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258 records – page 1 of 26.

2-substituted 1,2-dihydro-3H-dibenz[de,h]isoquinoline-1,3-diones. A new class of antitumor agent.

https://arctichealth.org/en/permalink/ahliterature24099
Source
J Med Chem. 1993 Mar 19;36(6):765-70
Publication Type
Article
Date
Mar-19-1993
Author
S M Sami
R T Dorr
D S Alberts
W A Remers
Author Affiliation
Department of Pharmaceutical Sciences and Cancer Center, University of Arizona, Tucson 85721.
Source
J Med Chem. 1993 Mar 19;36(6):765-70
Date
Mar-19-1993
Language
English
Publication Type
Article
Keywords
Animals
Antineoplastic Agents - chemical synthesis - chemistry - therapeutic use
Female
Humans
Isoquinolines - chemical synthesis - chemistry - therapeutic use
Leukemia L1210 - drug therapy
Leukemia P388 - drug therapy
Male
Melanoma, Experimental - drug therapy
Mice
Mice, Inbred DBA
Ovarian Neoplasms - drug therapy
Research Support, U.S. Gov't, P.H.S.
Structure-Activity Relationship
Tumor Cells, Cultured - drug effects
Abstract
A new class of antitumor agents, having structural analogy to amonafide, but differing by the addition of a fourth ring in the nucleus, was synthesized conveniently from anthracene. Compounds with a variety of substituents, containing a basic nitrogen atom and located on the imide nitrogen, were prepared. Thirteen of 19 new compounds had greater growth inhibitory potency than amonafide in a panel of cultured murine and human tumor cells using the sulforhodamine B and MTT dye assays. The most active agents were similarly more toxic than amonafide to normal neonatal rat myocytes in vitro, but they had better chemotherapeutic indexes. From these compounds, the one with a 2-(dimethylamino)ethyl side chain (named azonafide) was chosen for further study. It showed high potency against a panel of cultured human colon cancer cells and it was active against ip P388 leukemia and subcutaneous B16 melanoma in mice. Preliminary structure-activity correlations suggest that the basicity of the side-chain nitrogen and the length of side chain are important determinants of antitumor potency in vitro. Steric hindrance and rigidity of the side chains might be other determinants.
PubMed ID
8459403 View in PubMed
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6- and 7-substituted 2-[2'-(dimethylamino)ethyl]-1,2-dihydro-3H-dibenz[de,h] isoquinoline-1,3-diones: synthesis, nucleophilic displacements, antitumor activity, and quantitative structure-activity relationships.

https://arctichealth.org/en/permalink/ahliterature22674
Source
J Med Chem. 1996 Apr 12;39(8):1609-18
Publication Type
Article
Date
Apr-12-1996
Author
S M Sami
R T Dorr
A M Sòlyom
D S Alberts
B S Iyengar
W A Remers
Author Affiliation
Department of Pharmacology and Toxicology, University of Arizona, Tucson, 85721, USA.
Source
J Med Chem. 1996 Apr 12;39(8):1609-18
Date
Apr-12-1996
Language
English
Publication Type
Article
Keywords
Animals
Antineoplastic Agents - chemical synthesis - pharmacology
Humans
Isoquinolines - chemical synthesis
Male
Mice
Mice, Inbred DBA
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Structure-Activity Relationship
Tumor Cells, Cultured
Abstract
New 2-[2'-(dimethylamino)ethyl]-3H-dibenz[de,h]isoquinoline-1,3-diones with substituents at the 6- and 7-positions were prepared. Nucleophilic aromatic displacement was a key reaction in the syntheses. Ten of the new compounds were more potent than the unsubstituted compound, azonafide, in a panel of tumor cells including human melanoma and ovarian cancer and murine sensitive and MDR L1210 leukemia. They also were less cardiotoxic in cell culture. Four of these compounds were not cross-resistant with the MDR leukemia, and one of them, 6-ethoxyazonafide, was nearly as potent against solid tumor cells as leukemia cells. These compounds also had good potency against human breast, colon, and lung cancer cells, including doxorubicin and mitoxantrone resistant cell lines. Advantages of the new analogues over azonafide were less in vivo, but 6-ethoxyazonafide was more effective against L1210 leukemia and subcutaneous B16 melanoma in mice. Although correlations of antitumor potency in cells and physicochemical properties of substituents were not found, there were statistically significant correlations of DNA melt transition temperature (delta Tm) with potency in solid tumor cells and sensitive and MDR resistant L1210 leukemia cells for 6-substituted azonafides and with solid tumors for 7-substituted azonafides.
PubMed ID
8648600 View in PubMed
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17 beta-hydroxysteroid dehydrogenase gene expression in human breast cancer cells: regulation of expression by a progestin.

