Multiple-myeloma proteins.III. The antigenic relationship of Bence Jones proteins to normal gamma-globulin and multiple-myeloma serum proteins

Korngold, Leonhard; Lipari, Rose

doi:10.1002/1097-0142(195603/04)9:2<262::aid-cncr2820090210>3.0.co;2-b

Cited by 150 publications

(56 citation statements)

References 18 publications

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“…Identifications of two antigenically distinct types of Bence Jones protein also agree with those of Korngold and Lipari (22), whose type B is equivalent to our type I and whose type A is the same as our type II. The present studies and the recent studies of Mannik and Kunkel (37), however, extend the earlier work of Korngold and Lipari (22) and Franklin (24) to show that both groups of distinctive antigenic determinants are represented in all classes of anomalous proteins.…”

Section: Discussionsupporting

confidence: 89%

“…Such proteins are now identified as Bence Jones proteins, y-myeloma proteins, fl2A-myeloma proteins, or yi-macroglobulins on the basis of specific immunochemical and physicochemical properties (15)(16)(17)(18). Systematic differences of another type, however, may also occur within these four major groups.. Two antigenically different groups of Bence Jones proteins have been identified in several laboratories (19)(20)(21)(22)(23). Two types of y-myeloma proteins were identified by Korngold and Lipari (7), and Franklin (24) found two types of 82A-myeloma proteins.…”

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confidence: 99%

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TWO TYPES OF Γ-Myeloma PROTEINS, Β2A-Myeloma PROTEINS, Γ1-Macroglobulins, AND BENCE JONES PROTEINS IDENTIFIED BY TWO GROUPS OF COMMON ANTIGENIC DETERMINANTS

Fahey

Solomon²

1963

J. Clin. Invest.

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The serum myeloma proteins are characteristic products of malignant plasma cells, and individual myeloma proteins provide an important source of information on the protein-producing capacities (and limitations) of plasma cell clones. The globulins produced by malignant plasma cells are closely related to the normal v-globulins, but immunochemical studies of the antigenic determinants present on myeloma proteins have uniformly shown that myeloma proteins are antigenically deficient when compared to normal y-globulins (1)(2)(3)(4)(5)(6)(7)(8). Similar studies (9-13) have shown that macroglobulinemic macroglobulins are antigenically deficient when compared to the normal 71-macroglobulins. Antigen deletion has been demonstrated to occur with malignant transformation (14), and antigenic deficiency of myeloma proteins could be viewed as reflecting a plasma cell change associated with malignancy. Alternatively, myeloma protein differences may simply reflect differences between normal y-globulin molecules (and between normal plasma cells). Immunochemical studies have not settled this question, although marked variability in the antigenic determinants on individual myeloma proteins has been noted. A number of studies, however, have emphasized systematic differences among the proteins formed in malignant plasma cells. Such proteins are now identified as Bence Jones proteins, y-myeloma proteins, fl2A-myeloma proteins, or yi-macroglobulins on the basis of specific immunochemical and physicochemical properties (15-18). Systematic differences of another type, however, may also occur within these four major groups.. Two antigenically different groups of Bence Jones proteins have been identified in several laboratories (19)(20)(21)(22)(23). Two types of y-myeloma proteins were identified by Korngold and Lipari (7), and Franklin (24) found two types of 82A-myeloma proteins. The molecular differences within major y-globulin groups has received less attention than the y-, 82A-, yLm-, and BJgrouping, and the presence of two general subdivisions has not been established as a consistent feature of all of the anomalous y-globulin groups.In the course of immunochemical studies of y-globulins, differences were observed in the antigenic composition of S pieces obtained by papain digestion of individual myeloma proteins (25,26).In view of previous observations (16,27,28) that the antigenic determinants common to all y-globulin groups were present in the S pieces from y-globulin molecules and that Bence Jones proteins were antigenically related to the S pieces, studies were undertaken to determine whether all four classes of proteins formed in malignant plasma cells could be divided into two groups on the basis of readily identifiable antigenic differences.Two forms of molecules (types I and II) differing in antigenic composition were identified in each anomalous protein group (29). Further studies demonstrated that two sets of antigenic determinants (types I and II) were common to all the y-globulin groups, but that the relative frequency...

