ReviewCytotechnology1993
Non-P-glycoprotein multidrug resistance in cell lines which are defective in the cellular accumulation of drug.
Review in Cytotechnology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Mechanisms regulating resistance to inhibitors of topoisomerase II.Frontiers in pharmacology · 2013Article
- Dinuclear platinum anticancer complexes with fluorescent N,N'-bis(aminoalkyl)-1,4-diaminoanthraquinones: cellular processing in two cisplatin-resistant cell lines reflects the differences in their resistance profiles.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2005Article
- Reversing effect of agosterol A, a spongean sterol acetate, on multidrug resistance in human carcinoma cells.Japanese journal of cancer research : Gann · 2001Article
- The multidrug resistance-associated protein gene confers drug resistance in human gastric and colon cancers.Japanese journal of cancer research : Gann · 1996Article
- Tissue distribution of the multidrug resistance protein.The American journal of pathology · 1996Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Non-Pgp mdr related to a defect in drug accumulation has now been documented in a number of different cell lines exposed to certain cytotoxic agents. In studies conducted thus far most isolates have been obtained after selection in either adriamycin or mitoxantrone. The work in this area is in its early stages and very little is known about the molecular events which contribute to this mode of drug resistance. At the present time no protein with drug binding properties comparable to Pgp has been identified in non-Pgp mdr isolates. Evidence based on the finding that all isolates do not respond in the same way to reversal agents such as verapamil suggests the possibility that more than one mechanism may exist for non-Pgp mdr. Future studies may thus reveal that cells contain a multiplicity of genes which upon transcriptional activation can function to alter drug transport processes and thus contribute to the development of mdr. Identifying and characterizing these genes will be important since they may function in transport systems of normal cells. The exact identify of proteins which contribute to non-Pgp mdr remains to be determined. One protein designated P190 has been found to be overexpressed in cell lines of human promyelocytic leukemia, lung and adenocarcinoma treated with adriamycin. The protein also is increased in some clinical samples from patients undergoing chemotherapy. P190 which has a minor sequence homology with Pgp can bind ATP and may thus contribute to the energy dependent drug efflux systems found in cells containing this protein. Transfection studies with a P190 cDNA should determine whether this protein actually contributes to drug resistance. Many other protein changes have been detected in non-Pgp mdr cells but the importance of these in resistance also remains to be determined. In some systems a particular protein change can be identified in multiple independent isolates suggesting a correlation between the development of resistance and the presence of this cellular alteration. Experiments conducted thus far on the mechanism of non-Pgp mdr are intriguing. Studies utilizing fluorescence microscopy to follow the fate of daunomycin suggests that the drug passes to the interior of the cell and eventually localizes in the Golgi apparatus. Drug located at this site may move directly into an efflux pathway for rapid extrusion from the cell. Evidence also indicates that as drug leaves the Golgi some may be sequestered into other organelles such as lysosomes or mitochondria.(ABSTRACT TRUNCATED AT 250 WORDS)
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.