Bence jones proteins and light chains of immunoglobulins-XXVII. Unique susceptibility of certain κ-chains to proteolysis by human granulocyte-derived neutral proteases

Alan Solomon, Klaus Havemann

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4 Citations (Scopus)

Abstract

Light chains of human immunoglobulins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino-terminal, variant (VL) portion, and to the carboxyl-terminal, constant (CL) portion. We have investigated the effect of two human polymorphonuclear leucocyte-derived neutral proteases, the elastase-like protease (ELP) and the chymotrypsin-like protease (CLP), on Bence Jones proteins representative of the four structurally and immunochemically-defined groups of human kappa light chains. When κI, κII, κIII and κIV proteins were incubated with ELP or CLP, the result was an extensive proteolysis of the CL portion of these molecules and the generation of VL-related fragments. However, the VL portions of certain κ-chains classified immunologically as a subgroup of κI-chains, κI-1, were also extraordinarily susceptible to proteolysis by these granulocyte-derived neutral proteases. These findings have provided new evidence relating specific structural and antigenic features of human kappa light polypeptide chains.

Original languageEnglish (US)
Pages (from-to)453-458
Number of pages6
JournalMolecular Immunology
Volume15
Issue number7
DOIs
StatePublished - Jan 1 1978

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Bence Jones Protein
Immunoglobulin Light Chains
Granulocytes
Proteolysis
Peptide Hydrolases
Chymases
Pancreatic Elastase
Light
Endopeptidases
Neutrophils
Peptides
Proteins

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology

Cite this

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title = "Bence jones proteins and light chains of immunoglobulins-XXVII. Unique susceptibility of certain κ-chains to proteolysis by human granulocyte-derived neutral proteases",
abstract = "Light chains of human immunoglobulins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino-terminal, variant (VL) portion, and to the carboxyl-terminal, constant (CL) portion. We have investigated the effect of two human polymorphonuclear leucocyte-derived neutral proteases, the elastase-like protease (ELP) and the chymotrypsin-like protease (CLP), on Bence Jones proteins representative of the four structurally and immunochemically-defined groups of human kappa light chains. When κI, κII, κIII and κIV proteins were incubated with ELP or CLP, the result was an extensive proteolysis of the CL portion of these molecules and the generation of VL-related fragments. However, the VL portions of certain κ-chains classified immunologically as a subgroup of κI-chains, κI-1, were also extraordinarily susceptible to proteolysis by these granulocyte-derived neutral proteases. These findings have provided new evidence relating specific structural and antigenic features of human kappa light polypeptide chains.",
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T1 - Bence jones proteins and light chains of immunoglobulins-XXVII. Unique susceptibility of certain κ-chains to proteolysis by human granulocyte-derived neutral proteases

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AU - Havemann, Klaus

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N2 - Light chains of human immunoglobulins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino-terminal, variant (VL) portion, and to the carboxyl-terminal, constant (CL) portion. We have investigated the effect of two human polymorphonuclear leucocyte-derived neutral proteases, the elastase-like protease (ELP) and the chymotrypsin-like protease (CLP), on Bence Jones proteins representative of the four structurally and immunochemically-defined groups of human kappa light chains. When κI, κII, κIII and κIV proteins were incubated with ELP or CLP, the result was an extensive proteolysis of the CL portion of these molecules and the generation of VL-related fragments. However, the VL portions of certain κ-chains classified immunologically as a subgroup of κI-chains, κI-1, were also extraordinarily susceptible to proteolysis by these granulocyte-derived neutral proteases. These findings have provided new evidence relating specific structural and antigenic features of human kappa light polypeptide chains.

AB - Light chains of human immunoglobulins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino-terminal, variant (VL) portion, and to the carboxyl-terminal, constant (CL) portion. We have investigated the effect of two human polymorphonuclear leucocyte-derived neutral proteases, the elastase-like protease (ELP) and the chymotrypsin-like protease (CLP), on Bence Jones proteins representative of the four structurally and immunochemically-defined groups of human kappa light chains. When κI, κII, κIII and κIV proteins were incubated with ELP or CLP, the result was an extensive proteolysis of the CL portion of these molecules and the generation of VL-related fragments. However, the VL portions of certain κ-chains classified immunologically as a subgroup of κI-chains, κI-1, were also extraordinarily susceptible to proteolysis by these granulocyte-derived neutral proteases. These findings have provided new evidence relating specific structural and antigenic features of human kappa light polypeptide chains.

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