Expression of P-glycoprotein in L1210 cells is linked with rise in sensitivity to Ca2+
| Autor: | Uhrík B, Jozef Orlický, Mário Šereš, Roderik Fiala, Lenka Gibalová, Albert Breier, Zdena Sulova, Ima Dovinova |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Biophysics
chemistry.chemical_element Calcium Biochemistry Calcium in biology Mice chemistry.chemical_compound Adenosine Triphosphate Animals ATP Binding Cassette Transporter Subfamily B Member 1 Leukemia L1210 Molecular Biology P-glycoprotein Calcium metabolism biology Cell Biology Calcium Channel Blockers Antineoplastic Agents Phytogenic Cell biology Calcein Calcium ATPase Verapamil chemistry Vincristine Cytoplasm Cell culture biology.protein Flunarizine |
| Zdroj: | Biochemical and Biophysical Research Communications. 335:777-784 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2005.07.144 |
| Popis: | L1210/VCR cell line (R) was obtained by adaptation of the L1210 mouse leukaemia cells (S) to vincristine and showed P-glycoprotein (P-gp) mediated multidrug resistance (MDR). R cells were observed to be more sensitive to high external calcium as parental S. More pronounced calcium uptake was observed for R cells. Moreover, differences in intracellular calcium cell localization between S and R cells were found ultrastructurally following a calcium precipitating cytochemical method. In S cells, calcium precipitates were found to be localized predominantly along the cell surface coat and within mitochondria delineating the cristae. In R cells, precipitates were also found inside nuclei, at the border of heterochromatin clumps, and scattered within the cytoplasm. High extracellular calcium did not influence the P-gp mediated extrusion of calcein/AM as P-gp substrate. These results indicate that calcium enters and consequently damages the MDR cells to a higher extent than parental cells. |
| Databáze: | OpenAIRE |
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