntip Prapunpoj

   Pages 45-58

5. Evolutionary Insights from Fish Transthyretin

   • Deborah M. Power, Isabel Morgado, João C. R. Cardoso

   Pages 59-75

6. The Salmonella sp. TLP: A Periplasmic 5-Hydroxyisourate Hydrolase

   • Sarah Hennebry

   Pages 77-94

7. Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin

   • Giuseppe Zanotti, Ileana Ramazzina, Laura Cendron, Claudia Folli, Riccardo Percudani, Rodolfo Berni

   Pages 95-108

8. Transthyretin-Related and Transthyretin-like Proteins

   • A. Elisabeth Sauer-Eriksson, Anna Linusson, Erik Lundberg

   Pages 109-122

9. The Transthyretin—Retinol-Binding Protein Complex

   • Hugo L. Monaco

   Pages 123-142

10. Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology

    • Sancia Gaetani, Diana Bellovino

    Pages 143-157

11. Transthyretin and Endocrine Disruptors

    • Kiyoshi Yamauchi, Akinori Ishihara

    Pages 159-171

12. Genetics: Clinical Implications of Transthyretin Amyloidosis

    • Merrill D Benson

    Pages 173-189

13. Molecular Pathogenesis Associated with Familial Amyloidotic Polyneuropathy

    • Maria João Saraiva

    Pages 191-200

14. Histidine 31: The Achilles' Heel of Human Transthyretin. Microheterogeneity is Not Enough to Understand the Molecular Causes of Amyloidogenicity

    • Klaus Altland, Samantha J. Richardson

    Pages 201-214

15. New Therapeutic Approaches for Familial Amyloidotic Polyneuropathy (FAP)

    • Yukio Ando, Masaaki Nakamura, Mistuharu Ueda, Hirofumi Jono

    Pages 215-238

16. Liver Transplantation for Transthyretin Amyloidosis

    • Bo-Göran Ericzon, Erik Lundgren, Ole B. Suhr

    Pages 239-260

17. Mouse Models of Transthyretin Amyloidosis

    • Sadahiro Ito, Shuichiro Maeda

    Pages 261-280

18. What Have We Learned from Transthyretin-Null Mice: Novel Functions for Transthyretin?

    • João Carlos Sousa, Joana Almeida Palha

    Pages 281-295

19. Transthyretin Null Mice: Developmental Phenotypes

    • Julie A. Monk, Samantha J. Richardson

    Pages 297-310

20. 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

    Pages 311-328

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.

• bacteria
• biology
• growth
• hormone
• mutation
• neuropeptides
• physiology
• protein
• protein structure
• proteins
• synthesis
• thyroid hormone
• Proteomics

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)

• School of Medical Sciences, RMIT University, Bundoora, Australia

  Samantha J. Richardson

• Medical Research Institute, Hauptman-Woodward, Buffalo, USA

  Vivian Cody

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