Skip to main content
NCBI home page
The American Journal of Pathology logoLink to The American Journal of Pathology
. 1996 May;148(5):1339–1344.

Molecular anatomy and the pathological expression of antibody light chains.

M Schiffer 1
PMCID: PMC1861552  PMID: 8623904

Full text

PDF
1339

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alber T. Mutational effects on protein stability. Annu Rev Biochem. 1989;58:765–798. doi: 10.1146/annurev.bi.58.070189.004001. [DOI] [PubMed] [Google Scholar]
  2. Bowler B. E., May K., Zaragoza T., York P., Dong A., Caughey W. S. Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: implications for the denatured state. Biochemistry. 1993 Jan 12;32(1):183–190. doi: 10.1021/bi00052a024. [DOI] [PubMed] [Google Scholar]
  3. Buxbaum J. N., Chuba J. V., Hellman G. C., Solomon A., Gallo G. R. Monoclonal immunoglobulin deposition disease: light chain and light and heavy chain deposition diseases and their relation to light chain amyloidosis. Clinical features, immunopathology, and molecular analysis. Ann Intern Med. 1990 Mar 15;112(6):455–464. doi: 10.7326/0003-4819-76-3-112-6-455. [DOI] [PubMed] [Google Scholar]
  4. Ch'ang L. Y., Yen C. P., Besl L., Schell M., Solomon A. Identification and characterization of a functional human Ig V lambda VI germline gene. Mol Immunol. 1994 May;31(7):531–536. doi: 10.1016/0161-5890(94)90040-x. [DOI] [PubMed] [Google Scholar]
  5. Cogné M., Preud'homme J. L., Bauwens M., Touchard G., Aucouturier P. Structure of a monoclonal kappa chain of the V kappa IV subgroup in the kidney and plasma cells in light chain deposition disease. J Clin Invest. 1991 Jun;87(6):2186–2190. doi: 10.1172/JCI115252. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cogné M., Silvain C., Khamlichi A. A., Preud'homme J. L. Structurally abnormal immunoglobulins in human immunoproliferative disorders. Blood. 1992 May 1;79(9):2181–2195. [PubMed] [Google Scholar]
  7. Epp O., Lattman E. E., 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-A resolution. Biochemistry. 1975 Nov 4;14(22):4943–4952. doi: 10.1021/bi00693a025. [DOI] [PubMed] [Google Scholar]
  8. Frippiat J. P., Williams S. C., Tomlinson I. M., Cook G. P., Cherif D., Le Paslier D., Collins J. E., Dunham I., Winter G., Lefranc M. P. Organization of the human immunoglobulin lambda light-chain locus on chromosome 22q11.2. Hum Mol Genet. 1995 Jun;4(6):983–991. doi: 10.1093/hmg/4.6.983. [DOI] [PubMed] [Google Scholar]
  9. Furey W., Jr, Wang B. C., Yoo C. S., Sax M. Structure of a novel Bence-Jones protein (Rhe) fragment at 1.6 A resolution. J Mol Biol. 1983 Jul 5;167(3):661–692. doi: 10.1016/s0022-2836(83)80104-1. [DOI] [PubMed] [Google Scholar]
  10. Gallo G., Goñi F., Boctor F., Vidal R., Kumar A., Stevens F. J., Frangione B., Ghiso J. Light chain cardiomyopathy. Structural analysis of the light chain tissue deposits. Am J Pathol. 1996 May;148(5):1397–1406. [PMC free article] [PubMed] [Google Scholar]
  11. Gallo G., Picken M., Buxbaum J., Frangione B. The spectrum of monoclonal immunoglobulin deposition disease associated with immunocytic dyscrasias. Semin Hematol. 1989 Jul;26(3):234–245. [PubMed] [Google Scholar]
  12. Huang D. B., Chang C. H., Ainsworth C., Brünger A. T., Eulitz M., Solomon A., Stevens F. J., Schiffer M. Comparison of crystal structures of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers. Biochemistry. 1994 Dec 13;33(49):14848–14857. doi: 10.1021/bi00253a024. [DOI] [PubMed] [Google Scholar]
