By Jean D. Sipe
A first-stop reference on proteins linked to amyloidosis. This booklet is the 1st to provide a scientific evaluation 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 issues, 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 effect 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 device for clinicians and researchers alike.
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Additional resources for Amyloid Proteins: The Beta Sheet Conformation and Disease
Hawkins and M. B. Pepys. Primary localized orbital amyloidosis composed of the immunoglobulin gamma heavy chain CH3 domain. Clin Sci 1994, 87, 487–491. Engvig, J. , K. E. Olsen, R. E. Gislefoss, K. Sletten, O. Wahlström and P. Westermark. Constant region of a j III immunoglobulin light chain as a major AL-amyloid protein. Scand J Immunol 1998, 48, 92–98. , D. T. Weiss, C. L. Murphy, R. Hrncic, J. S. Wall and M. Schell. Light chain-associated amyloid deposits comprised of a novel kappa constant domain.
A later name has been “amylin”. IAPP was found to be a normal product of islet b cells, and is stored and released together with insulin [169, 170]. Several structural features of IAPP indicated a hormonal nature including C-terminal amidation [171, 172] and it is now accepted as a b-cell hormone, the first discovered since insulin . The identification of IAPP started a new branch in diabetes mellitus research. The interested can go to several reviews [174–176] and to Chapter 28 in this book.
T. Yamada, S. Odani, Y. Nakagawa, M. Arakawa, T. Kunitomo, H. Kataoka, M. Suzuki, Y. Hirasawa, T. Shirahama, A. S. Cohen and K. Schmid. A new form of amyloid protein associated with chronic hemodialysis was identified as b2-microglobulin. Biochem Biophys Res Commun 1985, 129, 701–706. 137 Gorevic, P. , T. T. Casey, W. J. Stone, 138 139 140 141 142 143 144 145 146 C. R. DiRaimondo, F. Prelli and B. Frangione. Beta-2 microglobulin is an amyloidogenic protein in man. J Clin Invest 1985, 76, 2425–2429.