caa a22 4500 475845714 CHVBK 20180406123913.0 cr unu---uuuuu 170329e20000301xx s 000 0 eng 10.1007/PL00000706 doi (NATIONALLICENCE)springer-10.1007/PL00000706 Immunoglobulin light chains, glycosaminoglycans, and amyloid [Elektronische Daten] [F. J. Stevens*, R. Kisilevsky] Abstract.: Immunoglobulin light chains are the precursor proteins for fibrils that are formed during primary amyloidosis and in amyloidosis associated with multiple myeloma. As found for the approximately 20 currently described forms of focal, localized, or systemic amyloidoses, light chain-related fibrils extracted from physiological deposits are invariably associated with glycosaminoglycans, predominantly heparan sulfate. Other amyloid-related proteins are either structurally normal, such as β2-microglobulin and islet amyloid polypeptide, fragments of normal proteins such as serum amyloid A protein or the precursor protein of the β peptide involved in Alzheimer's disease, or are inherited forms of single amino acid variants of a normal protein such as found in the familial forms of amyloid associated with transthyretin. In contrast, the primary structures of light chains involved in fibril formation exhibit extensive mutational diversity rendering some proteins highly amyloidogenic and others non-pathological. The interactions between light chains and glycosaminoglycans are also affected by amino acid variation and may influence the clinical course of disease by enhancing fibril stability and contributing to resistance to protease degradation. Relatively little is currently known about the mechanisms by which glycosaminoglycans interact with light chains and light-chain fibrils. It is probable that future studies of this uniquely diverse family of proteins will continue o shed light on the processes of amyloidosis, and contribute as well to a greater understanding of the normal physiological roles of glycosaminoglycans. Birkhäuser Verlag Basel,, 2000 Key words. Glycosaminoglycans nationallicence immunoglobulin light chains nationallicence amyloidosis nationallicence amyloid AL nationallicence heparan sulfate nationallicence heparin nationallicence Stevens* F. J. Biosciences Division, Argonne National Laboratory, Argonne (Illinois 60439, USA), Fax +1 630 252 5517, e-mail: stevens@anlcmb.bim.anl.gov, US aut Kisilevsky R. Department of Pathology, Queen's University, Kingston, Ontario, K7L 3N6 (Canada), CA aut https://doi.org/10.1007/PL00000706 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/PL00000706 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Stevens* F. J. Biosciences Division, Argonne National Laboratory, Argonne (Illinois 60439, USA), Fax +1 630 252 5517, e-mail: stevens@anlcmb.bim.anl.gov, US aut NATIONALLICENCE 700 1- Kisilevsky R. Department of Pathology, Queen's University, Kingston, Ontario, K7L 3N6 (Canada), CA aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer