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Berlin Brandenburg

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  • Gottesman, Michael M
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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 01 December 1993, Vol.90(23), pp.11247-11251
    Description: We have cloned a human ATP-dependent protease that is highly homologous to members of the bacterial Lon protease family. The cloned gene encodes a protein of 963 amino acids with a calculated molecular mass of 106 kDa, slightly higher than that observed by Western blotting the protein from human tissues and cell lines (100 kDa). A single species of mRNA was found for this Lon protease in all human tissues examined. The protease is encoded in the nucleus, and the amino-terminal portion of the protein sequence contains a potential mitochondrial targeting presequence. Immunofluorescence microscopy suggested a predominantly mitochondrial localization for the Lon protease in cultured human cells. A truncated LON gene, in which translation was initiated at Met 118 of the coding sequence, was expressed in Escherichia coli and produced a protease that degraded α-casein in vitro in an ATP-dependent manner and had other properties similar to E. coli Lon protease.
    Keywords: Physical sciences -- Chemistry -- Chemical compounds -- KB cells ; Biological sciences -- Biology -- Cytology -- KB cells ; Physical sciences -- Chemistry -- Chemical compounds -- KB cells ; Biological sciences -- Biology -- Cytology -- KB cells ; Biological sciences -- Biology -- Cytology -- KB cells ; Physical sciences -- Chemistry -- Chemical compounds -- KB cells ; Biological sciences -- Biology -- Cytology -- KB cells ; Biological sciences -- Biology -- Cytology -- KB cells ; Biological sciences -- Biology -- Cytology -- KB cells ; Applied sciences -- Laboratory techniques -- Nucleic acid amplification techniques -- KB cells
    ISSN: 00278424
    E-ISSN: 10916490
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  • 2
    Language: English
    In: Drug Resistance Updates, February 2012, Vol.15(1-2), pp.62-69
    Description: Resistance to chemotherapy remains a challenging issue for patients and their physicians. P-glycoprotein (Pgp, MDR1, ABCB1), as well as a family of structurally and functionally related proteins, are plasma membrane transporters able to efflux a variety of substrates from the cell cytoplasm, including chemotherapeutic agents. The discovery of ABCB1 made available a potential target for pharmacologic down-regulation of efflux-mediated chemotherapy resistance. In patients with acute myeloid leukemia (AML), a neoplasm characterized by proliferation of poorly differentiated myeloid progenitor cells, leukemic cells often express ABCB1 at high levels, which may lead to the development of resistance to chemotherapy. Thus, AML seemed to be a likely cancer for which the addition of drug efflux inhibitors to the chemotherapeutic regimen would improve outcomes in patients. Despite this rational hypothesis, the majority of clinical trials evaluating this strategy have failed to reach a positive endpoint, most recently the Eastern Cooperative Oncology Group E3999 trial. Here we review data suggesting the importance of ABCB1 in AML, address the failure of clinical trials to support a therapeutic strategy aimed at modulating ABCB1-mediated resistance, and consider the type of research that should be conducted in this field going forward.
    Keywords: Acute Myeloid Leukemia ; Multidrug Resistance ; ABC Transporters ; Cancer Stem Cells ; Gene Signatures ; Biology
    ISSN: 1368-7646
    E-ISSN: 1532-2084
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  • 3
    Language: English
    In: Journal of Molecular Biology, 1974, Vol.88(2), pp.471,IN37,479-478,IN38,487
    Description: λ reverse (λ rev ) (Zissler et al ., 1971a) is a recombination proficient derivative of a A phage which had lost the phage recombination genes by deletion. In this work, phages with the Rev phenotype have been obtained by a method of selection different from that of Zissler et al . (1971a). Comparison of DNA from two of our isolates and one of Zissler's by electron microscopic heteroduplex mapping shows that all three phages carry substitutions of non-λ DNA which are indistinguishable in extent, location and base sequence. Genetic and biochemical characterization of λ rev strongly suggests that the substituted DNA codes for recombination functions different from the λ recombination functions which are deleted. These substituted genes apparently derive from the host chromosome or a prophage, and may be the same as the genes responsible for the SbcA and Rac phenotypes in the host.
