chlortetracycline and 3-3--dihexyl-2-2--oxacarbocyanine

chlortetracycline has been researched along with 3-3--dihexyl-2-2--oxacarbocyanine* in 2 studies

Other Studies

2 other study(ies) available for chlortetracycline and 3-3--dihexyl-2-2--oxacarbocyanine

ArticleYear
Two distinct Ca2+ storage and release sites in human neutrophils.
    Journal of leukocyte biology, 1998, Volume: 63, Issue:2

    It is well established that changes in cytosolic free Ca2+ play a role in a number of neutrophil responses such as cell shape change and oxidase activation. The release of intracellular stored Ca2+ occurs with stimuli that either act by occupancy of seven membrane-spanning domain receptors or those which act by receptor cross-linking. Here, two distinct Ca2+ storage and release sites have been identified in neutrophils. Using chlortetracycline fluorescence as an indicator of Ca2+ storage, two separate Ca2+ storage sites have been identified. One site was located peripherally under the plasma membrane and the other was in the juxtanuclear space. Confocal imaging of Fluo3-loaded neutrophils demonstrated that the central Ca2+ storage site released Ca2+ in response to N-formyl-methionyl-leucyl-phenylalanine, whereas engagement and clustering of CD11b/CD18 integrins causes Ca2+ release from the peripheral stores. The release sites also correlated with organelles that stained with DiOC6(3). Localized phototoxicity generated by DiOC6(3) excitation resulted in inhibition of the release of stored Ca2+, which was selective for the stimulus used. The presence of two distinct cellular locations for these Ca2+ stores and their independent release raises the possibility that separate intracellular messengers for their release are generated.

    Topics: Calcium; Carbocyanines; Cell Compartmentation; Cell Membrane; Cell Nucleus; Cell Size; Chlortetracycline; Fluorescent Dyes; Humans; Microscopy, Confocal; N-Formylmethionine Leucyl-Phenylalanine; Neutrophil Activation; Neutrophils; Signal Transduction

1998
Does actin polymerization status modulate Ca2+ storage in human neutrophils? Release and coalescence of Ca2+ stores by cytochalasins.
    Experimental cell research, 1997, Aug-01, Volume: 234, Issue:2

    The aim of this paper was to establish whether actin polymerization modulated cytosolic Ca2+ storage in human neutrophils. Over the concentration ranges which inhibit actin polymerization, cytochalasins A, B, and D liberated Ca2+ from membrane-bound stores within neutrophils. Two Ca2+ storage sites were identified in neutrophils by the accumulation of the Ca2+ binding probe, chlortetracycline: one at the center of the cell and the other at the cell periphery. Confocal imaging demonstrated that cytochalasins released Ca2+ from the neutrophil periphery, but not from the central Ca2+ store. Ca2+ store release was coupled to Ca2+ influx, suggesting that the peripheral site may be a physiological store containing a Ca2+ influx factor. 3,3'-Dihexyloxacarbocyanine iodide staining organelles, which correlate with Ca2+ release sites, coalesced in neutrophils after treatment with cytochalasins. We propose that peripheral Ca2+ storage sites are restricted from coalescence by cortical polymerized actin and that Ca2+ store coalescence and Ca2+ release are coupled events.

    Topics: Actins; Animals; Botulinum Toxins; Calcium; Carbocyanines; Chelating Agents; Chlortetracycline; Cytochalasins; Cytosol; Fluorescent Dyes; Humans; Intracellular Membranes; Ionomycin; Ionophores; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Poly(ADP-ribose) Polymerases; Polymers; Rats

1997
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