Identification of the Interaction between P-Glycoprotein and Anxa2 in Multidrug-resistant Human Breast Cancer Cells.

Cancer Biol Med

Public Laboratory, Key Laboratory of Breast Cancer Prevention and Therapy, Tianjin Medical University, Ministry of Education, Tianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.

Published: June 2012

AI Article Synopsis

  • The study investigates how Anxa2 interacts with P-Glycoprotein (P-gp) in multidrug-resistant breast cancer cells (MCF-7/ADR) affecting their migration and invasion.
  • Researchers used short hairpin RNA (shRNA) to reduce P-gp levels, which resulted in significantly decreased ability of the cancer cells to migrate and invade.
  • The findings suggest that the connection between Anxa2 and P-gp is important for the aggressive nature of these MDR breast cancer cells.

Article Abstract

Objective: To explore the interaction of Anxa2 with P-Glycoprotein (P-gp) in the migration and invasion of the multidrug-resistant (MDR) human breast cancer cell line MCF-7/ADR.

Methods: A pair of short hairpin RNA (shRNA) targeting P-gp was transfected into MCF-7/ADR cells, and monoclonal cell strains were screened. The expression of P-gp was detected by Western blot. Transwell chambers were used to observe the cell migration capacity and invasion ability. The interaction between P-gp and Anxa2 was examined by immunoprecipitation and immunofluorescence confocal microscopy analyses.

Results: P-gp expression was significantly knocked down, and there were notable decreasing trends in the migration and invasion capability of MDR breast cancer cells (P<0.05). There was a close interaction between Anxa2 and P-gp.

Conclusions: MCF-7/ADR is an MDR human breast cancer cell line with high migration and invasion abilities. The knockdown of P-gp notably impaired the migration and invasion abilities of the tumor cells. The interaction of Anxa2 with P-pg may play an important role in the enhanced invasiveness of MDR human breast cancer cells.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3643660PMC
http://dx.doi.org/10.3969/j.issn.2095-3941.2012.02.003DOI Listing

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