7 S Globulin, Immunologically Identical to 19 S Gamma-1 (beta-2)-M-globulin, a New Protein of Horse Serum

Sandor, G; S, Korach; Mattern, P. J.

doi:10.1038/204795a0

Cited by 26 publications

(4 citation statements)

References 2 publications

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“…Lower vertebrates such as the smooth dogfish (1) and lemon shark (2) appear to possess a single immunoglobulin system with both high and low molecular weight components showing closest similarity to the human 1gM system. Studies of horse serum have also suggested the existence of a low molecular weight y-globulin antigenically related to the horse 19 S IgM (3). The occurrence of a similar system in humans was suggested by the findings of Killander (4) and especially those of Rothfield, Frangione, and Franklin (5).…”

Section: Introductionmentioning

confidence: 68%

A Low Molecular Weight Immunoglobulin Antigenically Related to 19 S IgM*

Stobo¹,

Tomasi²

1967

J. Clin. Invest.

139

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Section: Introductionmentioning

confidence: 68%

A Low Molecular Weight Immunoglobulin Antigenically Related to 19 S IgM*

Stobo¹,

Tomasi²

1967

J. Clin. Invest.

139

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“…Although this is the first reported finding of monolneric IgM on the surface of normal lymphocytes, such monomers have been described as the major class of immunoglobulin in the sera of some lower vertebrates (42)(43)(44)(45)(46)(47)(48) and occasionally in trace amounts in normal mammalian sera (49)(50)(51) or in association with immunological deficiencies (52)(53)(54)(55)(56), myeloma (57), connective tissue diseases (58), and parasitic or other infections (59,60). IgM monomers have also been described intracellularly in a mouse myeloma tumor that secretes polymeric IgM (61).…”

Section: Discussionmentioning

confidence: 99%

Cell Surface Immunoglobulin

Vitetta

Baur

Uhr

1971

The Journal of Experimental Medicine

353

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There is accumulating evidence that the capacity of lymphocytes to bind antigen specifically (1-6) is due to Ig on the cell surface: anti-Ig causes the transformation of lymphocytes (7-12) and other changes in membrane properties (13,14); anti-L chain and anti-Ig inhibit both binding of specific antigen and stimulation of cellmediated immune reactions by antigen (15-18); anti-Ig of allotype or class specificity binds to lymphocytes (19-23); "rosette" formation around lymphocytes occurs when hybrid antibody to both Ig and specific antigen is added along with red cells coated with antigen (24, 25); lymphocytes treated with anti-Ig form rosettes with Ig-coated red cells (26,27); and specific adherence of lymphocytes to antigen-coated columns is blocked by pretreatment of cells with anti-Ig serum (28). There is conflicting evidence, however, as to whether the major class of cell surface immunoglobulin on normal splenic lymphocytes is IgM (12,20) or IgG (7, 21), as well as the distribution of Ig on cells (20,21).In evaluating the above results, I t should be emphasized that the methodologies used rely on the capacity of anti-Ig antibody to make effective contact with antigenic determinants of the receptor. Such contact depends upon the presence of determinants on portions of the receptor available to anti-Ig antibody in the medium and retention of antigenicity when the receptor is bound to the plasma membrane. These problems may account for the several contradictory reports mentioned above and the finding that individual antisera directed against the same immunoglobulin can give conflicting results, presumably depending on differences in the specificities of the antisera (20,29).For these reasons we developed an approach in which surface Ig could be studied by standard immuno-and biochemical techniques after its removal from the celt surface (30).

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“…In these animals the low molecular weight immunoglobulin is quantitatively predominant, the 7S IgM/19S IgM ratio ranging between 1.6 and 2 [15].Recent studies have also demonstrated the existence of small amounts of 7S proteins with IgM antigenic determinants in the horse serum [18], as well as in the sera of normal human beings [11] and of patients with different diseases [2,5,8,17,22].Increasing attention is being paid to this peculiar low molecular weight IgM in view of recently acquired evidence, which seems to suggest that it may represent still another class of human immuno globulins. The present report describes the occurrence of 7S IgM in some sera from patients with several disease states associated with abnormalities of serum immunoglobulins.…”

mentioning

confidence: 97%