Soluble forms of low affinity Fc gamma receptors, process for th

Details Soluble forms of low affinity Fc gamma receptors, process for th Soluble forms of low affinity Fc gamma receptors, process for th

1989-04-07

1993-06-15

Nucker, Christine M.

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving antigen-antibody binding, specific binding protein...

530380, 530395, 435 79, 435 792, 435 794, 435 795, 514 2, 514 8, C12Q 100, G01N 3353, A61K 3514, A61K 3700, A61K 3710, A61K 3704, A01N 3718, C07K 300

Patent

active

052197280

DESCRIPTION:

BRIEF SUMMARY
The present invention relates to soluble forms of low affinity receptors for the Fc fragment of IgG molecules; the present invention also relates to a method for the identification and assay of soluble forms of low affinity Fc gamma receptors, especially human soluble Fc receptors; it also relates to a kit of the reagents necessary for carrying out this method; it relates finally to the applications of this method for the diagnosis of pathological conditions in which the above-mentioned receptors are involved, such as infectious diseases, autoimmune diseases, transplant rejections, human complex diseases, cancers, myelomas and acquired immune deficiency syndrome (AIDS), for the therapeutic monitoring of the course of these conditions, as well as for the study of human polymorphisms.
At the surface of many cells, in particular the cells of the immune system (macrophages, B lymphocytes, polymorphonuclear leukocytes, NK cells, and the like), there are receptors which permit a relationship between antibodies or immunoglobulins and these cells are involved in immunity. These receptors have an affinity for the Fc fragment of antibodies (FcR). This Fc fragment corresponds to the portion of immunoglobulins not endowed with antibody activity. The importance of these receptors is considerable, since their mediation makes possible the recognition of foreign antigens (viruses, tumor cells and the like) and the initiation of a cytotoxic reaction, by T lymphocytes or humoral, with secretion of specific antibodies by B lymphocytes; phagocytosis, that is to say the extraction from tissues and the blood of particles recognized as foreign by the cells of the reticuloendothelial system (monocytes, macrophages); cell interactions between different cells involved in immunity; the transplacental transfer of antibodies from mother to fetus; and the clearance of immune complexes whose pathogenic role in many conditions is known.
The existence of a secretion of these receptors for the Fc fragment (FcR) by mouse T cell cultures activated by a specific activator has been demonstrated. These Fc receptor molecules, secreted in vitro under very special conditions of activation and culture (in particular, in medium devoid of all serum, which has a deleterious effect on the cells in culture), still possess the capacity to bind immunoglobulins through their Fc fragment, and they have hence been christened "immunoglobulin binding factor" (IBF). The existence of this type of IBF has been demonstrated for three classes of immunoglobulins, IgG, IgA and IgE, namely the factors IgGBF, IgABF and IgEBF.
It has, moreover, been demonstrated that these IBF molecules are capable, when they are in contact with B lymphocytes in culture, or even myeloma cells in vitro, of completely inhibiting the activation of these cells and, as a result, the secretion of immunoglobulins by these B or myeloma cells. The molecules in question are hence secreted by cells belonging to the immune system under artificial conditions of in vitro culture, but are nevertheless endowed with a functional capacity to bind antibodies and to bring about a substantial suppression of the activation of the B lymphocyte system (lymphokine).
The existence of an Fc receptor for mouse IgG immunoglobulins (FcR) in mouse serum has been demonstrated. These molecules have been defined both by their capacity to be recognized by a monoclonal antibody specific for mouse Fc gamma receptors (monoclonal antibody 2.4G2) and their functional capacity to be purified from immunoglobulin Fc fragments. This discovery is extremely important, since this lymphokine is secreted at a level which increases with age (level zero at birth, appearing at around the fifth day in newborn mice and becoming systematically detectable at around the seventh day), that this level increases in proportion to the presence of infections or, more generally, that the immune system is stimulated (mice kept in a microbe-free environment having strictly zero levels throughout their life), this level being, moreover, determined in a

REFERENCES:
Fleit et al (1982) Human neotrophil Fc .gamma.receptor . . . PNAS 79:3275-3279.
Ruan et al (1984) Abstract only CA 103:35728 The Immune Detection . . . .
Khayat et al (1984) Circulatory Cell Free Fe .gamma.2b/.gamma.1 . . . J Immunol 132:2496-2501.
Fleit et al., "Identification of a Soluble Form of a Human . . . ", J. leukocyte Biol. vol. 40 (3) p. 252 (1986).
Ulvestad et al., "Soluble Fc .gamma. Receptors (FcR) in Human Sera . . . ", Scandonovian J. of Immunology vol. 24(4) p. 481 (1986).
Pure et al., "Identification of Soluble Fc Receptors . . . ", J. Exp. Med vol. 160, pp. 1836-1849 (1984).
Perussia et al, "The Fc Receptor for IgG on Human . . . ", The Journal of Immunology, vol 133, No. 1, pp. 180-188 (1984).
Khayat et al, "Soluble circulating Fc gamma receptors . . . " Journal of Immunological, Methods, vol. 100, Jun. 26, 1987 pp. 235-241.
Looney et al, "Humman monoytes and U937 Cells . . . " Journal of Immunology, vol. 136 No. 5 1986.
Anderson et al, "Monoclord antibodies to Fc receptors . . . ", Chem. Abstracts, vol. 261 (27), 12856-64, 1986.
Fleit et al, "Identification of a soluble . . . ", Biological Abstracts vol. 40, No. 3, p. 252 1987.
Pure et al., "Identification of soluble Fc receptors . . . ", Chem. Abstracts, vol. 102, No. 11 (1985).
Rosenberg et al, "Fc receptors for IgG . . . ", Chem Abstracts vol. 103, No. 17 (1985).

Affiliated with

Also associated with

Rating

Soluble forms of low affinity Fc gamma receptors, process for th does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Soluble forms of low affinity Fc gamma receptors, process for th, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Soluble forms of low affinity Fc gamma receptors, process for th will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-1041872