A new concept of triggering mechanisms of IgE-mediated histamine release

Ishizaka, Kimishige; Conrad, Daniel H.; Froese, Arnold

doi:10.1016/0091-6749(78)90054-4

Cited by 65 publications

(22 citation statements)

References 25 publications

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“…3s j Froese, 1978). rt is quite obvious that HRMC12.6 has two different cell surface molecules (Fig-37c) (Froese, HRMC12.6 appears to be associated with both mol-ecuIes.…”

Section: Histamine Content Determinationsmentioning

confidence: 98%

Establishment and characterization of hybrid rat mast cells

Zheng

Chan

Rector

et al. 1991

Experimental Cell Research

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“…3s j Froese, 1978). rt is quite obvious that HRMC12.6 has two different cell surface molecules (Fig-37c) (Froese, HRMC12.6 appears to be associated with both mol-ecuIes.…”

Section: Histamine Content Determinationsmentioning

confidence: 98%

Establishment and characterization of hybrid rat mast cells

Zheng

Chan

Rector

et al. 1991

Experimental Cell Research

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“…Furthermore, in this study increased phosphorylation of the a component is demonstrated to be a selective effect of antigen because little change is found in phosphorylation of the predominant phosphoproteins in unpurified Nonidet P-40 extracts of the major contaminants of receptor preparations (in the Mr 67,000-90,000 region) or of the P component of the IgE receptor. Because apposition of adjacent IgE receptors is the necessary and sufficient signal for mediator release (8) (28). Thus, although the RBL line has been a good model for studying IgE receptor structure (3), study of the mechanism of IgE receptor signal transduction may require normal mast cells.…”

Section: Selective Phosphorylation Of Ige Receptor a Componentmentioning

confidence: 99%

“…The apposition of adjacent receptors on rat mast cells is the necessary and sufficient signal (8) for cell activation leading to the noncytotoxic release and generation of a variety of cellular mediators. Mast cell activation has been associated with changes in diacylglycerol levels (9), phospholipid methylation (10), cyclic AMP levels (11), influx of calcium (10), and protein phosphorylation (12).…”

mentioning

confidence: 99%

Selective phosphorylation of the IgE receptor in antigen-stimulated rat mast cells.

Hempstead¹,

Parker²,

Kulczycki³

1983

Proc. Natl. Acad. Sci. U.S.A.

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Purified rat serosal mast cells were sensitized with mouse immunoglobulin E (IgE) anti-2,4-dinitrophenyl antibody, partially depleted of phosphate, labeled with [32P]orthophosphate, and stimulated with dinitrophenylated bovine serum albumin or control protein. After 15-120 seconds at 37C, the cells were extracted with nonionic detergent. IgE receptors were purified by repetitive affinity chromatography and were analyzed by NaDodSO4/polyacrylamide gel electrophoresis and radioautography. Antigenic stimulation of intact rat mast cells produced a rapid and marked increase in the phosphorylation of the surface-exposed a component of the IgE receptor. However, phosphorylation of the 33,000 Mr (3 component of the IgE receptor was not altered significantly by antigen stimulation. This suggests that the selective increase in phosphorylation of the IgE receptor a component may be part of the physiologic mediator secretion process triggered by antigen.Mast cells and basophils have cell-surface receptors that bind IgE with high affinity. Each IgE receptor is composed of a surface-exposed glycoprotein (1, 2), referred to as the a component in recent terminology (3), and a nonglycosylated protein (4, 5) termed the ,B component. Tryptic peptide mapping studies indicate that each component is a distinct polypeptide (6). The a component of rat mast cells, Mr 45,000 (7), is somewhat smaller than the a component of rat leukemic basophils analyzed in the same NaDodSO4/polyacrylamide gel system (6), whereas P components of both cell types are indistinguishable in size (Mr 33,000) (6, 7).The apposition of adjacent receptors on rat mast cells is the necessary and sufficient signal (8) for cell activation leading to the noncytotoxic release and generation of a variety of cellular mediators. Mast cell activation has been associated with changes in diacylglycerol levels (9), phospholipid methylation (10), cyclic AMP levels (11), influx of calcium (10), and protein phosphorylation (12). We have demonstrated that the IgE receptor a component of rat mast cells is a phosphoprotein and that its phosphorylation is significantly increased by a nonimmunologic stimulus of histamine release (7). In this study, we demonstrate that an immunologic stimulus with antigen produces a rapid and selective increase in phosphorylation of the a component of the rat mast cell IgE receptor. Thus, it seems possible that increased phosphorylation of the receptor a component is part of the antigen-stimulated process leading to mediator secretion. MATERIALS AND METHODSAntigen and IgE Antibody. The monoclonal 2,4-dinitrophenyl (DNP)-specific murine IgE antibody H1 DNP-E-26 (13) was isolated from ascites from the hybridoma made available by Fu-Tong Liu and David Katz. Protein soluble in 30% saturated ammonium sulfate was precipitated by 60% saturated ammonium sulfate (13) and was further purified by gel filtration on Sepharose CL-6B. Based on polyacrylamide gel electrophoresis in NaDodSO4, the IgE was >95% pure. DNP-treated bovine serum albumin (DNP-albumin...

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“…It has been established that human baso phils have specific receptors for IgE mole cules and that the bridging of these recep tors is the activating signal which results in histamine release [7,8]. Cross-linking of the surface-bound IgE can be achieved physiol ogically by antigens [15] or experimentally by anti-IgE (a-IgE) antibodies [14].…”

Section: Introductionmentioning

confidence: 99%

IgE-Mediated Histamine Release from Human Basophils: Differences between Antigen E- and Anti-IgE-Induced Secretion

Marone¹,

Kagey‐Sobotka²,

Lichtenstein³

1981

Int Arch Allergy Immunol

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The mechanism of the IgE-mediated release of histamine from human basophils differs when the process is initiated by antigen as compared to anti-IgE (a-IgE). Antigen causes release from the basophils of different individuals over a wide range of concentrations, while release to a-IgE occurs over a limited concentration range; antigen excess inhibition is also relatively slight as compared to that observed with a-IgE. Release by antigen occurs with a shorter lag period and a more rapid rate than seen with a-IgE· Agonists which inhibit release by acting through adenylate cyclase (dimaprit, adenosine, isoproterenol) are significantly more potent with respect to antigen than to a-IgE-induced release. Other agonists (3-isobutyl-1-methylxanthine, dibutyryl cyclic AMP) which increase cyclic AMP by different mechanisms are equally effective against antigen and a-IgE, suggesting that the receptor-adenylate cyclase interactions differ between the two stimuli. The cyclooxygenase inhibitor, indomethacin, consistently enhances antigen- but not a-IgE-induced release while cytochalasin B, which acts in part on microfilaments, enhances both processes equally. These data indicate that cross-linking of surface antibody IgE by antigen initiates a release process different from that caused by a-IgE, perhaps because the former is a multivalent ligand and the latter is functionally bivalent.

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A new concept of triggering mechanisms of IgE-mediated histamine release

Cited by 65 publications

References 25 publications

Establishment and characterization of hybrid rat mast cells

Establishment and characterization of hybrid rat mast cells

Selective phosphorylation of the IgE receptor in antigen-stimulated rat mast cells.

IgE-Mediated Histamine Release from Human Basophils: Differences between Antigen E- and Anti-IgE-Induced Secretion

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