Serologically defined V region subgroups of human lambda light chains.
Open Access
- 1 August 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 139 (3) , 824-830
- https://doi.org/10.4049/jimmunol.139.3.824
Abstract
The availability of numerous antisera prepared against lambda-type Bence Jones proteins and lambda chains of known amino acid sequence has led to the differentiation and classification of human lambda light chains into one of five V lambda subgroups. The five serologically defined subgroups, V lambda I, V lambda II, V lambda III, V lambda IV, and V lambda VI, correspond to the chemical classification that is based on sequence homologies in the first framework region (FR1). Proteins designated by sequence as lambda V react with specific anti-lambda II antisera and are thus included in the V lambda II subgroup classification. The isotypic nature of the five V lambda subgroups was evidenced through analyses of lambda-type light chains that were isolated from the IgG of normal individuals. Based on analyses of 116 Bence Jones proteins, the frequency of distribution of the lambda I, lambda II/V, lambda III, lambda IV, and lambda VI proteins in the normal lambda chain population is estimated to be 27%, 37%, 23%, 3%, and 10%, respectively. This distribution of V lambda subgroups was comparable to that found among 82 monoclonal Ig lambda proteins. Considerable V lambda intragroup antigenic heterogeneity was also apparent. At least two sub-subgroups were identified among each of the five major V lambda subgroups, implying the existence of multiple genes in the human V lambda genome. The V lambda classification of 54 Ig lambda proteins obtained from patients with primary or multiple myeloma-associated amyloidosis substantiated the preferential association of lambda VI light chains with amyloidosis AL and the predominance of the normally rare V lambda VI subgroup in this disease.This publication has 17 references indexed in Scilit:
- Preferential association of kappa IIIb light chains with monoclonal human IgM kappa autoantibodies.The Journal of Immunology, 1983
- Comparative Studies on the Structure of the Light Chains of Human Immunoglobulins. IV. Assignment of a Subsubgroup1The Journal of Biochemistry, 1983
- Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda).Journal of Clinical Investigation, 1982
- Further Structural and Antigenic Studies of Light-chain Amyloid ProteinsScandinavian Journal of Immunology, 1981
- The complete amino acid sequence of a prototype immunoglobulin-λ light-chain-type amyloid-fibril protein ARBiochemical Journal, 1981
- The variable region of human immunoglobulins. I. Serologic and structural correlations of antigenic markers common to V lambda I and V lambda IV proteins (isotypic cross-reactivities).The Journal of Immunology, 1980
- Comparative Study on the Structure of the Light Chains of Human Immunoglobulins1The Journal of Biochemistry, 1979
- Bence jones proteins and light chains of immunoglobulinsImmunogenetics, 1977
- Bence-Jones Proteins and Light Chains of ImmunoglobulinsNew England Journal of Medicine, 1976
- The heat precipitation of Bence-Jones proteins. I. Optimum conditionsArchives of Biochemistry and Biophysics, 1959