    Keywords: Biology ; Chemistry
    ISSN: 0022-2836
    E-ISSN: 1089-8638
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  • 4
    In: Biochemistry, June 9, 1998, Vol.37(23), p.8584(11)
    Description: Research was conducted to determine the existence of an area within the primary sequence of the proenzyme form of cathepsin L that may affect its subcellular and extracellular localization. Results show that the secretion of alanine into the culture medium was blocked by substitutions of the amino acids S, P or V. It was therefore established that procathepsin L's carboxy terminus features a sequence that is required for its secretion.
    Keywords: Proteases -- Research ; Amino Acids -- Research
    ISSN: 0006-2960
    E-ISSN: 1943295X
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  • 5
    In: Nature Reviews Cancer, 2002, Vol.2(1), p.48
    Description: Multidrug resistance of cancer cells is a potentially surmountable obstacle to effective chemotherapy of cancer. ATP-binding cassette (ABC) transporters, including MDR1 (ABCB1), MRP1 (ABCC1) and ABCG2, can confer multidrug resistance to cancer cells in vitro. MRP2 (ABCC2), MRP3 (ABCC3), MRP4 (ABCC4), MRP5 (ABCC5), ABCA2 and BSEP (ABCB11) are capable of transporting drugs; future studies are needed to determine a role in drug resistance. ABC transporters such as MDR1 and MRP1 are expressed in many human cancers, including leukaemias and some solid tumours; in some studies, expression of these transporters has been shown to correlate with response to therapy and survival. Inhibitors of ABC transporters such as MDR1/P-glycoprotein have been tested in clinical trials with a suggestion of benefit, especially in acute myelogenous leukaemia. Interpretation of clinical trials using inhibitors of MDR1/P-glycoprotein has been confounded by their effects on the pharmacokinetics of anticancer drugs. Development of inhibitors of ABC transporters should focus on potency and specificity to minimize unexpected pharmacokinetic effects. Efficacy should be confirmed using surrogate assays. Normal tissues might be protected from toxicity by gene transfer of drug-resistance genes. Prevention of ABC transporter induction in cancer cells might help to avert drug resistance.
    Keywords: Multidrug Resistance ; Reviews ; Drug Development ; ABC Transporter ; Mpr1 Gene ; Mdr1 Gene ; Other Oncogenes ; ABC Transporter ; Mdr1 Gene ; Mpr1 Gene;
    ISSN: 1474-175X
    E-ISSN: 14741768
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  • 6
    Language: English
    In: Cancer Research, 07/01/2017, Vol.77(13 Supplement), pp.4040-4040
    ISSN: 0008-5472
    E-ISSN: 1538-7445
    Source: CrossRef
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  • 7
    Language: English
    In: Cancer Chemotherapy and Pharmacology, 2008, Vol.62(6), pp.977-984
    Description: Byline: Xing-Jie Liang (1,5), Jun-Jie Yin (2), Barbara Taylor (3), Stephen M. Winkovitch (4), Susan H. Garfield (4), Ding-Wu Shen (1), Michael M. Gottesman (1), Adorjan Aszalos (1) Keywords: Cisplatin; Electron spin resonance; Cytochalasin B; Carcinoma cell lines; Microfilaments Abstract: Background Although cisplatin is a frequently used cancer chemotherapeutic drug, its effectiveness is hindered by the development of resistance in cancer cells. In order to understand the reason(s) for this resistance, the mechanism of uptake of cisplatin into cells must be characterized. While several previous studies showed structural differences between cisplatin-sensitive and resistant cells, the influence of microfilaments, known to affect transport of molecules into cells, and the influence of certain biophysical characteristics of the plasma membrane needed clarification. Results We show that resistant human epidermal carcinoma (KB-CP20) and liver carcinoma (BEL-7404-CP20) cells become relatively more resistant if their already weak microfilaments are degraded by cytochalasin B treatment (.5--2 uM). The sensitive counterparts of these cells with intact microfilaments are not significantly affected by this treatment. We also show that the "fluidity" of the plasma membrane and the membrane potential of the sensitive and resistant cells studied do not appear to influence the uptake of cisplatin into the cells. Conclusion Our results suggest that the status of the microfilament