The amino acid sequence of the glycosylated amyloid immunoglobulin light chain protein AL MS

Scandinavian Journal of Immunology

Volumn 45, Issue 5, 1997, Pages 551-556

  Omtvedt, L A ^a   Husby, G ^a   Cornwell III, G G ^b   Kyle, R A ^c   Sletten, K ^a  

^a UNIVERSITY OF OSLO   (Norway)

^b DARTMOUTH HITCHCOCK MEDICAL CENTER   (United States)

^c MAYO CLINIC COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; CASE REPORT; GLYCOSYLATION; HUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

EID: 0030915212     PISSN: 03009475     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-3083.1997.d01-431.x     Document Type: Article

References (29)

1. Putchler H, Sweat F, Levine M. On the binding of Congo red by amyloid. J Histochem Cytochem 1962;10:335-64.
2. Kisilevsky R. Amyloidogenesis - a critical review. In: Kisilevsky R, Benson MD, Frangione B et al., eds. Amyloid and Amyloidosis. Pathenon Publishing 1994;9-12.
3. Sipe JD. Amyloidosis. Crit Rev in Clin Lab Sci 1994;31:325-54.
4. Glenner GG, Eanes ED, Bladen HA, Terry W, Page DL. Creation of amyloid fibrils from Bence Jones protein in vitro. Science 1971;174:712-14.
5. Klafki H-W, Kratzin, HD, Pick AI, Eckart K, Karas M, Hilschmann N. Complete amino acid sequence determinations demonstrate identity of the urinary Bence Jones protein (BJP-DIA) and the amyloid fibril protein (AL-DIA) in a case of AL-amyloidosis. Biochemistry 1992;31:3265-72.
6. Tan SY, Pepys MB. Amyloidosis. Histopathology 1994;25:403-14.
7. Stevens FJ, Myatt EA, Chang C-H et al. A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains. Biochemistry 1995;34:10697-702.
8. Hurle MR, Helms LR, Li L, Chan W, Wetzel R. A role for destabilizing light chain amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci 1994;91:5446-50.
9. Sletten K, Westermark P, Husby G. Structural studies of the variable region of immunoglobulin light-chain-type amyloid fibril proteins. In: Glenner GG, Osserman EF, Benditt EP, Calkins E, Cohen AS, Zucker-Franklin D, eds. Amyloidosis. New York: Plenum Press, 1986:463-75.
10. Pras M, Schubert M, Zucker-Franklin D, Rimon A, Franklin EC. The characterization of soluble amyloid prepared in water. J Clin Invest 1968;47:924-33.
11. Friedman M, Krull H, Cavins JF. The Chromatographic determination of cystine and cysteine residues in protein as S-β-(4-pyridylethyl)cysteine. J Biol Chem 1970;245:3868-71.
12. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
13. Wilson CM. Studies and critique of amido black 10B, Coomassie blue R and fast green FCF as stains for proteins after polyacrylamide gel-electrophoresis. Anal Biochem 1979;96:263-78.
14. Sletten K, Natvig JB, Husby G, Juul J. The complete amino acid sequence of a prototype immunoglobulin-λ light-chain-type amyloid-fibril protein AR. Biochem J 1981;195:561-72.
15. Austen BM, Smith EL. Action of staphylococcal proteinase on peptides of varying chain length and composition. Biochem Biophys Res Commun 1976;72:411-17.
16. Allen G. Sequencing of protein and peptides (Laboratory techniques, in Biochemistry and Molecular Biology, v 9). Elsevir/North-Holland Biomedical Press, 1981.
17. Podell DN, Abraham GN. A technique for the removal of pyroglutamic acid from the amino terminus of proteins using calf liver pyroglutamate amino peptidase. Biochem Biophys Res Commun 1978;81:176-85.
18. Fontana A. Modification of tryptophan with BNPS-skatole. Methods Enzymol 1972;25:419-23.
19. Yuen SW, Chui AH, Wilson KJ, Yuan PM. Microanalysis of SDS-PAGE electroblotted proteins. Biotechniques 1989;7:74-82.
20. Weitzhandler M, Kadlecek D, Avdalovic N, Forte JG, Chow D, Townsend RR. Monosaccharide and oligosaccharide analysis of proteins transferred to polyvinylidene fluoride membranes after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 1993;268:5121-30.
21. Devereux J, Haeherli P, Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acid Res 1984; 12:387-95.
22. Dwulet FE, O'Connor TP, Benson MD. Polymorphism in a kappa 1 primary (AL) amyloid protein (BAN). Molec Immunol 1986;23: 73-8.
23. Sox HJ Jr, Hood L. Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains. Proc Natl Acad Sci 1970;66:975-82.
24. Rademacher TW, Dwek RA. Structural, functional and conformational analysis of immunoglobulin G-derived asparagine-linked oligosaccharides. Prog Immunol 1983;5:95-112.
25. κIV subgroup in the kidney and plasma cells in light chain deposition disease. J Clin Invest 1991;87:2186-90.
26. Toft KG, Sletten K, Husby G. The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS. Biol Chem Hoppe-Seyler 1985;366:617-25.
27. Kabat EA, Wu TT, Perry HM, Gottesmann KS, Foeller C. In: Sequences of Proteins of Immunological Interest, volume 1, fifth edition, 1991. U.S. Department of Health and Human Services, National Institutes of Health.
28. Furey W, Wang BC, Yoo CS, Sax M. Structure of a novel Bence-Jones protein (Rhe) fragment at 1.6 A resolution. J Mol Biol 1983; 167:661-92.
29. Epp O, Lattman EE, Schiffer M, Huber R, Palm W. The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution. Biochemistry 1975;14:4943-52.