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Effect of the ostreolysin A/pleurotolysin B pore-forming complex on intracellular Ca2+ activity in the vascular smooth muscle cell line A10.

  • Academic Journal
  • Vrecl M; Veterinary Faculty, Institute of Anatomy, Histology and Embryology, Gerbičeva 60, SI-1000 Ljubljana, Slovenia.
    Babnik M; Institute of Physiology, Pharmacology and Toxicology, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia.
    Sepčić K; Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
    Žužek MC; Institute of Physiology, Pharmacology and Toxicology, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia.
    Maček P; Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
    Diacci U; Institute of Physiology, Pharmacology and Toxicology, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia.
    Frangež R; Institute of Physiology, Pharmacology and Toxicology, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia. Electronic address: robert.frangez@vf.uni-lj.si.
  • Toxicology in vitro : an international journal published in association with BIBRA [Toxicol In Vitro] 2015 Dec; Vol. 29 (8), pp. 2015-21. Date of Electronic Publication: 2015 Aug 28.
  • English
  • Ostreolysin A/pleurotolysin B (OlyA/PlyB) is a binary pore-forming protein complex that produces a rapid cardiorespiratory arrest. Increased tonus of the coronary vascular wall produced by OlyA/PlyB may lead to ischemia, arrhythmias, the hypoxic injury of cardiomyocytes and cardiotoxicity. We evaluated the effects of OlyA/PlyB in cultured vascular smooth muscle A10 cells. Fluorometric measurements using the Ca(2+) indicator Fluo-4 AM and Fura-2 AM revealed that nanomolar concentrations of OlyA/PlyB increased the intracellular Ca(2+) activity [Ca(2+)]i in A10 cells. This effect was absent in a Ca(2+)-free medium, indicating that OlyA/PlyB-induced [Ca(2+)]i increase was dependent on Ca(2+) influx into cells. The increase in [Ca(2+)]i by OlyA/PlyB was partially prevented by: i) the calcium channel blockers verapamil and La(3+), ii) the inhibitor of the sodium-calcium exchanger (NCX) benzamil, and iii) the iso-osmotic replacement of NaCl by sucrose. The pre-treatment of cells with the Ca(2+)-ATPase inhibitor thapsigargin reduced the [Ca(2+)]i increase evoked by OlyA/PlyB, whereas the plasma membrane depolarization with high K(+) in the medium did not prevent OlyA/PlyB-induced [Ca(2+)]i. In summary, our data could suggest that the OlyA/PlyB-induced increase in [Ca(2+)]i is due to an influx of Ca(2+) through a variety of co-existing plasma membrane Ca(2+)-permeable channels, Ca(2+) entry through non-selective ion permeable pores formed de novo by OlyA/PlyB in the plasma membrane and calcium-induced intracellular Ca(2+) release, altogether leading to disturbed Ca(2+) homeostasis in A10 cells.
    (Copyright © 2015 Elsevier Ltd. All rights reserved.)
Additional Information
Publisher: Pergamon Press Country of Publication: England NLM ID: 8712158 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-3177 (Electronic) Linking ISSN: 08872333 NLM ISO Abbreviation: Toxicol In Vitro Subsets: MEDLINE
Original Publication: Oxford ; New York : Pergamon Press, c1987-
Keywords: Fluo-4/AM; Fura-2/AM; OlyA/PlyB; Ostreolysin; Smooth muscle cells; [Ca(2+)](i)
0 (Fungal Proteins)
SY7Q814VUP (Calcium)
Date Created: 20150901 Date Completed: 20160826 Latest Revision: 20151103
20211214
10.1016/j.tiv.2015.08.014
26320834
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