Related Experiment Video

Updated: Aug 8, 2026

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
10:43

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Published on: December 3, 2010

Golgi complex is brefeldin A resistant in multidrug resistant cells

M V Erokhina1, A A Stavrovskaya, G E Onishchenko

  • 1Institute of Carcinogenesis, Blokhin Cancer Research Center, Russian Academy of Medical Sciences, Moscow. rak@sunny.aha.ru

Membrane & Cell Biology
|October 8, 1999
PubMed

Insights

Multidrug resistance (MDR) in cancer involves P-glycoprotein (Pgp). Brefeldin A (BFA) reveals distinct vacuolar system responses in Pgp-expressing cells, impacting cancer chemotherapy effectiveness.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Multidrug resistance (MDR) is a major cause of chemotherapy failure in cancer.
  • Overexpression of P-glycoprotein (Pgp) confers MDR by enabling resistant tumor cells.
  • Previous work showed Pgp-mediated MDR involves cytoskeleton and vacuolar system reorganization.

Purpose of the Study:

  • To investigate vacuolar system properties in Pgp-expressing cells.
  • To understand the effects of Brefeldin A (BFA) on parental and resistant cells.
  • To explore the role of BFA targets in the evolution of MDR.

Main Methods:

  • Utilized Syrian hamster embryo fibroblasts transformed by Raus sarcoma virus.
  • Compared the effects of Brefeldin A (BFA) on parental and Pgp-expressing resistant sublines.
  • Assessed BFA's impact on Golgi apparatus structure and vesicular transport.

Main Results:

  • Brefeldin A (BFA) differentially affects parental and resistant cells.
  • In parental cells, BFA impacts both Golgi apparatus structure and vesicular transport.
  • In resistant cells, BFA affects vesicular transport but not Golgi apparatus structure.

Conclusions:

  • Vacuolar system responses to BFA differ between parental and Pgp-expressing cells.
  • These differences suggest distinct BFA targets contributing to MDR evolution.
  • Understanding these mechanisms may offer new avenues for overcoming chemotherapy resistance.

More Related Videos

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

Small-Scale Plasma Membrane Preparation for the Analysis of Candida albicans Cdr1-mGFPHis09:44

Small-Scale Plasma Membrane Preparation for the Analysis of Candida albicans Cdr1-mGFPHis

Published on: June 13, 2021

Related Concept Videos

Golgi Apparatus01:49

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Transport Across the Golgi01:26

Transport Across the Golgi

While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...