Abstract
The response to chemotherapy by tumor cells depends on the concentration of cytostatics accumulated inside the cells. The accumulation of anticancer drugs in tumor cells is mainly dependent on functional expression of efflux and influx transporters and to a minor extent on passive diffusion through the membrane. Efflux transporters of the ABC family are partially responsible for the chemoresistance of cancer cells by secreting these cytostatics. Over the past decades, the role of ABC transporters in the chemoresistance of various malignant tumors has been very well documented. By contrast, very little is known about the impact on tumor therapy of influx transporters belonging to the solute carrier transporters (SLC family). In this review, we focus on the interaction of SLC22 transporters with cytostatics, the expression of these transporters in tumor cells as well as their impact on the chemosensitivity of cancer cells.
©2011 by Walter de Gruyter Berlin New York
Artikel in diesem Heft
- Publisher’s Note
- Publisher’s Note
- Guest Editorial
- Highlight: Membrane transport in light of structure, function, and evolution
- HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
- Pathways of transport protein evolution: recent advances
- Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
- Omp85 in eukaryotic systems: one protein family with distinct functions
- Evolution of ABC transporters by gene duplication and their role in human disease
- A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
- The multidrug transporter Pdr5: a molecular diode?
- The lysosomal polypeptide transporter TAPL: more than a housekeeping factor?
- Pumping lipids with P4-ATPases
- Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery
- Substrate recognition and translocation by polyspecific organic cation transporters
- The ugly side of amphetamines: short- and long-term toxicity of 3,4-methylenedioxymethamphetamine (MDMA, ‘Ecstasy’), methamphetamine and d-amphetamine
- SLC22 transporter family proteins as targets for cytostatic uptake into tumor cells
- Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
- Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
- Structure determination of channel and transport proteins by high-resolution microscopy techniques
Artikel in diesem Heft
- Publisher’s Note
- Publisher’s Note
- Guest Editorial
- Highlight: Membrane transport in light of structure, function, and evolution
- HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
- Pathways of transport protein evolution: recent advances
- Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
- Omp85 in eukaryotic systems: one protein family with distinct functions
- Evolution of ABC transporters by gene duplication and their role in human disease
- A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
- The multidrug transporter Pdr5: a molecular diode?
- The lysosomal polypeptide transporter TAPL: more than a housekeeping factor?
- Pumping lipids with P4-ATPases
- Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery
- Substrate recognition and translocation by polyspecific organic cation transporters
- The ugly side of amphetamines: short- and long-term toxicity of 3,4-methylenedioxymethamphetamine (MDMA, ‘Ecstasy’), methamphetamine and d-amphetamine
- SLC22 transporter family proteins as targets for cytostatic uptake into tumor cells
- Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
- Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
- Structure determination of channel and transport proteins by high-resolution microscopy techniques