Effect fixation on T and B lymphocyte surface membrane antigen demonstration in paraffin processed tissue

1986 ◽  
Vol 149 (4) ◽  
pp. 293-300 ◽  
Author(s):  
Clive S. Holgate ◽  
Peter Jackson ◽  
Kenneth Pollard ◽  
Declan Lunny ◽  
Colin C. Bird
Keyword(s):  
B Lymphocyte ◽  
Surface Membrane ◽  
Lymphocyte Surface

Antibody-mediated internalization of B lymphocyte surface membrane immunoglobulin

1973 ◽  
Vol 81 (2) ◽  
pp. 317-329 ◽  
Author(s):  
A.S. Rosenthal ◽  
J.M. Davie ◽  
D.L. Rosenstreich ◽  
Kerstin U. Cehrs
Keyword(s):  
B Lymphocyte ◽  
Surface Membrane ◽  
Lymphocyte Surface ◽  
Membrane Immunoglobulin

scholarly journals Interactions between lymphocyte membrane molecules. I. Interaction between B lymphocyte surface IgM and Fc IgG receptors requires ligand occupancy of both receptors.

1981 ◽  
Vol 153 (5) ◽  
pp. 1329-1343 ◽  
Author(s):  
H B Dickler ◽  
M T Kubicek
Keyword(s):  
B Lymphocyte ◽  
Surface Membrane ◽  
Specific Interaction ◽  
Normal Serum ◽  
Membrane Receptors ◽  
Soluble Antigen ◽  
Lymphocyte Surface ◽  
Igg Receptors ◽  
Antigen Antibody

The independent B lymphocyte surface membrane receptors IgM and Fc IgG receptors were evaluated for interactions using immunoflourescence. Ligand [F(ab')2 anti-mu]-induced capping of surface IgM resulted in capping of Fc IgG receptors only if the latter were occupied during the capping process by: (a) soluble antigen-antibody complexes that themselves provided insufficient cross-linking to result in capping; or (b) monomeric IgG at physiologic concentrations (or less) either purified or as normal serum. Ligand-induced capping of Fc IgG receptors did not result in capping of surface IgM occupied by monomeric F(ab') anti-mu. Control experiments showed that ligand binding to or capping of only one of these two receptors has no effect on the other, and that there were no cross-reactions. The interaction appears specific in that ligand-induced capping of surface IgM did not induce capping of ligand-occupied surface IgD or I-A antigens. Thus, there appears to be a specific interaction between ligand-bound surface IgM and ligand-bound Fc IgG receptors on the B lymphocyte surface. The results also indicate that binding of monomeric IgG produces a reversible alteration in the Fc IgG receptor leading to association with ligand-bound surface IgM. Because Fc IgG receptors are continuously exposed to monomeric IgG in vivo, these results suggest that whenever surface IgM is involved in a B lymphocyte response to an immunologic stimulus, the Fc IgG receptor is also involved.

scholarly journals EVIDENCE FOR IDENTITY OR CLOSE ASSOCIATION OF THE Fc RECEPTOR OF B LYMPHOCYTES AND ALLOANTIGENS DETERMINED BY THE Ir REGION OF THE H-2 COMPLEX

1974 ◽  
Vol 140 (3) ◽  
pp. 779-796 ◽  
Author(s):  
Howard B. Dickler ◽  
David H. Sachs
Keyword(s):  
B Lymphocytes ◽  
B Lymphocyte ◽  
Close Association ◽  
Surface Membrane ◽  
Fc Receptor ◽  
F1 Hybrid ◽  
Ia Antigens ◽  
Series Of Experiments ◽  
Mouse Lymphocytes ◽  
Mouse Antibody

Immunoglobulin complexes, composed of heat-aggregated human Ig, were shown to bind to mouse B lymphocytes of a variety of strains, but not to either thymocytes or thymus-derived (T) lymphocytes under a variety of conditions. It was shown that this binding was not due to either natural human antibodies against mouse nor to nonspecific binding of human Ig by mouse lymphocytes. Such complexes were shown to bind to the same sites which bind mouse antibody-antigen complexes. This site is known as the Fc receptor. The binding of Ig complexes to mouse B lymphocytes was markedly inhibited by pretreatment of the lymphocytes with anti-H-2 antisera. A series of experiments indicated the specificity of this result, including the fact that this inhibition was shown not to be due to the artifact of shedding of H-2 antibody-antigen complexes, nor to nonspecific steric inhibition. The antibodies within anti-H-2 antisera which were responsible for this inhibition were specific for alloantigens associated with the Ir region of the H-2 complex (Ia antigens). Antiserum specific for these Ia antigens produced inhibition, whereas antisera specific for antigens determined by the K or D regions of the H-2 complex did not. Evidence was obtained using F1 hybrid cells that at least some Ia antigens of both parental types are expressed on every B lymphocyte (i.e. codominant expression). These data indicate that the Fc receptor and a series of alloantigens controlled by the Ir region of the H-2 complex are identical or closely associated on the B-lymphocyte surface membrane. This observation may have implications for the mechanism of control of the immune response.

The biochemical basis of transmembrane signalling by B lymphocyte surface immunoglobulin

1985 ◽  
Vol 6 (7) ◽  
pp. 218-222 ◽  
Author(s):  
John C. Cambier ◽  
John G. Monroe ◽  
K. Mark Coggeshall ◽  
John T. Ransom
Keyword(s):  
B Lymphocyte ◽  
Biochemical Basis ◽  
Transmembrane Signalling ◽  
Lymphocyte Surface ◽  
Surface Immunoglobulin

scholarly journals Isotypic discordance of paraproteins and lymphocyte surface immunoglobulins in myeloma

Blood ◽  
1981 ◽  
Vol 57 (1) ◽  
pp. 192-195 ◽  
Author(s):  
M Nicholls ◽  
PC Vincent ◽  
E Repka ◽  
J Saunders ◽  
FW Gunz
Keyword(s):  
Multiple Myeloma ◽  
Heavy Chain ◽  
Light Chain ◽  
B Lymphocyte ◽  
Plasma Cells ◽  
Light Chains ◽  
Lymphocyte Surface ◽  
Light Chain Type ◽  
Surface Immunoglobulins ◽  
Chain Type

Abstract B lymphocyte surface immunoglobulins (Smlg) were studied in 24 patients with multiple myeloma by means of anti-isotypic antisera, and their heavy and light chain isotypes were compared in each patient with those of the paraprotein. In 21 patients, lymphocyte Smlg consisted of only one light chain type, and in 16 of only 1 heavy chain type. However, the Smlg and paraprotein heavy and light chain types were identical in only 5 patients while in 6 they differed in heavy and light chain types, in 7 in light chain type, and in 4 in heavy chain type. In 2 patients with light chain myeloma, Smlg light chains were isotypically the same as the paraprotein. Isotypic discordance between paraprotein and Smlg may signify the proliferation of a second malignant clone with failure to differentiate into secreting plasma cells. Alternatively, it is conceivable that the lymphocyte Smlg could have the same idiotypic specificity as the paraprotein despite the isotypic differences, but this will require further studies using anti-idiotypic antisera.

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