Endocytic Recycling Compartments Altered in Cisplatin-Resistant Cancer Cells

Liang, Xing‐Jie; Mukherjee, Sushmita; Shen, Donglai; Maxfield, Frederick R.; Gottesman, Michael M.

doi:10.1158/0008-5472.can-05-3436

Cited by 55 publications

(46 citation statements)

References 45 publications

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“…In general, there was less intracellular transferrin in CP-r cells compared with CP-s cells ( 4). The difference in transferrin distribution between the CP-r and CP-s cells may result from defective endocytosis of the CP-r cells as demonstrated by our previous studies (32,35). Cisplatin passes through the plasma membrane and enters cells in part by endocytosis (36)(37)(38).…”

Section: Intracellular Cisplatin Accumulation By Reactivating the Defmentioning

confidence: 55%

“…Of these mechanisms, accumulation defect seems to be dominant in various cell lines (8,43). As mentioned above, CP-r cells have a defect in endocytosis (32), which may lead to diminished accumulation of cisplatin and confer the cells on resistance against extracellular cisplatin. The restored endocytosis of transferrin by [Gd@C 82 (OH) 22 ] n nanoparticles indicated that the nanoparticles can circumvent the acquired resistance of the CP-r PC-3-luc variants by enhancing uptake of cisplatin ( Fig.…”

Section: Intracellular Cisplatin Accumulation By Reactivating the Defmentioning

confidence: 98%

“…Nanoparticles have been used to deliver drugs or genes for cancer treatment using the unique characteristics associated with the nanoscale size (30,31). It is known that tumors become resistant to cisplatin, partially because of reduced uptake of cisplatin resulting from an endocytic defect following defective formation of the endocytic recycling compartment (ERC) (32). Although the specific molecular or regulatory defect responsible for the reduced accumulation of cisplatin in the CP-r cells has not been identified, several proteins have been found to be associated with this phenotype (33,34).…”

Section: Intracellular Cisplatin Accumulation By Reactivating the Defmentioning

confidence: 99%

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Metallofullerene nanoparticles circumvent tumor resistance to cisplatin by reactivating endocytosis

Lü

Meng

Wang

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Cisplatin is a chemotherapeutic drug commonly used in clinics. However, acquired resistance confines its application in chemotherapeutics. To overcome the acquired resistance to cisplatin, it is reasoned, based on our previous findings of mediation of cellular responses by [Gd@C 82 (OH) 22 ] n nanoparticles, that [Gd@C 82 (OH) 22 ] n may reverse tumor resistance to cisplatin by reactivating the impaired endocytosis of cisplatin-resistant human prostate cancer (CP-r) cells. Here we report that exposure of the CP-r PC-3-luc cells to cisplatin in the presence of nontoxic [Gd@C 82 (OH) 22 ] n not only decreased the number of surviving CP-r cells but also inhibited growth of the CP-r tumors in athymic nude mice as measured by both optical and MRI. Labeling the CP-r PC-3 cells with transferrin, an endocytotic marker, demonstrated that pretreatment of the CPr PC-3-luc cells with [Gd@C 82 (OH) 22 ] n enhanced intracellular accumulation of cisplatin and formation of cisplatin-DNA adducts by restoring the defective endocytosis of the CP-r cancer cells. The results suggest that [Gd@C 82 (OH) 22 ] n nanoparticles overcome tumor resistance to cisplatin by increasing its intracellular accumulation through the mechanism of restoring defective endocytosis. The technology can be extended to other challenges related to multidrug resistance often found in cancer treatments.A s a major chemotherapeutic agent for tumor treatment, cisplatin remains a cornerstone of the present-day chemotherapy regimens against not only epithelial malignancies but also a number of metastatic and advanced malignancies (1, 2). However, because of high toxicity and easy development of drug resistance, successful treatment with cisplatin often is limited (3,4). Following the discovery of ATP-binding cassette (ABC) transporters and their roles in drug resistance in various types of tumors (5), much research has been done to explore the relationship between ABC transporter activity and specific chemotherapeutics, including cisplatin. Because no ABC transporter has been identified for "pumping" cisplatin out of cisplatin-resistant human prostate cancer (CP-r) cells (6-8), it would be difficult to sensitize CP-r cells by using any known strategy that targets resistant cancer cells by inhibiting multidrug resistance (MDR)-associated proteins on plasma membrane of the CP-r cells. Diffusion has been considered as a pathway for cisplatin to penetrate plasma membrane. Recently, studies have indicated that cisplatin entered cells by endocytosis and other mechanisms (9-12).To increase susceptibility of cancer cells to cisplatin, i.e., to reverse drug resistance, many efforts have been made through chemical modification, gene therapy, vector delivery, and other means (2, 9, 13). Combination of traditional chemotherapy with nanotechnology may provide a promising alternative for novel cancer treatments. The use of nanoparticles to sensitize tumor cells to cisplatin in vitro and in vivo has been described recently (14-16). In these studies, cisplatin-encap...

