Cytophilic Antibodies

Leslie, R. G. Q.; Alexander, Manfred

doi:10.1007/978-3-642-67331-3_2

Cited by 22 publications

(15 citation statements)

References 247 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The positive cells were shown to be viable monocytes, and the antibodies could be shown to be binding in a saturable manner to the cell surface and not to the nucleus. Two of the anti-histone antibodies used, including the strongest reactor, were IgM, and thus Fc receptor-mediated binding did not seem likely (30). We also showed that the marked increase in positive cells after 12 to 16 h of culture was not paralleled by a similar kinetic change in Fc receptor-mediated binding of aggregated human Ig.…”

Section: Discussionmentioning

confidence: 71%

Human peripheral blood monocytes display surface antigens recognized by monoclonal antinuclear antibodies.

Holers¹,

Kotzin²

1985

J. Clin. Invest.

View full text Add to dashboard Cite

We used monoclonal anti-nuclear autoantibodies and indirect immunofluorescence to examine normal human peripheral blood mononuclear leukocytes for the presence of cell surface nuclear antigens. Only one monoclonal anti-histone antibody (MH-2) was found to bind to freshly isolated PBL, staining 10% of large cells. However, after cells were placed into culture for 16-24 h, a high percentage (up to 60%) of large-sized cells were recognized by an anti-DNA (BWD-1) and several different antihistone monoclonal antibodies (BWH-1, MH-1, and MH-2). These antibodies recognize separate antigenic determinants on chromatin and histones extracted from chromatin. None of the monoclonal autoantibodies appeared to bind to a significant percentage of cells of relatively small cell size, either before or after culture. The histone antigen-positive cells were viable, and the monoclonal antibodies could be shown to be binding to the cell surface and not to the nucleus. Further experiments, including those using aggregated Ig to block antibody binding, strongly indicated that anti-histone antibody binding was not Fc receptor mediated. Using monoclonal antibodies specific for monocytes and T cells, and complement-mediated cytotoxicity, the cells bearing histone antigens were shown to be primarily monocytes. The appearance of histone and DNA antigen-positive cells was nearly completely inhibited by the addition of low concentrations (0.25 sg/ml) of cycloheximide at initiation of the cultures. In contrast, little effect on the percentage of positive cells was detected if cells were exposed to high doses of gamma irradiation before culture. These data further support the existence of cell surface nuclear antigens on selected cell subsets, which may provide insight into the immunopathogenesis of systemic lupus erythematosus and related autoimmune diseases.

show abstract

Section: Discussionmentioning

confidence: 71%

Human peripheral blood monocytes display surface antigens recognized by monoclonal antinuclear antibodies.

Holers¹,

Kotzin²

1985

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…Later, it was found that the IgE class is perhaps the most representative type of cytophilic Ig molecule. Reaginic IgE antibody has strong binding to IgE-specific FcR on various cell types, and this interaction triggers release of histamine and other pharmacologically active agents upon antigen attachment (7,8). More recently, it has been reported that IgAl also may be cytophilic (9), but to our knowledge there are no available data regarding IgD.…”

Section: Ig Classes and Cell Types Involved In The Cytophilic Interacmentioning

confidence: 97%

Cytophilic immunoglobulins revisited via natural killer cells

Sulica¹,

Herberman

1996

FASEB j.

View full text Add to dashboard Cite

Cytophilia is one of the biologic properties of the Fc region of immunoglobulins operationally defined as the ability of an antibody molecule to attach to certain cell types before combination with antigen. By attachment of cytophilic antibody to membrane Fc receptors, cells become "armed" with antibodies and able to interact specifically with soluble or particulate antigens. In contrast to this cytophilia, the so-called opsonic antibody binds to FcR of various cell types only after it has complexed with antigen. In spite of knowledge of cytophilic properties of immunoglobulins for more than 30 years and an impressive accumulation of facts regarding the structure and function of cell-surface FcR binding IgG, IgE, or IgA molecules, less progress has been made in understanding the molecular basis of cytophilia. Our extensive studies of the structural and functional aspects of the interaction of IgG in monomeric form with human natural killer cells, via the type IIIA IgG Fc receptor (Fc gamma RIIIA), provide a focal point for revisiting this major pathway of direct and continuous communication between the humoral and cellular compartments of the immune system.

show abstract

“…When the macrophages are overloaded (5-9), or otherwise impaired in their function (9)(10)(11)(12)(13)(14), or when the phagocytes cannot interact with the complexes because of chemical modi-less, or not at all capable of triggering phagofication of the antibodies (23), an overflow of cytosis (34), and neither is IgM. Yet, IgM antiimmune complexes can occur to sites that are DNA antibodies are associated with a milder not suitable for the elimination of these com-course of SLE (35,36) than are IgG antibodies, plexes (e.g.…”

Section: Size Of the Complexesmentioning

confidence: 99%

Factors Influencing the Development of Immune‐Complex Diseases

Lamers

1981

Allergy

View full text Add to dashboard Cite

Cytophilic Antibodies

Cited by 22 publications

References 247 publications

Human peripheral blood monocytes display surface antigens recognized by monoclonal antinuclear antibodies.

Human peripheral blood monocytes display surface antigens recognized by monoclonal antinuclear antibodies.

Cytophilic immunoglobulins revisited via natural killer cells

Factors Influencing the Development of Immune‐Complex Diseases

Contact Info

Product

Resources

About