Amyloidosis
Editat de J. Marrink, M.H. van Rijswijken Limba Engleză Paperback – 26 sep 2011
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Specificații
ISBN-13: 9789401084154
ISBN-10: 9401084157
Pagini: 400
Ilustrații: 396 p.
Dimensiuni: 155 x 235 x 21 mm
Greutate: 0.56 kg
Ediția:Softcover reprint of the original 1st ed. 1986
Editura: SPRINGER NETHERLANDS
Colecția Springer
Locul publicării:Dordrecht, Netherlands
ISBN-10: 9401084157
Pagini: 400
Ilustrații: 396 p.
Dimensiuni: 155 x 235 x 21 mm
Greutate: 0.56 kg
Ediția:Softcover reprint of the original 1st ed. 1986
Editura: SPRINGER NETHERLANDS
Colecția Springer
Locul publicării:Dordrecht, Netherlands
Public țintă
ResearchCuprins
Section I.- I.1 General introduction and a brief history of amyloidosis.- Section II Chemical and Ultrastructural Aspects.- II.1 Amyloid proteins.- II.2 Carbohydrate-containing AL proteins.- II.3 Endocrine amyloid fibril proteins.- II.4 Amyloid P-component: structure and properties.- II.5 A brief review of the ultrastructure of amyloid.- Section III Clinical Aspects.- III.1 Clinical evaluation of AA and AL amyloid disease.- III.2 Cardiac involvement in amyloidosis.- III.3 Hemodialysis-associated amyloid of ?2-microglobulin nature.- III.4 Amyloid P-component: clinical implications.- Section IV Pathogenesis.- IV.1 Amyloid protein AA and its precursor, the acute phase proteins(s) ApoSAA: a perspective.- IV.2 Sites and regulation of biosynthesis of SAA.- IV.3 Serum amyloid A protein in plasma: characteristics of acute phase HDL.- IV.4 Correlation between sequence variability and structure prediction in AA proteins.- IV.5 Gene structure of a human serum amyloid A protein and comparison with amyloid A.- IV.6 Structure and expression of murine serum amyloid A protein genes: implications for amyloidogenesis.- IV.7 Amyloidogenic proteins in human central nervous system diseases.- IV.8 Structure of the Alzheimer paired helical filament.- IV.9 The significance of non-protein AA material in water-soluble bovine AA-amyloid fibrils.- IV.10 Fibril derived Amyloid Enhancing Factor (FAEF) in hamster: evidence for a close relationship between AEF and AA-amyloid fibrils.- Section V Familial Amyloidosis.- V.1 The hereditary amyloidoses.- V.2 Familial amyloidotic polyneuropathies.- V.3 Biochemical and genetic characterization of a variant transthyretin causing familial amyloidotic polyneuropathy.- Section VI Senile Amyloidosis.- VI.1 The nature and pathogenesis of the amyloid deposits inAlzheimer’s disease.- VI.2 Biochemistry of cerebral amyloid in Alzheimer’s disease, the unconventional slow virus diseases and Icelandic cerebrovascular amyloidosis.- VI.3 Amyloid of the islets of Langerhans and its connection with diabetes mellitus.- VI.4 Senile amyloid affecting the heart.- VI.5 Amyloid arthropathy.- VI.6 Peripheral angiopathy.- VI.7 Animal models.- Section VII Experimental Amyloidosis.- VII.1 Pathology of experimental amyloidosis.- VII.2 What factors are necessary for the induction of AA amyloidosis? (AA amyloid, glycosaminoglycans, amyloid enhancing factor, apo-SAA).- VII.3 Amyloidogenic proteins in mice.- VII.4 Sites of SAA/AA synthesis.- VII.5 The role of the macrophage phagocytic system (MPS) in the development of secondary amyloidosis.- VII.6 SAA kinetics in animals.- VII.7 Amyloid and female protein: sex-related occurrence in the Syrian hamster.- VII.8 Endocrine amyloid in animals.- VII.9 Dietary treatment during the induction and resorption phases of experimental amyloidosis.- Section VIII.- Section VIII.1 Future directions in amyloid research.- Contributors.