IgE receptor-activated calcium permeability pathway in rat basophilic leukemia cells: measurement of the unidirectional influx of calcium using quin2-buffered cells

Fewtrell, Clare; Sherman, Emily J.

doi:10.1021/bi00396a021

Cited by 47 publications

(29 citation statements)

References 44 publications

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“…The ratio of Ca 2ϩ -bound indicator to Ca 2ϩ -free indicator can be estimated, and n CB (changes in the number of Ca 2ϩ -bound indicators) can be evaluated by the changes in the fluorescence intensity. Hence, if the amount of increase in total Ca 2ϩ can be calculated, the endogenous Ca 2ϩ -buffering capacity can be estimated based on the assumption that Ca 2ϩ that enters the cell diffuses throughout the cell immediately (before the pump or sequestration mechanism work) (108,272,274,410). In addition, sufficiently loaded Ca 2ϩ indicators dominate the intrinsic Ca 2ϩ buffers and allow accurate quantification of Ca 2ϩ efflux across the plasma membrane (176,272,274).…”

Section: A Intracellular Bufferingmentioning

confidence: 99%

Measurement of Intracellular Calcium

Takahashi

Camacho

Lechleiter

et al. 1999

Physiological Reviews

668

511

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To a certain extent, all cellular, physiological, and pathological phenomena that occur in cells are accompanied by ionic changes. The development of techniques allowing the measurement of such ion activities has contributed substantially to our understanding of normal and abnormal cellular function. Digital video microscopy, confocal laser scanning microscopy, and more recently multiphoton microscopy have allowed the precise spatial analysis of intracellular ion activity at the subcellular level in addition to measurement of its concentration. It is well known that Ca2+ regulates numerous physiological cellular phenomena as a second messenger as well as triggering pathological events such as cell injury and death. A number of methods have been developed to measure intracellular Ca2+. In this review, we summarize the advantages and pitfalls of a variety of Ca2+ indicators used in both optical and nonoptical techniques employed for measuring intracellular Ca2+ concentration.

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Section: A Intracellular Bufferingmentioning

confidence: 99%

Measurement of Intracellular Calcium

Takahashi

Camacho

Lechleiter

et al. 1999

Physiological Reviews

668

511

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“…This assay was based on the method of Fewtrell and Sherman (1987). IgE-sensitized RBL cells were placed in 24-well Vol.…”

Section: Ca2" Influx Assaymentioning

confidence: 99%

“…Phospholipase C hydrolyzes the phosphoinositides to produce inositol phosphates and diacylglycerol, which lead to the increase in intracellular Ca2' and activation of protein kinase C (PKC), respectively (Beaven et al, 1984a,b;Cunha-Melo et aL, 1987). The increase in cytoplasmic Ca21 is due mainly to the influx of extracellular Ca2+ through an ion channel, although there is also probably release from intracellular stores (Beaven et al, 1984b;Fewtrell and Sherman, 1987; Mohr and Fewtrell, 1987). Phospholipase A2 activation is responsible for the production of lysophospholipids and arachidonic acid, which is further metabolized into the prostaglandins and leukotrienes (Crews et al, 1981).…”

Section: Introductionmentioning

confidence: 99%

Association of the crosslinked IgE receptor with the membrane skeleton is independent of the known signaling mechanisms in rat basophilic leukemia cells.

Apgar¹

1991

Cell Regul

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Crosslinking of the IgE receptor on the surface of rat basophilic leukemia (RBL) cells by multivalent antigen induces an association of these receptors with the detergent-insoluble membrane skeleton. Detergent insolubility of the receptor can also be induced on purified plasma membranes isolated from RBL cells by the use of either IgE oligomers or IgE monomers plus multivalent antigen. The critical event in initiating this interaction between the receptor and the membrane skeleton is crosslinking of the receptor. This association is rapid, and, when triggered by multivalent antigen, it is quickly reversed by the addition of excess monovalent antigen. The fact that this association occurs with the use of purified plasma membranes indicates that all of the components necessary for this interaction are present in the plasma membrane and that intracellular components are not required.Although crosslinking of the receptor activates phospholipase C and phospholipase A2 leading to the generation of several second messengers, none of these signaling mechanisms appears to be involved in IgE receptor interaction with the membrane skeleton. This interaction cannot be induced by phorbol 12-myristate 13-acetate (PMA), ionomycin, or a combination of these two reagents, although this will result in degranulation. Furthermore, receptor detergent insolubility is temperature independent when triggered by multivalent antigen, thus indicating that enzyme-catalyzed reactions are not important. This was verified by the fact that a variety of inhibitors that block phosphatidylinositol metabolism, arachidonic acid metabolism, Ca2l influx, and protein kinase C (PKC) activation had no effect on antigen-induced association of the receptor with the membrane skeleton. These results indicate that the signaling mechanisms leading to the degranulation response are not involved in the association of the crosslinked receptor with the membrane skeleton.

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“…For control experiments, DMSO alone was included in the modified Tyrode's solution to keep the concentration of DMSO the same for both control and PMA-treated cells. The concentration of antigen used for these experiments, 1 g/ml, is optimal for secretion (Fewtrell and Sherman, 1987). Secretion assays were performed periodically to ensure that the cells were functional.…”

Section: ؉ Imaging Experimentsmentioning

confidence: 99%

Protein kinase C activator PMA reduces the Ca2+ response to antigen stimulation of adherent RBL-2H3 mucosal mast cells by inhibiting depletion of intracellular Ca2+ stores

Kuchtey

Fewtrell

1999

J. Cell. Physiol.

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Activation of protein kinase C has been shown to reduce the Ca(2+) responses of a variety of cell types. In most cases, the reduction is due to inhibition of Ca(2+) influx, but acceleration of Ca(2+) efflux and inhibition of Ca(2+) store depletion by protein kinase C activation have also been described. For adherent RBL-2H3 mucosal mast cells, results from whole-cell patch clamp experiments suggest that protein kinase C activation reduces Ca(2+) influx, while experiments with intact, fura-2-loaded cells suggest that Ca(2+) influx is not affected. Here we present single-cell data from Ca(2+) imaging experiments with adherent RBL-2H3 cells, showing that antigen-stimulated Ca(2+) responses of phorbol 12-myristate 13-acetate (PMA)-treated cells are more transient than those of control cells. PMA also reduced the response to antigen in the absence of extracellular Ca(2+), indicating that depletion of intracellular Ca(2+) stores is inhibited. If PMA was added after stores had been depleted by thapsigargin, a small decrease in [Ca(2+)](i) was observed, consistent with a slight inhibition of Ca(2+) influx. However, the major effect of PMA on the antigen-stimulated Ca(2+) response is to inhibit depletion of intracellular Ca(2+) stores. We also show that inhibition of protein kinase C did not enhance the Ca(2+) response to antigen, suggesting that inhibition of the Ca(2+) response by activation of protein kinase C does not contribute to the physiological response to antigen.

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IgE receptor-activated calcium permeability pathway in rat basophilic leukemia cells: measurement of the unidirectional influx of calcium using quin2-buffered cells

Cited by 47 publications

References 44 publications

Measurement of Intracellular Calcium

Measurement of Intracellular Calcium

Association of the crosslinked IgE receptor with the membrane skeleton is independent of the known signaling mechanisms in rat basophilic leukemia cells.

Protein kinase C activator PMA reduces the Ca2+ response to antigen stimulation of adherent RBL-2H3 mucosal mast cells by inhibiting depletion of intracellular Ca2+ stores

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