Amyloid Proteins: The Beta Sheet Conformation and Disease by Jean D. Sipe

By Jean D. Sipe

A first-stop reference on proteins linked to amyloidosis. This ebook is the 1st to provide a scientific assessment of all recognized fibril-forming proteins, together with their biochemical features and pathophysiology. It considers the clinically famous amyloid proteins which are identified to be linked to the amyloid protein folding problems, facing their universal structural and thermodynamic positive aspects that bring about amyloid fibril formation and affliction. Emphasis is at the thermodynamics of protein folding, the constitution and physiologic results of universal oligomeric and subfibrillar intermediates and the impact of the extracellular matrix and mobile trafficking and metabolism at the genesis and catabolism of beta pleated sheet proteins. The chapters on particular amyloid proteins all keep on with a standard constitution, permitting easy access to the specified biochemical and clinical facts, making this a useful instrument for clinicians and researchers alike.

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Levine. On the binding of Congo red by amyloid. J Histochem Cytochem 1962, 10, 355–364. , L. Ruinen, J. H. Scholten and A. S. Cohen (eds). Amyloidosis, Excerpta Medica, Amsterdam, 1968. Cohen, A. S. and E. Calkins. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 1959, 183, 1202–1203. , J. Kempf and A. Porte. Structure et formation de la substance amyloide dans l’amylose expérimentale de la Souris. Étude au microscope électronique. C R Acad Sci (Paris) 1960, 250, 1385–1386.

Husby and J. Juul. The complete amino acid se- 102 103 104 105 106 107 108 109 110 quence of a prototype immunoglobulin-k light-chain-type amyloid-fibril protein AR. Biochem J 1981, 195, 561–572. , B. Frangione and E. C. Franklin. Bence Jones proteins and light chains of immunoglobulins. Preferential association of the VkVI subgroup of human light chains with amyloidosis AL(k). J Clin Invest 1982, 70, 453–460. , D. T. Weiss and A. Solomon. Immunoglobulin heavy-chain-associated amyloidosis. Proc Natl Acad Sci USA 1990, 87, 6542–6546.

It was suggested that this property of amyloid depends on an ordered arrangement of the elongated Congo red molecules in the amyloid, indicating that, in fact, the substance is not amorphous, as earlier described, but has an organized substructure [31–34]. A standardized Congo red staining method was introduced by Puchtler et al. [35] and is still used. Additional staining methods have been and are still used. The most important of these is probably Thioflavin T or S. 2 Amyloid Proteins – Modern History There were once divided opinions as to which of the two stainings Congo red or Thioflavin S is more specific for amyloid, but each method now has its own role today in the study of amyloidosis [36].

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