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Chemical and serologic characterization of human lambda VIII light chains.
J Immunol. 1994 Aug 15; 153(4):1658-64.JI

Abstract

The primary structural features and serologic properties of a newly recognized human lambda light (L) chain V region subgroup (V lambda VIII) were elucidated through study of two monoclonal L chains, Bence Jones proteins HAG and BIV. The V region amino acid sequences of these components were highly homologous to each other and to that deduced from the prototypic V lambda VIII cDNA, Humla8f10, which encodes the L chains of the IgM lambda rheumatoid factor HAF10. Proteins HAG and BIV could be classified as members of the V lambda VIII subgroup and distinguished from L chains of the V lambda I, V lambda II, V lambda III, V lambda IV, and V lambda VI subgroups on the basis of amino acid sequence. In addition to distinctive residues found within the V lambda gene-encoded portion of the molecules, L chains HAG, BIV, and HAF10 contained remarkably different second complementarity-determining regions (CDR2) that consisted of 11 residues, rather than the seven typically found among members of the other five V lambda subgroups. This elongated structure would presumably impart to the ligand-binding site of lambda VIII molecules a markedly different canonical structure compared with those of lambda I, lambda II, lambda III, lambda IV, and lambda VI L chains. By using Bence Jones protein HAG as an immunogen, we obtained polyclonal and monoclonal anti-V lambda VIII subgroup-specific Abs that were used to identify and quantify lambda VIII-related molecules in normal and pathologic states. Among the Ig lambda components present in the serum of normal individuals, approximately 3% had lambda VIII L chains, a frequency comparable to that found among monoclonal Ig lambda proteins or surface(s) Ig lambda+ cells obtained from patients with malignant plasma cell- or B cell-related disorders, respectively. In contrast, lambda VIII L chains were detected on approximately 19% of monoclonal IgM lambda rheumatoid factors produced by B cell lines established from PBLs or synovial cells from patients with rheumatoid arthritis. The results of our studies provide new information on the structural and immunochemical features of lambda VIII L chains and the possible functional importance of the human V lambda VIII subgroup.

Authors+Show Affiliations

Department of Medicine, University of Tennessee Medical Center/Graduate School of Medicine, Knoxville 37920.No 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
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8046238

Citation

Solomon, A, et al. "Chemical and Serologic Characterization of Human Lambda VIII Light Chains." Journal of Immunology (Baltimore, Md. : 1950), vol. 153, no. 4, 1994, pp. 1658-64.
Solomon A, Weiss DT, Murphy C, et al. Chemical and serologic characterization of human lambda VIII light chains. J Immunol. 1994;153(4):1658-64.
Solomon, A., Weiss, D. T., Murphy, C., Fu, S. M., & Robbins, D. L. (1994). Chemical and serologic characterization of human lambda VIII light chains. Journal of Immunology (Baltimore, Md. : 1950), 153(4), 1658-64.
Solomon A, et al. Chemical and Serologic Characterization of Human Lambda VIII Light Chains. J Immunol. 1994 Aug 15;153(4):1658-64. PubMed PMID: 8046238.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Chemical and serologic characterization of human lambda VIII light chains. AU - Solomon,A, AU - Weiss,D T, AU - Murphy,C, AU - Fu,S M, AU - Robbins,D L, PY - 1994/8/15/pubmed PY - 1994/8/15/medline PY - 1994/8/15/entrez SP - 1658 EP - 64 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J Immunol VL - 153 IS - 4 N2 - The primary structural features and serologic properties of a newly recognized human lambda light (L) chain V region subgroup (V lambda VIII) were elucidated through study of two monoclonal L chains, Bence Jones proteins HAG and BIV. The V region amino acid sequences of these components were highly homologous to each other and to that deduced from the prototypic V lambda VIII cDNA, Humla8f10, which encodes the L chains of the IgM lambda rheumatoid factor HAF10. Proteins HAG and BIV could be classified as members of the V lambda VIII subgroup and distinguished from L chains of the V lambda I, V lambda II, V lambda III, V lambda IV, and V lambda VI subgroups on the basis of amino acid sequence. In addition to distinctive residues found within the V lambda gene-encoded portion of the molecules, L chains HAG, BIV, and HAF10 contained remarkably different second complementarity-determining regions (CDR2) that consisted of 11 residues, rather than the seven typically found among members of the other five V lambda subgroups. This elongated structure would presumably impart to the ligand-binding site of lambda VIII molecules a markedly different canonical structure compared with those of lambda I, lambda II, lambda III, lambda IV, and lambda VI L chains. By using Bence Jones protein HAG as an immunogen, we obtained polyclonal and monoclonal anti-V lambda VIII subgroup-specific Abs that were used to identify and quantify lambda VIII-related molecules in normal and pathologic states. Among the Ig lambda components present in the serum of normal individuals, approximately 3% had lambda VIII L chains, a frequency comparable to that found among monoclonal Ig lambda proteins or surface(s) Ig lambda+ cells obtained from patients with malignant plasma cell- or B cell-related disorders, respectively. In contrast, lambda VIII L chains were detected on approximately 19% of monoclonal IgM lambda rheumatoid factors produced by B cell lines established from PBLs or synovial cells from patients with rheumatoid arthritis. The results of our studies provide new information on the structural and immunochemical features of lambda VIII L chains and the possible functional importance of the human V lambda VIII subgroup. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/8046238/Chemical_and_serologic_characterization_of_human_lambda_VIII_light_chains_ L2 - https://www.jimmunol.org/lookup/pmidlookup?view=long&pmid=8046238 DB - PRIME DP - Unbound Medicine ER -