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Section: Intracellular Cisplatin Accumulation By Reactivating the Defmentioning

confidence: 55%

Section: Intracellular Cisplatin Accumulation By Reactivating the Defmentioning

confidence: 98%

Section: Intracellular Cisplatin Accumulation By Reactivating the Defmentioning

confidence: 99%

See 1 more Smart Citation

Metallofullerene nanoparticles circumvent tumor resistance to cisplatin by reactivating endocytosis

Lü

Meng

Wang

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

232

160

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“…It is also possible that cDDP is directly internalized from the extracellular milieu into melanosomes via endocytosis or phagocytosis, thus bypassing a cytoplasm to nucleus route. Supporting this is data showing that platinum compounds can be internalized via phagocytosis and that cells with impaired endocytosis have decreased intracellular accumulation of cDDP (35,36). Melanosome sequestration may act as a resistance modulator for other compounds, in addition to cDDP, through other drug-specific mechanisms.…”

Section: Discussionmentioning

confidence: 87%

Multidrug Resistance Decreases with Mutations of Melanosomal Regulatory Genes

et al. 2009

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Whereas resistance to chemotherapy has long impeded effective treatment of metastatic melanoma, the mechanistic basis of this resistance remains unknown. One possible mechanism of drug resistance is alteration of intracellular drug distribution either by drug efflux or sequestration into intracellular organelles. Melanomas, as well as primary melanocytes from which they arise, have intracellular organelles, called melanosomes, wherein the synthesis and storage of the pigment melanin takes place. In this study, comparisons of congenic cells with and without functional molecules regulating melanosome formation show that sensitivity to the chemotherapeutic agent cis-diaminedichloroplatinum II (cis-platin) significantly increases with the mutation of genes regulating melanosome formation, concomitant disruption of melanosome morphology, and loss of mature melanosomes. Absence of the melanosomal structural protein gp100/Pmel17 causes increased cis-platin sensitivity. Independent mutations in three separate genes that regulate melanosome biogenesis (Dtnbp1, Pldn, Vps33a) also result in increased cis-platin sensitivity. In addition, a mutation of the gene encoding the integral melanosomal protein tyrosinase, resulting in aberrant melanosome formation, also causes increased cis-platin sensitivity. Furthermore, sensitivity to agents in other chemotherapeutic classes (e.g., vinblastine and etoposide) also increased with the mutation of Pldn. In contrast, a mutation in another melanosomal regulatory gene, Hps1, minimally affects melanosome biogenesis, preserves the formation of mature melanosomes, and has no effect on cis-platin or vinblastine response. Together, these data provide the first direct evidence that melanosomal regulatory genes influence drug sensitivity and that the presence of mature melanosomes likely contributes to melanoma resistance to therapy. [Cancer Res 2009;69(3):992-9]

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“…Lipids with long and saturated acyl chains, such as the synthetic fluorescent lipid analogue 1,1 ¶-dihexadecyl-3,3,3 ¶,3 ¶-tetramethylindocarbocyanine perchlorate (DiIC 16 ), preferentially partition into the ordered domains (20). In many studies, these and other lipid analogues have been used to observe the formation and dynamics of membrane domains in living cells (21,22).…”

Section: Introductionmentioning

confidence: 99%

The Inhibitory Effect of (−)-Epigallocatechin Gallate on Activation of the Epidermal Growth Factor Receptor Is Associated with Altered Lipid Order in HT29 Colon Cancer Cells

et al. 2007

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Abstract(À)-Epigallocatechin gallate (EGCG), a major biologically active constituent of green tea, inhibits activation of the epidermal growth factor (EGF) receptor (EGFR) and downstream signaling pathways in several types of human cancer cells, but the precise mechanism is not known. Because several plasma membrane-associated receptor tyrosine kinases (RTK) including EGFR are localized in detergent-insoluble ordered membrane domains, so-called ''lipid rafts,'' we examined whether the inhibitory effect of EGCG on activation of the EGFR is associated with changes in membrane lipid order in HT29 colon cancer cells. First, we did cold Triton X-100 solubility assays. Phosphorylated (activated) EGFR was found only in the Triton X-100-insoluble (lipid raft) fraction, whereas total cellular EGFR was present in the Triton X-100-soluble fraction. Pretreatment with EGCG inhibited the binding of Alexa Fluor 488-labeled EGF to the cells and also inhibited EGF-induced dimerization of the EGFR. To examine possible effects of EGCG on membrane lipid organization, we labeled the cells with the fluorescent lipid analogue 1, 1 ¶-dihexadecyl-3,3,3 ¶,3 ¶-tetramethylindocarbocyanine perchlorate, which preferentially incorporates into ordered membrane domains in cells and found that subsequent treatment with EGCG caused a marked reduction in the Triton X-100-resistant membrane fraction. Polyphenon E, a mixture of green tea catechins, had a similar effect but (À)-epicatechin (EC), the biologically inactive compound, did not significantly alter the Triton X-100 solubility properties of the membrane. Furthermore, we found that EGCG but not EC caused dramatic changes in the function of bilayer-incorporated gramicidin channels. Taken together, these findings suggest that EGCG inhibits the binding of EGF to the EGFR and the subsequent dimerization and activation of the EGFR by altering membrane organization. These effects may also explain the ability of EGCG to inhibit activation of other membrane-associated RTKs, and they may play a critical role in the anticancer effects of this and related compounds. [Cancer Res 2007; 67(13):6493-501]

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Endocytic Recycling Compartments Altered in Cisplatin-Resistant Cancer Cells

Cited by 55 publications

References 45 publications

Metallofullerene nanoparticles circumvent tumor resistance to cisplatin by reactivating endocytosis

Metallofullerene nanoparticles circumvent tumor resistance to cisplatin by reactivating endocytosis

Multidrug Resistance Decreases with Mutations of Melanosomal Regulatory Genes

The Inhibitory Effect of (−)-Epigallocatechin Gallate on Activation of the Epidermal Growth Factor Receptor Is Associated with Altered Lipid Order in HT29 Colon Cancer Cells

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