ArticleThe Journal of membrane biology1997
Protein kinase C-independent correlation between P-glycoprotein expression and volume sensitivity of Cl- channel.
Article in The Journal of membrane biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Physiology of the volume-sensitive/regulatory anion channel VSOR/VRAC: part 2: its activation mechanisms and essential roles in organic signal release.The journal of physiological sciences : JPS · 2024Review
- Physiology of the volume-sensitive/regulatory anion channel VSOR/VRAC. Part 1: from its discovery and phenotype characterization to the molecular entity identification.The journal of physiological sciences : JPS · 2024Review
- Specific and essential but not sufficient roles of LRRC8A in the activity of volume-sensitive outwardly rectifying anion channel (VSOR).Channels (Austin, Tex.) · 2017Article
- Evidence for P-Glycoprotein Involvement in Cell Volume Regulation Using Coulter Sizing in Flow Cytometry.International journal of molecular sciences · 2015Article
- Identification of key signaling molecules involved in the activation of the swelling-activated chloride current in human glioblastoma cells.The Journal of membrane biology · 2014Article
- Pathophysiology and puzzles of the volume-sensitive outwardly rectifying anion channel.The Journal of physiology · 2009Review
- Regulation of volume-activated chloride channels by P-glycoprotein: phosphorylation has the final say!The Journal of physiology · 2000Review
- Reduced intracellular ionic strength as the initial trigger for activation of endothelial volume-regulated anion channels.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- High intracellular chloride delays the activation of the volume-sensitive chloride conductance in mouse L-fibroblasts.The Journal of physiology · 1999Article
- Protein kinase C isoenzyme patterns characteristically modulated in early prostate cancer.The American journal of pathology · 1999Article
- A serine residue in ClC-3 links phosphorylation-dephosphorylation to chloride channel regulation by cell volume.The Journal of general physiology · 1999Article
- Criteria for the molecular identification of the volume-sensitive outwardly rectifying Cl- channel.The Journal of general physiology · 1998Article
- Protein kinase C phosphorylation disengages human and mouse-1a P-glycoproteins from influencing the rate of activation of swelling-activated chloride currents.The Journal of physiology · 1998Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The possible correlation between P-glycoprotein (PGP) and volume-sensitive Cl- channel was examined in a pair of cell lines: a subline of the human epidermoid KB cell (KB-3-1) and the corresponding MDR1-transfected cell line (KB-G2). Western blot analysis and indirect immunofluorescence studies indicated that KB-G2, but not KB-3-1, exhibits the PGP expression. Patch-clamp whole-cell recordings showed that osmotic swelling activates Cl- currents not only in PGP-expressing but also in PGP-lacking cells. The amplitude of the maximal current was indistinguishable between both cells. Activation of protein kinase C (PKC) or loading with a PKC inhibitor failed to affect the swelling-induced activation of the Cl- currents in both cells. The relation between whole-cell Cl- currents and cell size measured simultaneously showed that volume sensitivity of the Cl- channel was augmented by the PGP expression irrespective of the activity of PKC on the plasma membrane. A similar increase in volume sensitivity of the Cl- channel was also induced by the expression of the ATP hydrolysis-deficient PGP mutant, K433M. We conclude that P-glycoprotein does not represent the volume-sensitive Cl- channel but that its expression modulates volume sensitivity of the Cl- channel in a manner independent of its ATPase activity or of the protein kinase C activity.
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