Tags

Type your tag names separated by a space and hit enter

The V kappa III subgroup light chain proteins in AL amyloidosis & autoimmune diseases.
Indian J Med Res. 2001 Jul; 114:30-5.IJ

Abstract

BACKGROUND & OBJECTIVES

Light chain associated amyloidosis (AL) is characterized by extracellular deposition of immunoglobulin light chain and its fragments. In vitro and in vivo studies have shown that some light chains are nonamyloidogenic and nonnephrotoxic, whereas others are potentially amyloidogenic. Some light chains are prone to be deposited as rheumatoid materials, and also as nodular amorphous aggregates (light chain deposition diseases). These findings suggest that specific sequence element(s) may control the various kinds of light chain associated diseases. In this study we tried to identify such sequence element(s).

METHODS

Two Bence Jones proteins (BJPs), NIG93 and NIG2 of subgroup V kappa III, were characterized and compared with other members of the same subgroup whose sequences are available in the data base.

RESULTS

Both NIG93 and NIG2 proteins had sequences characteristics of V kappa IIIa as distinguished from V kappa IIIb, subsubgroup proteins. They also contained several novel substitutions, such as Met-37, Leu-40, Val-58, and IIe-85 in NIG93, and Val-2, His-29, Arg-50, and Ile-72 in NIG2. The data accumulated at present indicate that all members of the V kappa IIIa subsubgroup are related to either AL amyloidosis or rheumatoid arthritis, whereas the V kappa IIIb proteins are related to autoimmune diseases.

INTERPRETATION & CONCLUSION

These observations indicate that subgroup-specific residues might be critical for light chain pathogenesis, at least for the V kappa III proteins. Point mutations within these proteins may be another structural element controlling their conformation as well as their pathogenic aggregation.

Authors+Show Affiliations

Laboratory of Biochemistry, Graduate School of Science, Tokyo Metropolitan University, Tokyo, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11762204

Citation

Alim, M A., et al. "The V Kappa III Subgroup Light Chain Proteins in AL Amyloidosis & Autoimmune Diseases." The Indian Journal of Medical Research, vol. 114, 2001, pp. 30-5.
Alim MA, Hara Y, Kaji H, et al. The V kappa III subgroup light chain proteins in AL amyloidosis & autoimmune diseases. Indian J Med Res. 2001;114:30-5.
Alim, M. A., Hara, Y., Kaji, H., & Shinoda, T. (2001). The V kappa III subgroup light chain proteins in AL amyloidosis & autoimmune diseases. The Indian Journal of Medical Research, 114, 30-5.
Alim MA, et al. The V Kappa III Subgroup Light Chain Proteins in AL Amyloidosis & Autoimmune Diseases. Indian J Med Res. 2001;114:30-5. PubMed PMID: 11762204.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The V kappa III subgroup light chain proteins in AL amyloidosis & autoimmune diseases. AU - Alim,M A, AU - Hara,Y, AU - Kaji,H, AU - Shinoda,T, PY - 2002/1/5/pubmed PY - 2002/2/20/medline PY - 2002/1/5/entrez SP - 30 EP - 5 JF - The Indian journal of medical research JO - Indian J Med Res VL - 114 N2 - BACKGROUND & OBJECTIVES: Light chain associated amyloidosis (AL) is characterized by extracellular deposition of immunoglobulin light chain and its fragments. In vitro and in vivo studies have shown that some light chains are nonamyloidogenic and nonnephrotoxic, whereas others are potentially amyloidogenic. Some light chains are prone to be deposited as rheumatoid materials, and also as nodular amorphous aggregates (light chain deposition diseases). These findings suggest that specific sequence element(s) may control the various kinds of light chain associated diseases. In this study we tried to identify such sequence element(s). METHODS: Two Bence Jones proteins (BJPs), NIG93 and NIG2 of subgroup V kappa III, were characterized and compared with other members of the same subgroup whose sequences are available in the data base. RESULTS: Both NIG93 and NIG2 proteins had sequences characteristics of V kappa IIIa as distinguished from V kappa IIIb, subsubgroup proteins. They also contained several novel substitutions, such as Met-37, Leu-40, Val-58, and IIe-85 in NIG93, and Val-2, His-29, Arg-50, and Ile-72 in NIG2. The data accumulated at present indicate that all members of the V kappa IIIa subsubgroup are related to either AL amyloidosis or rheumatoid arthritis, whereas the V kappa IIIb proteins are related to autoimmune diseases. INTERPRETATION & CONCLUSION: These observations indicate that subgroup-specific residues might be critical for light chain pathogenesis, at least for the V kappa III proteins. Point mutations within these proteins may be another structural element controlling their conformation as well as their pathogenic aggregation. SN - 0971-5916 UR - https://www.unboundmedicine.com/medline/citation/11762204/The_V_kappa_III_subgroup_light_chain_proteins_in_AL_amyloidosis_&_autoimmune_diseases_ L2 - http://www.diseaseinfosearch.org/result/675 DB - PRIME DP - Unbound Medicine ER -