  13. Hurle M. R., Helms L. R., Li L., Chan W., Wetzel R. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5446–5450. doi: 10.1073/pnas.91.12.5446. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Khamlichi A. A., Aucouturier P., Silvain C., Bauwens M., Touchard G., Preud'homme J. L., Nau F., Cogné M. Primary structure of a monoclonal kappa chain in myeloma with light chain deposition disease. Clin Exp Immunol. 1992 Jan;87(1):122–126. doi: 10.1111/j.1365-2249.1992.tb06424.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Klein R., Jaenichen R., Zachau H. G. Expressed human immunoglobulin kappa genes and their hypermutation. Eur J Immunol. 1993 Dec;23(12):3248–3262. doi: 10.1002/eji.1830231231. [DOI] [PubMed] [Google Scholar]
  16. Kyle R. A. The monoclonal gammopathies. Clin Chem. 1994 Nov;40(11 Pt 2):2154–2161. [PubMed] [Google Scholar]
  17. Myatt E. A., Westholm F. A., Weiss D. T., Solomon A., Schiffer M., Stevens F. J. Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3034–3038. doi: 10.1073/pnas.91.8.3034. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rocca A., Khamlichi A. A., Aucouturier P., Noël L. H., Denoroy L., Preud'homme J. L., Cogné M. Primary structure of a variable region of the V kappa I subgroup (ISE) in light chain deposition disease. Clin Exp Immunol. 1993 Mar;91(3):506–509. doi: 10.1111/j.1365-2249.1993.tb05932.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Solomon A., Weiss D. T., Kattine A. A. Nephrotoxic potential of Bence Jones proteins. N Engl J Med. 1991 Jun 27;324(26):1845–1851. doi: 10.1056/NEJM199106273242603. [DOI] [PubMed] [Google Scholar]
  20. Solomon A., Weiss D. T., Pepys M. B. Induction in mice of human light-chain-associated amyloidosis. Am J Pathol. 1992 Mar;140(3):629–637. [PMC free article] [PubMed] [Google Scholar]
  21. Steipe B., Schiller B., Plückthun A., Steinbacher S. Sequence statistics reliably predict stabilizing mutations in a protein domain. J Mol Biol. 1994 Jul 15;240(3):188–192. doi: 10.1006/jmbi.1994.1434. [DOI] [PubMed] [Google Scholar]
  22. Stevens F. J., Myatt E. A., Chang C. H., Westholm F. A., Eulitz M., Weiss D. T., Murphy C., Solomon A., Schiffer M. A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains. Biochemistry. 1995 Aug 29;34(34):10697–10702. doi: 10.1021/bi00034a001. [DOI] [PubMed] [Google Scholar]
  23. Stevens F. J., Schiffer M. Structure and properties of human immunoglobulin light-chain dimers. Methods Mol Biol. 1995;51:51–81. doi: 10.1385/0-89603-275-2:51. [DOI] [PubMed] [Google Scholar]
  24. Stevens P. W., Raffen R., Hanson D. K., Deng Y. L., Berrios-Hammond M., Westholm F. A., Murphy C., Eulitz M., Wetzel R., Solomon A. Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins. Protein Sci. 1995 Mar;4(3):421–432. doi: 10.1002/pro.5560040309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Tomlinson I. M., Cox J. P., Gherardi E., Lesk A. M., Chothia C. The structural repertoire of the human V kappa domain. EMBO J. 1995 Sep 15;14(18):4628–4638. doi: 10.1002/j.1460-2075.1995.tb00142.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wu T. T., Kabat E. A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J Exp Med. 1970 Aug 1;132(2):211–250. doi: 10.1084/jem.132.2.211. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The American Journal of Pathology are provided here courtesy of American Society for Investigative Pathology

RESOURCES