system influences the mechanism of uptake of cisplatin into cells. Author Affiliation: (1) Laboratory of Cell Biology, National Cancer Institute, NIH, Bethesda, MD, 20892, USA (2) Instrumentation and Biophysics Branch, Center for Food Safety and Applied Nutrition, Food and Drug Administration, College Park, MD, 20740, USA (3) Laboratory of Cancer Biology and Genetics, NIH, Bethesda, MD, 20892, USA (4) Laboratory of Experimental Carcinogenesis, NIH, Bethesda, MD, 20892, USA (5) Division of Nanomedicine and Nanobiology, National Center of Nanoscience and Technology, Zhongguancun, 100080, Beijing, China Article History: Registration Date: 19/01/2008 Received Date: 31/07/2007 Accepted Date: 18/01/2008 Online Date: 15/02/2008
    Keywords: Cisplatin ; Electron spin resonance ; Cytochalasin B ; Carcinoma cell lines ; Microfilaments
    ISSN: 0344-5704
    E-ISSN: 1432-0843
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  • 8
  • 9
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 27 June 2006, Vol.103(26), pp.9903-7
    Description: Multidrug resistance mechanisms underlying the intractability of malignant melanomas remain largely unknown. In this study, we demonstrate that the development of multidrug resistance in melanomas involves subcellular sequestration of intracellular cytotoxic drugs such as cis-diaminedichloroplatinum II (cisplatin; CDDP). CDDP is initially sequestered in subcellular organelles such as melanosomes, which significantly reduces its nuclear localization when compared with nonmelanoma/KB-3-1 epidermoid carcinoma cells. The melanosomal accumulation of CDDP remarkably modulates melanogenesis through a pronounced increase in tyrosinase activity. The altered melanogenesis manifested an approximately 8-fold increase in both intracellular pigmentation and extracellular transport of melanosomes containing CDDP. Thus, our experiments provide evidence that melanosomes contribute to the refractory properties of melanoma cells by sequestering cytotoxic drugs and increasing melanosome-mediated drug export. Preventing melanosomal sequestration of cytotoxic drugs by inhibiting the functions of melanosomes may have great potential as an approach to improving the chemosensitivity of melanoma cells.
    Keywords: Drug Resistance, Multiple ; Drug Resistance, Neoplasm ; Antineoplastic Agents -- Metabolism ; Cisplatin -- Metabolism ; Melanoma -- Metabolism ; Melanosomes -- Enzymology ; Skin Neoplasms -- Metabolism
    ISSN: 0027-8424
    E-ISSN: 10916490
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  • 10
    Language: English
    In: Cancer research, 15 September 2003, Vol.63(18), pp.5909-16
    Description: The accumulation of [(14)C]carboplatin and [(3)H]methotrexate is reduced in single-step KB epidermoid adenocarcinoma (KB-CP) cells, which are cross-resistant to carboplatin, methotrexate, and sodium arsenite. In these KB-CP cells, multidrug resistance is accompanied by mislocalization of multidrug resistance associated protein (MRP) 1 and other membrane proteins such as folate-binding protein. MRP1 was not decreased in amount in single-step variants but accumulates in a cytoplasmic fraction, and its apparent molecular weight was altered probably because of reduced glycosylation in resistant cells. This low-density compartment was partially labeled with antibodies to lectin-GSII (a Golgi marker) and Bip/GRP78 (an endoplasmic reticulum marker). Pulse-chase labeling of MRP1 with (35)S-methionine and (35)S-cysteine and pulse-chase biotinylation of cell surface MRP1 suggests that membrane protein mislocalization is caused mainly by a defect of plasma membrane protein recycling, manifested also as a defect in acidification of lysosomes. The reduced accumulation of cytotoxic compounds in the KB-CP cells is presumed to result from the failure of carrier proteins and/or transporters to localize to the plasma membrane.
    Keywords: Receptors, Cell Surface ; ATP Binding Cassette Transporter, Subfamily B, Member 1 -- Metabolism ; Antineoplastic Agents -- Pharmacology ; Biotin -- Analogs & Derivatives ; Carrier Proteins -- Metabolism ; Cisplatin -- Pharmacology ; Drug Resistance, Multiple -- Physiology
    ISSN: 0008-5472
    E-ISSN: 15387445
    Source: MEDLINE/PubMed (U.S. National Library of Medicine)
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