Novel human light chain V(κ) segment

Serologic and structural analyses of the κIII-like Bence Jones protein and IgGκ light chain REE

F. Prelli, D. Tummolo, Alan Solomon, B. Frangione

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Immunochemical and sequence analysis of κ light chain REE (Bence Jones protein REE and the light chain isolated from IgGκ myeloma protein REE) revealed antigenic and structural features not previously described for human κ-chains. Although closely related to proteins of the V(κIII) subgroup, light chain REE is readily distinguished from light chains classified serologically as members of the κIIIa or κIIIb sub-subgroups. Light chains REE (Bence Jones protein REE and light chain REE) are identical in sequence and differ from κIII proteins by at least 10 uncommon amino acid substitutions in the first three framework regions. Further, κ-chain REE is unique by virtue of a four-residue deletion in the third complementary-determining region. The deletion encompasses the three carboxyl-terminal residues in the V(κ)-encoded segment and the first residue at the site of V-J recombination. Urine specimens from patient REE also contained a light chain fragment that lacked the first (amino-terminal) 85 residues of the native light chain but otherwise was identical in sequence to the light chain REE. The extensive amino acid differences and unique length of the V(κ) segment in light chain REE indicate that this κ-chain is the product of an unusual V(κIII) gene or, alternatively, represents a rarely expressed and novel human V(κ) gene.

Original languageEnglish (US)
Pages (from-to)4169-4173
Number of pages5
JournalJournal of Immunology
Volume136
Issue number11
StatePublished - Jan 1 1986
Externally publishedYes

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Bence Jones Protein
Immunoglobulin G
Light
Myeloma Proteins
Amino Acid Substitution
Genetic Recombination
Genes
Sequence Analysis
Proteins

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Novel human light chain V(κ) segment : Serologic and structural analyses of the κIII-like Bence Jones protein and IgGκ light chain REE. / Prelli, F.; Tummolo, D.; Solomon, Alan; Frangione, B.

In: Journal of Immunology, Vol. 136, No. 11, 01.01.1986, p. 4169-4173.

Research output: Contribution to journalArticle

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abstract = "Immunochemical and sequence analysis of κ light chain REE (Bence Jones protein REE and the light chain isolated from IgGκ myeloma protein REE) revealed antigenic and structural features not previously described for human κ-chains. Although closely related to proteins of the V(κIII) subgroup, light chain REE is readily distinguished from light chains classified serologically as members of the κIIIa or κIIIb sub-subgroups. Light chains REE (Bence Jones protein REE and light chain REE) are identical in sequence and differ from κIII proteins by at least 10 uncommon amino acid substitutions in the first three framework regions. Further, κ-chain REE is unique by virtue of a four-residue deletion in the third complementary-determining region. The deletion encompasses the three carboxyl-terminal residues in the V(κ)-encoded segment and the first residue at the site of V-J recombination. Urine specimens from patient REE also contained a light chain fragment that lacked the first (amino-terminal) 85 residues of the native light chain but otherwise was identical in sequence to the light chain REE. The extensive amino acid differences and unique length of the V(κ) segment in light chain REE indicate that this κ-chain is the product of an unusual V(κIII) gene or, alternatively, represents a rarely expressed and novel human V(κ) gene.",
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T2 - Serologic and structural analyses of the κIII-like Bence Jones protein and IgGκ light chain REE

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AU - Tummolo, D.

AU - Solomon, Alan

AU - Frangione, B.

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N2 - Immunochemical and sequence analysis of κ light chain REE (Bence Jones protein REE and the light chain isolated from IgGκ myeloma protein REE) revealed antigenic and structural features not previously described for human κ-chains. Although closely related to proteins of the V(κIII) subgroup, light chain REE is readily distinguished from light chains classified serologically as members of the κIIIa or κIIIb sub-subgroups. Light chains REE (Bence Jones protein REE and light chain REE) are identical in sequence and differ from κIII proteins by at least 10 uncommon amino acid substitutions in the first three framework regions. Further, κ-chain REE is unique by virtue of a four-residue deletion in the third complementary-determining region. The deletion encompasses the three carboxyl-terminal residues in the V(κ)-encoded segment and the first residue at the site of V-J recombination. Urine specimens from patient REE also contained a light chain fragment that lacked the first (amino-terminal) 85 residues of the native light chain but otherwise was identical in sequence to the light chain REE. The extensive amino acid differences and unique length of the V(κ) segment in light chain REE indicate that this κ-chain is the product of an unusual V(κIII) gene or, alternatively, represents a rarely expressed and novel human V(κ) gene.

AB - Immunochemical and sequence analysis of κ light chain REE (Bence Jones protein REE and the light chain isolated from IgGκ myeloma protein REE) revealed antigenic and structural features not previously described for human κ-chains. Although closely related to proteins of the V(κIII) subgroup, light chain REE is readily distinguished from light chains classified serologically as members of the κIIIa or κIIIb sub-subgroups. Light chains REE (Bence Jones protein REE and light chain REE) are identical in sequence and differ from κIII proteins by at least 10 uncommon amino acid substitutions in the first three framework regions. Further, κ-chain REE is unique by virtue of a four-residue deletion in the third complementary-determining region. The deletion encompasses the three carboxyl-terminal residues in the V(κ)-encoded segment and the first residue at the site of V-J recombination. Urine specimens from patient REE also contained a light chain fragment that lacked the first (amino-terminal) 85 residues of the native light chain but otherwise was identical in sequence to the light chain REE. The extensive amino acid differences and unique length of the V(κ) segment in light chain REE indicate that this κ-chain is the product of an unusual V(κIII) gene or, alternatively, represents a rarely expressed and novel human V(κ) gene.

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