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Structural relationship of lambda-type light chains with AL amyloidosis.
Clin Immunol. 1999 Mar; 90(3):399-403.CI

Abstract

Three human amyloidogenic Bence Jones proteins, NIG76 VlambdaII, NIG204 VlambdaI, and NIG250 VlambdaV, were characterized. In a comparative study, three amino acids, Ser-25a, Thr-68, and Val-95, were found to be common to amyloidogenic proteins of the VlambdaII subgroup. NIG204 had an insertion of Pro residue following position 30 (30a). Proteins having an insertion at this position are invariantly amyloidogenic. NIG250 had a characteristic VlambdaV VL domain, with Mcg+ and KERN+ CL domain isotypes. Following the protein DEL, this is the second example of this subgroup. No common residue is found in the other subgroup proteins but unique substitutions do occur. It would seem that any substitution that causes an alteration in the protein conformation may lead to its being more prone to association with the amyloid processes.

Authors+Show Affiliations

Graduate School of Science, Tokyo Metropolitan University, Minamiohsawa, Hachioji, 192-0397, Japan. alim@comp.metro-u.ac.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

10075869

Citation

Alim, M A., et al. "Structural Relationship of Lambda-type Light Chains With AL Amyloidosis." Clinical Immunology (Orlando, Fla.), vol. 90, no. 3, 1999, pp. 399-403.
Alim MA, Yamaki S, Hossain MS, et al. Structural relationship of lambda-type light chains with AL amyloidosis. Clin Immunol. 1999;90(3):399-403.
Alim, M. A., Yamaki, S., Hossain, M. S., Takeda, K., Yamagata, F., Takashi, I., & Shinoda, T. (1999). Structural relationship of lambda-type light chains with AL amyloidosis. Clinical Immunology (Orlando, Fla.), 90(3), 399-403.
Alim MA, et al. Structural Relationship of Lambda-type Light Chains With AL Amyloidosis. Clin Immunol. 1999;90(3):399-403. PubMed PMID: 10075869.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural relationship of lambda-type light chains with AL amyloidosis. AU - Alim,M A, AU - Yamaki,S, AU - Hossain,M S, AU - Takeda,K, AU - Yamagata,F, AU - Takashi,I, AU - Shinoda,T, PY - 1999/3/17/pubmed PY - 1999/3/17/medline PY - 1999/3/17/entrez SP - 399 EP - 403 JF - Clinical immunology (Orlando, Fla.) JO - Clin Immunol VL - 90 IS - 3 N2 - Three human amyloidogenic Bence Jones proteins, NIG76 VlambdaII, NIG204 VlambdaI, and NIG250 VlambdaV, were characterized. In a comparative study, three amino acids, Ser-25a, Thr-68, and Val-95, were found to be common to amyloidogenic proteins of the VlambdaII subgroup. NIG204 had an insertion of Pro residue following position 30 (30a). Proteins having an insertion at this position are invariantly amyloidogenic. NIG250 had a characteristic VlambdaV VL domain, with Mcg+ and KERN+ CL domain isotypes. Following the protein DEL, this is the second example of this subgroup. No common residue is found in the other subgroup proteins but unique substitutions do occur. It would seem that any substitution that causes an alteration in the protein conformation may lead to its being more prone to association with the amyloid processes. SN - 1521-6616 UR - https://www.unboundmedicine.com/medline/citation/10075869/Structural_relationship_of_lambda_type_light_chains_with_AL_amyloidosis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1521-6616(98)94662-9 DB - PRIME DP - Unbound Medicine ER -