https://arctichealth.org/en/permalink/ahliterature24541
Source
Cancer Res. 1992 Jan 15;52(2):290-4
Publication Type
Article
Date
Jan-15-1992
Author
M. Poutanen
B. Moncharmont
R. Vihko
Author Affiliation
Department of Clinical Chemistry, University of Oulu, Finland.
Source
Cancer Res. 1992 Jan 15;52(2):290-4
Date
Jan-15-1992
Language
English
Publication Type
Article
Keywords
17-Hydroxysteroid Dehydrogenases - genetics - metabolism
Breast Neoplasms - enzymology - genetics
Gene Expression Regulation, Neoplastic - drug effects
Humans
Isoenzymes - genetics
Placenta - enzymology
Pregnenediones - pharmacology
Progesterone Congeners - pharmacology
RNA, Messenger - genetics
RNA, Neoplasm - genetics
Receptors, Estrogen - metabolism
Receptors, Progesterone - metabolism
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
The expression of the 17 beta-hydroxysteroid dehydrogenase (17-HSD) gene in a series of human breast cancer cell lines was studied by Northern blot hybridization with a cDNA probe and by a time-resolved immunofluorometric assay using polyclonal antibodies against the enzyme protein. The 17-HSD enzyme protein concentration was measured in the 800 x g cell extract. A high concentration was measured in the BT-20 cell line, corresponding to one-fourth of the average concentration in placental tissue. Western blot analysis indicated that the antigen corresponded to a single Mr 35,000 band. In 2 other cell lines (MDA-MB-361 and T-47D), the 17-HSD protein concentration was much lower, but still measurable, whereas in the remaining 5 cell lines (HBL-100, MCF-7, MDA-MB-231, MDA-MB-468, and ZR-75-1) it was below the detection limit of the assay. Treatment of the cells for 5 days with the synthetic progestin, ORG2058, resulted in an increase of the 17-HSD protein concentration only in the T-47D cell line. By Northern blot analysis, a low level of 2.3-kilobase mRNA transcripts was detected in all 8 cell lines. In addition, a 1.3-kilobase 17-HSD mRNA was present in the samples from the 3 cell lines containing measurable amounts of 17-HSD protein in the cell extract, and the band intensities were proportional to the amount of protein measured with the immunofluorometric assay. Only in the T-47D cell line did progestin treatment correspond to an increased amount of the 17-HSD 1.3-kilobase mRNA. These results suggest that the 1.3-kilobase mRNA for 17-HSD is the form most closely associated with protein expression and is also the only form responding to the progestin induction of the 17-HSD gene.
PubMed ID
1728403 View in PubMed
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17 beta-hydroxysteroid dehydrogenases and cancers.

