Ebook: Recent Advances in Transthyretin Evolution, Structure and Biological Functions
- Tags: Human Physiology, Endocrinology, Proteomics
- Year: 2009
- Publisher: Springer-Verlag Berlin Heidelberg
- Edition: 1
- Language: English
- pdf
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 clinical research into TTR.
Transthyretin is a protein found in human blood and cerebrospinal fluid. It is directly involved in the transport of thyroid hormones, and indirectly in that of retinol. These hormones are essential for normal growth and development, particularly that of the brain. Spontaneous and inherited diseases affecting transthyretin result in amyloidosis. More than 80 point mutations in transthyretin lead to a variety of illnesses. Liver transplants are the most common treatment, although much research is also being carried out in drug therapies.
The evolution of transthyretin has been extensively investigated – from humans to bacteria, invertebrate animals and plants. The structure of the protein has not changed, but its function has changed significantly. This is a most exciting example for the study of the evolution of protein structure-function relationships.
This monograph will bring the reader up to date on the latest developments and discoveries.
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 clinical research into TTR.
Transthyretin is a protein found in human blood and cerebrospinal fluid. It is directly involved in the transport of thyroid hormones, and indirectly in that of retinol. These hormones are essential for normal growth and development, particularly that of the brain. Spontaneous and inherited diseases affecting transthyretin result in amyloidosis. More than 80 point mutations in transthyretin lead to a variety of illnesses. Liver transplants are the most common treatment, although much research is also being carried out in drug therapies.
The evolution of transthyretin has been extensively investigated – from humans to bacteria, invertebrate animals and plants. The structure of the protein has not changed, but its function has changed significantly. This is a most exciting example for the study of the evolution of protein structure-function relationships.
This monograph will bring the reader up to date on the latest developments and discoveries.
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 clinical research into TTR.
Transthyretin is a protein found in human blood and cerebrospinal fluid. It is directly involved in the transport of thyroid hormones, and indirectly in that of retinol. These hormones are essential for normal growth and development, particularly that of the brain. Spontaneous and inherited diseases affecting transthyretin result in amyloidosis. More than 80 point mutations in transthyretin lead to a variety of illnesses. Liver transplants are the most common treatment, although much research is also being carried out in drug therapies.
The evolution of transthyretin has been extensively investigated – from humans to bacteria, invertebrate animals and plants. The structure of the protein has not changed, but its function has changed significantly. This is a most exciting example for the study of the evolution of protein structure-function relationships.
This monograph will bring the reader up to date on the latest developments and discoveries.
Content:
Front Matter....Pages i-xiii
Mechanisms of Molecular Recognition: Structural Characteristics of Transthyretin Ligand Interactions....Pages 1-21
Transthyretin Synthesis During Development and Evolution: What the Marsupials Revealed....Pages 23-43
Evolution of Transthyretin Gene Structure....Pages 45-58
Evolutionary Insights from Fish Transthyretin....Pages 59-75
The Salmonella sp. TLP: A Periplasmic 5-Hydroxyisourate Hydrolase....Pages 77-94
Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin....Pages 95-108
Transthyretin-Related and Transthyretin-like Proteins....Pages 109-122
The Transthyretin—Retinol-Binding Protein Complex....Pages 123-142
Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology....Pages 143-157
Transthyretin and Endocrine Disruptors....Pages 159-171
Genetics: Clinical Implications of Transthyretin Amyloidosis....Pages 173-189
Molecular Pathogenesis Associated with Familial Amyloidotic Polyneuropathy....Pages 191-200
Histidine 31: The Achilles' Heel of Human Transthyretin. Microheterogeneity is Not Enough to Understand the Molecular Causes of Amyloidogenicity....Pages 201-214
New Therapeutic Approaches for Familial Amyloidotic Polyneuropathy (FAP)....Pages 215-238
Liver Transplantation for Transthyretin Amyloidosis....Pages 239-260
Mouse Models of Transthyretin Amyloidosis....Pages 261-280
What Have We Learned from Transthyretin-Null Mice: Novel Functions for Transthyretin?....Pages 281-295
Transthyretin Null Mice: Developmental Phenotypes....Pages 297-310
Transthyretin Null Mice as a Model to Study the Involvement of Transthyretin in Neurobiology: From Neuropeptide Processing to Nerve Regeneration....Pages 311-328
Plasma Transthyretin Reflects the Fluctuations of Lean Body Mass in Health and Disease....Pages 329-357
Back Matter....Pages 359-360
Erratum to....Pages 361-362
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 clinical research into TTR.
Transthyretin is a protein found in human blood and cerebrospinal fluid. It is directly involved in the transport of thyroid hormones, and indirectly in that of retinol. These hormones are essential for normal growth and development, particularly that of the brain. Spontaneous and inherited diseases affecting transthyretin result in amyloidosis. More than 80 point mutations in transthyretin lead to a variety of illnesses. Liver transplants are the most common treatment, although much research is also being carried out in drug therapies.
The evolution of transthyretin has been extensively investigated – from humans to bacteria, invertebrate animals and plants. The structure of the protein has not changed, but its function has changed significantly. This is a most exciting example for the study of the evolution of protein structure-function relationships.
This monograph will bring the reader up to date on the latest developments and discoveries.
Content:
Front Matter....Pages i-xiii
Mechanisms of Molecular Recognition: Structural Characteristics of Transthyretin Ligand Interactions....Pages 1-21
Transthyretin Synthesis During Development and Evolution: What the Marsupials Revealed....Pages 23-43
Evolution of Transthyretin Gene Structure....Pages 45-58
Evolutionary Insights from Fish Transthyretin....Pages 59-75
The Salmonella sp. TLP: A Periplasmic 5-Hydroxyisourate Hydrolase....Pages 77-94
Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin....Pages 95-108
Transthyretin-Related and Transthyretin-like Proteins....Pages 109-122
The Transthyretin—Retinol-Binding Protein Complex....Pages 123-142
Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology....Pages 143-157
Transthyretin and Endocrine Disruptors....Pages 159-171
Genetics: Clinical Implications of Transthyretin Amyloidosis....Pages 173-189
Molecular Pathogenesis Associated with Familial Amyloidotic Polyneuropathy....Pages 191-200
Histidine 31: The Achilles' Heel of Human Transthyretin. Microheterogeneity is Not Enough to Understand the Molecular Causes of Amyloidogenicity....Pages 201-214
New Therapeutic Approaches for Familial Amyloidotic Polyneuropathy (FAP)....Pages 215-238
Liver Transplantation for Transthyretin Amyloidosis....Pages 239-260
Mouse Models of Transthyretin Amyloidosis....Pages 261-280
What Have We Learned from Transthyretin-Null Mice: Novel Functions for Transthyretin?....Pages 281-295
Transthyretin Null Mice: Developmental Phenotypes....Pages 297-310
Transthyretin Null Mice as a Model to Study the Involvement of Transthyretin in Neurobiology: From Neuropeptide Processing to Nerve Regeneration....Pages 311-328
Plasma Transthyretin Reflects the Fluctuations of Lean Body Mass in Health and Disease....Pages 329-357
Back Matter....Pages 359-360
Erratum to....Pages 361-362
....