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Section: Discussionsupporting

confidence: 89%

mentioning

confidence: 99%

TWO TYPES OF Γ-Myeloma PROTEINS, Β2A-Myeloma PROTEINS, Γ1-Macroglobulins, AND BENCE JONES PROTEINS IDENTIFIED BY TWO GROUPS OF COMMON ANTIGENIC DETERMINANTS

Fahey

Solomon²

1963

J. Clin. Invest.

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“…It is clear from the present experiments thatL chains of normal -y-globulin, which have been shown to behave physically like Bence-Jones proteins, are more closely related antigenically to Bence-Jones proteins and L chains of myeloma proteins than to whole myeloma proteins. Although the present experiments showed reactions of identity between the L chains of the -r-myeloma protein and the L chains of normal -y-globulin, it would not he surprising if more extensive studies revealed that L chains of various myeloma proteins were antigenically deficient to those of normal -y-globulin (21).…”

Section: Discussioncontrasting

confidence: 57%

The ANTIGENIC STRUCTURE OF THE POLYPEPTIDE CHAINS OF HUMAN Γ-Globulin

Olins

Edelman

1962

The Journal of Experimental Medicine

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One of the goals of chemical and immunological studies of T-globulins is to relate the biological activities of the whole molecules to structural features of their constituent polypeptide chains. 7S ~'-globulin molecules consist of multiple polypeptide chains linked by disulfide bonds and non-covalent interactions (1). Two types of chains have been described (2, 3): light (L) chains, having molecular weights of approximately 20,000; and heavy (H) chains, having molecular weights greater than 50,000. Certain physicochemical characterisitics of L chains have been associated with differences in the specificity of antibodies (4), with the individuality of myeloma proteins (5), and with the unique thermosolubility properties of Bence-Jones proteins (3). The current evidence and hypotheses relating the properties of normal and pathological "y-globulins to properties of their L and H chains have been reviewed (6).The present study is concerned with an analysis of the antigenic characteristics of the polypeptide chains of normal human 7S %globulin and of a human myeloma protein. The antigenic determinants of L and H chains have been correlated with the previously described S and F determinants (7), which comprise two major non-cross-reacting antigenic groups of the whole "},-globulin molecule. Antigenic identity has been found between the L chains of a myeloma protein and the Bence-Jones protein from the same patient, thus providing further evidence of their structural similarity, and corroborating the results of previous chemical studies (3).These results furnish a basis for relating the polypeptide chains of qt-globulin molecules to the fragments produced by hydrolysis with papain. Methods and Materials'y-Globul~ns.--Lyophillzed human 7S T-globulln was obtained as fraction II of Cohn (Lot C-679) from Lederle Laboratories (Pearl River, New York). A portion was further purified by zone electrophoresis on starch (8). The preparation of a "y-myeloma protein (patient Haw) and Bence-Jones protein from the same patient has been described previously (3). Protein concentrations were determined by measurement of the optical density of solutions at 280 m# and by a modification of the Folin-Ciocalteu method (9).

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“…Recently it has been shown (13,14) that differences in antigenic specificity o[ Bence Jones proteins can be correlated with the presence or absence of terminal Br-asparfic acid. The finding of Deutsch and Morton (1) that rnercaptoethanol de-polymerizes 71-macroglobulins opened another line of approach, since the action of this chemical is directed against the disulfide bond of the protein.…”

Section: Discussionmentioning

confidence: 99%

Macroglobulinemia

Korngold

Leeuwen

1959

The Journal of Experimental Medicine

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The monomers obtained by treating γ1-macroglobulins with mercaptoethanol have proved to be antigenically different from normal 7S 7γ-globulin. The depolymerization of the macroglobulins resulted in the loss of several antigenic determinants, although the monomers still cross-reacted with antisera against macroglobulins. Reaggregation of the monomers occasionally resulted in the reconstitution of some or all of the antigenic determinants that were lost during depolymerization. Repeated freezing and thawing of pathological macroglobulins in iodoacetate resulted in their complete antigenic destruction. Repeated freezing and thawing of one of the monomers in excess iodoacetate resulted in the degradation to a protein antigenically indistinguishable from Bence Jones protein. The other two monomers studied were stable under these conditions.

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Multiple-myeloma proteins.III. The antigenic relationship of Bence Jones proteins to normal gamma-globulin and multiple-myeloma serum proteins

Cited by 150 publications

References 18 publications

TWO TYPES OF Γ-Myeloma PROTEINS, Β2A-Myeloma PROTEINS, Γ1-Macroglobulins, AND BENCE JONES PROTEINS IDENTIFIED BY TWO GROUPS OF COMMON ANTIGENIC DETERMINANTS

TWO TYPES OF Γ-Myeloma PROTEINS, Β2A-Myeloma PROTEINS, Γ1-Macroglobulins, AND BENCE JONES PROTEINS IDENTIFIED BY TWO GROUPS OF COMMON ANTIGENIC DETERMINANTS

The ANTIGENIC STRUCTURE OF THE POLYPEPTIDE CHAINS OF HUMAN Γ-Globulin

Macroglobulinemia

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