https://arctichealth.org/en/permalink/ahliterature18539
Source
J Steroid Biochem Mol Biol. 2002 Dec;83(1-5):119-22
Publication Type
Article
Date
Dec-2002
Author
P. Vihko
P. Härkönen
O. Oduwole
S. Törn
R. Kurkela
K. Porvari
A. Pulkka
V. Isomaa
Author Affiliation
Biocenter Oulu and Research Center for Molecular Endocrinology, University of Oulu, P.O. Box 5000, FIN-90014 Oulu, Finland. pvihko@whoccr.oulu.fi
Source
J Steroid Biochem Mol Biol. 2002 Dec;83(1-5):119-22
Date
Dec-2002
Language
English
Publication Type
Article
Keywords
17-Hydroxysteroid Dehydrogenases - metabolism
Breast Neoplasms - enzymology
Cell Line
Colonic Neoplasms - enzymology - pathology
Disease Progression
Female
Humans
Male
Neoplasms - enzymology
Oxygen - metabolism
Prostatic Neoplasms - enzymology
Protein Isoforms
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
17 beta-Hydroxysteroid dehydrogenases (17HSDs) catalyze the interconversions between active 17 beta-hydroxysteroids and less-active 17-ketosteroids thereby affecting the availability of biologically active estrogens and androgens in a variety of tissues. The enzymes have different enzymatic properties and characteristic cell-specific expression patterns, suggesting differential physiological functions for the enzymes. Epidemiological and endocrine evidence indicate that estrogens play a key role in the etiology of breast cancer while androgens are involved in mechanisms controlling the growth of prostatic cells, both normal and malignant. Recently, we have developed, using LNCaP prostate cancer cell lines, a cell model to study the progression of prostate cancer. In the model LNCaP cells are transformed in culture condition to more aggressive cells, able to grow in suspension cultures. Our results suggest that substantial changes in androgen and estrogen metabolism occur in the cells during the process. These changes lead to increased production of active estrogens during transformation of the cells. Data from studies of breast cell lines and tissues suggest that the oxidative 17HSD type 2 may predominate in human non-malignant breast epithelial cells, while the reductive 17HSD type 1 activity prevails in malignant cells. Deprivation of an estrogen response by using specific 17HSD type 1 inhibitors is a tempting approach to treat estrogen-dependent breast cancer. Our recent studies demonstrate that in addition to sex hormone target tissues, estrogens may be important in the development of cancer in some other tissues previously not considered as estrogen target tissues such as colon. Our data show that the abundant expression of 17HSD type 2 present in normal colonic mucosa is significantly decreased during colon cancer development.
PubMed ID
12650708 View in PubMed
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Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH.

https://arctichealth.org/en/permalink/ahliterature19175
Source
FEBS Lett. 2002 Apr 10;516(1-3):217-24
Publication Type
Article
Date
Apr-10-2002
Author
Sakari Kellokumpu
Raija Sormunen
Ilmo Kellokumpu
Author Affiliation
Department of Biochemistry, University of Oulu, P.O. Box 3000, FIN-90014, Oulu, Finland. sakari.kellokumpu@oulu.fi
Source
FEBS Lett. 2002 Apr 10;516(1-3):217-24
Date
Apr-10-2002
Language
English
Publication Type
Article
Keywords
Animals
Antigens, Tumor-Associated, Carbohydrate - metabolism
Breast Neoplasms - immunology - metabolism - ultrastructure
COS Cells
Cells, Cultured
Colorectal Neoplasms - immunology - metabolism - ultrastructure
Female
Glycosylation
Golgi Apparatus - immunology - metabolism - ultrastructure
Humans
Hydrogen-Ion Concentration
Ion Transport
Microscopy, Electron
Rats
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
Abnormal glycosylation of cellular glycoconjugates is a common phenotypic change in many human tumors. Here, we explore the possibility that an altered Golgi pH may also be responsible for these cancer-associated glycosylation abnormalities. We show that a mere dissipation of the acidic Golgi pH results both in increased expression of some cancer-associated carbohydrate antigens and in structural disorganization of the Golgi apparatus in otherwise normally glycosylating cells. pH dependence of these alterations was confirmed by showing that an acidification-defective breast cancer cell line (MCF-7) also displayed a fragmented Golgi apparatus, whereas the Golgi apparatus was structurally normal in its acidification-competent subline (MCF-7/AdrR). Acidification competence was also found to rescue normal glycosylation potential in MCF-7/AdrR cells. Finally, we show that abnormal glycosylation is also accompanied by similar structural disorganization and fragmentation of the Golgi apparatus in colorectal cancer cells in vitro and in vivo. These results suggest that an inappropriate Golgi pH may indeed be responsible for the abnormal Golgi structure and lowered glycosylation potential of the Golgi apparatus in malignant cells.
PubMed ID
11959136 View in PubMed
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Acetyldinaline: a new oral cytostatic drug with impressive differential activity against leukemic cells and normal stem cells--preclinical studies in a relevant rat model for human acute myelocytic leukemia.

