Receptor Sites of Human Monocytes for IgG

Huber, H.; Fudenberg, H. Hugh

doi:10.1159/000230091

Cited by 330 publications

(94 citation statements)

References 8 publications

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“…This small difference between (Fab')2 and Fab suggested that the attachment of anti-Dcoated cells was partly blocked by a portion of (Fab~)2 residing in the vicinity of the inter-heavy chain disulfide bond. This is consistent with the report that (Fab~)2 of anti-D, when attached to red ce]ls, formed rosettes, although not as effectively as with intact anti-D (18). Pepsin component II, a noncovalently linked dimer of 116 amino acids of the C-terminal end of IgG, and smaller peptides, components III and IV, all failed to inhibit rosette formation.…”

Section: Resultssupporting

confidence: 91%

See 1 more Smart Citation

The Interaction Between Human Monocytes and Red Cells

Abramson

Gelfand

Jandl

et al. 1970

The Journal of Experimental Medicine

191

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Red cells coated with IgG globulin are bound circumferentially about a central mononuclear cell or monocyte into a "rosette" (1). Attached red cells appear deformed and closely resemble the abnormal red cell morphology frequently observed in the peripheral blood of patients with Coombs positive hemolytic anemia associated with IgG antibodies. Although in some studies the monocyte receptor was specific for IgG globulin without specificity for the third component of complement (C3) (1, 2), in others a receptor for C3 (3, 4) as well as a nonspecific receptor (5) have been described. We report here confirmation of the IgG specificity of the mononuclear cell receptor for rosette formation. A C3 receptor for rosette formation was not observed. Some of the well described biologic functions of the Fc fragment of IgG globulin reside in selective IgG subclasses (6). IgG subclass specificity for rosette formation is described in this report in addition to studies which further delineate the peptide portion of the Fc fragment of IgG that binds to the monocyte. 1 Materials and MethodsProteins.--Sera containing high titers of anti-D were obtained from patients with Rh incompatibility as a result of pregnancy and from one individual previously immunized. These anti-D antibodies were warm-active IgG globulins. Sera containing cold agglutinins (anti-l) were derived from patients who had mycoplasma pneumonia or from individuals with "idio-

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Section: Resultssupporting

confidence: 91%

“…As shown in Table I I (18). Since anti-D antibody is'reported to be composed of IgG1 and IgG3 molecules (19), the inhibition of rosette formation by free IgG1 and IgG3 does not by itself indicate the selectivity of the receptor site for these antibody subclasses.…”

Section: Resultsmentioning

confidence: 99%

The Interaction Between Human Monocytes and Red Cells

Abramson

Gelfand

Jandl

et al. 1970

The Journal of Experimental Medicine

191

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“…In addition to B lymphocytes, there is much evidence that other cell types can also bind immunoglobulin, including some T lymphocytes (22), activated T lymphocytes (22,36,37), monocytes and macrophages (38,39), and basophils (40). The present observations raise the question of whether the Ig-binding site(s) of these other cell types may also be associated with Ia antigens.…”

Section: Failure Of Antisera Against the K And D Regions Of The H-2 Cmentioning

confidence: 99%

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

Dickler

Sachs

1974

The Journal of Experimental Medicine

172

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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.

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“…It is thus significant that the Gm'0 allotype is restricted to the IgG3 sub-class (Martensson and Kunkel, 1965) whilst the Gm' and Gm2 allotypes are restricted to IgGl (Terry, Fahey and Steinberg, 1965; for review see Grubb, 1970). Other workers have shown that whilst IgGI and IgG3 are efficient in-hibitors, both of the phagocytosis of antibody-coated erythrocytes by monocytes (Huber and Fudenberg, 1968) and HEA rosetting by lymphocytes, (Fr0land et al, 1974a), IgGl is much less efficient than IgG3 in attaching to leucocyte Fc receptors (Abramson et al, 1970b).…”

Section: Discussionmentioning

confidence: 99%