https://arctichealth.org/en/permalink/ahliterature23997
Source
Cancer Res. 1993 Jul 1;53(13):3008-14
Publication Type
Article
Date
Jul-1-1993
Author
H M el-Beltagi
A C Martens
P. Lelieveld
E A Haroun
A. Hagenbeek
Author Affiliation
Department of Hemato-Oncology TNO, Erasmus University Rotterdam, The Netherlands.
Source
Cancer Res. 1993 Jul 1;53(13):3008-14
Date
Jul-1-1993
Language
English
Publication Type
Article
Keywords
Administration, Oral
Animals
Antineoplastic Agents - pharmacology
Bone Marrow - drug effects
Bone Marrow Cells
Cell Differentiation - drug effects
Cell Survival - drug effects
Clone Cells
Comparative Study
Disease Models, Animal
Dose-Response Relationship, Drug
Drug Administration Schedule
Drug Evaluation
Drug Screening Assays, Antitumor
Hematopoietic Stem Cells - cytology - drug effects
Leukemia, Myelocytic, Acute - drug therapy - pathology
Male
Phenylenediamines - pharmacology
Rats
Rats, Inbred BN
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
Acetyldinaline [CI-994; GOE 5549; PD 123 654; 4-acetylamino-N-(2'-aminophenyl)-benzamide] is the acetylated derivative form of the original compound Dinaline (GOE 1734; PD 104 208). The efficacy and toxicity of Acetyldinaline for remission-induction treatment of leukemia were evaluated and compared with those observed in previous studies of Dinaline in the Brown Norway acute myelocytic leukemia, as a preclinical model for human acute myelocytic leukemia. There were three treatment groups. Leukemic animals received either 1 or 2 courses of 5 daily p.o. administrations of Acetyldinaline with a "full dose" of 23.7 mg/kg once daily (first group), a twice daily "half dose" of 11.85 mg/kg with an interval of 8 h (second group), or a "half dose" of 11.85 mg/kg once daily (third group). The drug-free interval between the 2 courses was 2 or 9 days. With repeated daily p.o. administrations of 23.7 mg/kg either in a single daily dose or a split daily dose of 2 x 11.85 mg/kg for 1 course, at least an 8-log leukemic cell kill was achieved. In contrast, with these treatment schedules, less than a 1-log cell kill of normal pluripotent hemopoietic stem cells (CFU-S) in the femoral bone marrow was found. Split daily dose treatment was more effective resulting in 37.5% cures, while no cures were observed with the single daily treatment for one course. Treatment with single daily dose of 23.7 mg/kg or a split daily dose of 2 x 11.85 mg/kg for 2 courses, with either a 2- or 9-day interval in between, resulted in lethal toxicity in most of rats. This result was comparable with that previously observed after equimolar doses of Dinaline (20 mg/kg). The half-dose once daily treatment with Acetyldinaline (11.85 mg/kg) for 1 or 2 cycles resulted in about a 4.5 or > 8-log leukemic cell kill, respectively. Toxic side effects, i.e., damage to the gastro-intestinal tract and hemorrhages in the lungs, were more pronounced with full dose either in the single or the split daily dose regimen. No significant toxicity was observed at the half-dose treatment once daily. In conclusion, the impressive differential activity against leukemic cells and normal stem cells observed in this relevant rat model for human acute myelocytic leukemia warrants the introduction of this compound in clinical phase I/II studies.
PubMed ID
8319208 View in PubMed
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Activation and relocalization of caspase 3 during the apoptotic cascade of human mesothelioma cells.

https://arctichealth.org/en/permalink/ahliterature16909
Source
APMIS. 2005 Jun;113(6):426-35
Publication Type
Article
Date
Jun-2005
Author
Y. Soini
K. Kahlos
R. Sormunen
M. Säily
P. Mäntymaa
P. Koistinen
P. Pääkkö
V. Kinnula
Author Affiliation
Department of Pathology, University of Oulu, Finland. msoini@cc.oulu.fi
Source
APMIS. 2005 Jun;113(6):426-35
Date
Jun-2005
Language
English
Publication Type
Article
Keywords
Antibiotics, Antineoplastic - pharmacology
Antigens, CD95 - genetics - metabolism
Apoptosis
Caspases - analysis - metabolism
Enzyme Activation
Epirubicin - pharmacology
Humans
Membrane Glycoproteins - genetics - metabolism
Mesothelioma - enzymology
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
Apoptosis plays an important role in cancer biology. We investigated the expression of caspases 3 and 8 in malignant mesothelioma and malignant mesothelioma cell lines and putative changes in their ultrastructural expression prior and after exposure to epirubicin. Further studies were conducted to compare these changes to the localization and expression of the bcl-2 group of proteins bcl-X, bax and mcl-1, and Fas-Fas ligand in the same cells. In the histological samples, caspase 3 and 8 immunoreactivity was seen in 27/37 (73%) and 16/37 (43%) of the mesotheliomas. The immunostaining was cytoplasmic diffuse, granular, and occasionally nuclear. All six mesothelioma cell lines expressed caspases 3 and 8 by immunoblotting. After exposure to epirubicin the extent of apoptosis was increased in all cell lines investigated, being weakest in the most resistant M38K cell line. Immunoelectron microscopy revealed immunogold labeling for caspases 3 and 8 in the mitochondria with the accumulation of caspase 3 in the apoptotic bodies, while the mitochondrial localization of the bcl-2 proteins appeared to be very stable. Fas receptor could be detected by flow cytometry, whereas the most resistant cell line (M38K) lacked Fas ligand when assessed by RT-PCR. These results suggest the importance of caspase 3 during the apoptotic process of mesothelioma cells and indicate that epirubicin-induced apoptosis is independent of the mitochondrial pathway.
PubMed ID
15996160 View in PubMed
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[Activity of proteolytic enzymes and their inhibitors during proliferation of P-815 mastocytoma cell proliferation in vitro]

https://arctichealth.org/en/permalink/ahliterature19357
Source
Vopr Onkol. 2001;47(5):619-22
Publication Type
Article
Date
2001
Author
O E Akbasheva
Iu P Bel'skii
N V Bel'skaia
T I Panova
Author Affiliation
Siberian Medical University, Tomsk.
Source
Vopr Onkol. 2001;47(5):619-22
Date
2001
Language
Russian
Publication Type
Article
Keywords
Animals
Cell Division - drug effects
Dactinomycin - pharmacology
English Abstract
Hydrolysis
Male
Mast-Cell Sarcoma - enzymology - metabolism - pathology
Mice
Mice, Inbred DBA
Tumor Cells, Cultured
alpha 1-Antitrypsin - metabolism
alpha-Macroglobulins - metabolism
Abstract
Proliferation of mastocytoma P-815 cells in vitro was accompanied by a rise in cathepsin D, elastase- and trypsin-like proteinase activity during 6 hours of culturing and a decline by hour 24. Yet alpha 1-proteinase inhibitor activity was inversely proportional to proteinase concentration. Antiproliferative action of actinomycin D disrupted phase variation of proteinase activity and, consequently, the level of alpha 1-proteinase inhibitor rose after 6 hours of cell culturing while that of alpha 2-macroglobulin--after 48 hr. Antiproliferative effect of actinomycin D was eliminated by reduced inhibitor level brought about under the influence of exogenous trypsin. When trypsin was added cathepsin D activity reached its peak 6 hr later while that of alpha 1-proteinase inhibitor declined. That effect and the actomycin D-proteinase inhibitor mechanism were retained when trypsin and actomycin D were present together. It is suggested that cathepsin D and alpha 1-proteinase inhibitor activity plays a key role in realizing the proliferative potential of mastocytoma P-815 cells.
PubMed ID
11785107 View in PubMed
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Acute myeloblastic leukaemia cells produce soluble interleukin 6 receptor by a mechanism of alternative splicing.

https://arctichealth.org/en/permalink/ahliterature21239
Source
Cytokine. 1998 Nov;10(11):860-7
Publication Type
Article
Date
Nov-1998
Author
M. Säily
P. Koistinen
K. Pulkki
A. Zheng
E R Savolainen
Author Affiliation
Department of Clinical Chemistry, University of Oulu, Finland.
Source
Cytokine. 1998 Nov;10(11):860-7
Date
Nov-1998
Language
English
Publication Type
Article
Keywords
Adolescent
Adult
Aged
Alternative Splicing
Female
Humans
Interleukin-6 - biosynthesis - genetics
Leukemia, Myelocytic, Acute - genetics - metabolism
Male
Middle Aged
RNA, Messenger - genetics
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured
Abstract
The aim of the present work was to investigate whether acute myeloblastic leukaemia (AML) blast cells express a soluble (s) form of interleukin 6 (IL-6) receptor (R), and if they do, what is the mechanism of production. Eight AML patient cell lines and 25 primary AML blast cell samples were investigated. The cell lines secreted high quantities of sIL-6R into their culture medium when examined by enzyme-linked immunosorbent assay (ELISA). To determine whether sIL-6R is synthesized by a mechanism of alternative splicing, RNA was analysed from all the AML blast cell samples by using reverse transcription polymerase chain reaction. In this method, primer sites flanking the transmembrane domain were utilized and the alternatively spliced IL-6R mRNA was distinguished from the non-spliced transcript form by size. All the cell lines and 64% of the primary blast cell samples expressed the alternatively spliced IL-6R mRNA. To confirm the phenomenon of alternative splicing at protein level, cytoplasmic protein fractions of the cell lines were investigated by using a sensitive adaptation of the Western blot method. All the cell lines expressed two IL-6R proteins sized 80 and 50 kDa and corresponding to the membraneous and soluble forms of IL-6R, respectively. In conclusion, the results obtained at both mRNA and protein levels strongly support alternative splicing as a mechanism of sIL-6R production in AML. Because sIL-6R modulates the effects of IL-6 on target cells, differences in sIL-6R expression levels may partially explain the previously observed diversity in IL-6-induced growth responses in AML
Notes
Comment In: Cytokine. 2000 Apr;12(4):42210805228
PubMed ID
10025979 View in PubMed
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Aldehyde dehydrogenase involvement in a variant of the brown Norway rat acute myelocytic leukaemia (BNML) that acquired cyclophosphamide resistance in vivo.

https://arctichealth.org/en/permalink/ahliterature23805
Source
Eur J Cancer. 1994;30A(14):2137-43
Publication Type
Article
Date
1994
Author
C J de Groot
A C Martens
A. Hagenbeek
Author Affiliation
Institute of Haematology, Eramus University Rotterdam, The Netherlands.
Source
Eur J Cancer. 1994;30A(14):2137-43
Date
1994
Language
English
Publication Type
Article
Keywords
Aldehyde Dehydrogenase - antagonists & inhibitors - metabolism
Animals
Antineoplastic Agents - therapeutic use
Cyclophosphamide - analogs & derivatives - therapeutic use
Disulfiram - pharmacology
Drug resistance
Leukemia, Myelocytic, Acute - drug therapy - enzymology - mortality
Male
Rats
Rats, Inbred BN
Research Support, Non-U.S. Gov't
Tumor Cells, Cultured - enzymology
Abstract
The development of drug resistance is an important factor contributing to failure of chemotherapy in cancer patients. Cyclophosphamide (CP) is a cytostatic drug widely used in the treatment of haematological malignancies and solid tumours. Because CP requires bioactivation to become cytotoxic, an in vivo approach was chosen to generate a subline of the Brown Norway rat acute myelocytic leukaemia (BNML/CPR) highly resistant to CP to serve as a model to investigate the molecular mechanism(s) of cyclophosphamide resistance. The role of the CP-detoxifying enzyme aldehyde dehydrogenase (ALDH) in the molecular mechanism of CP resistance in this subline of the BNML has been investigated. Compared to the parent BNML cell line, the BNML/CPR cell line displayed an approximately 6-fold higher level of ALDH enzyme activity. Pretreatment of leukaemic rats with the ALDH inhibitor disulfiram resulted in a restoration of CP sensitivity of animals carrying the BNML/CPR cells. Furthermore, in vitro incubation of BNML/CPR cells with disulfiram prior to incubation with the activated CP derivative mafosfamide resulted in an extra 2-3 log cell kill as indicated by the survival time of rats which were injected with disulfiram pretreated BNML/CPR cells compared to non-pretreated BNML/CPR cells. Data on the glutathione S-transferases (GSTs) isozyme profiles of cytoplasmic liver and spleen extracts of BNML- and BNML/CPR-carrying leukaemic rats indicated that the total GST enzyme amount was lower in BNML/CPR cells than in parent BNML cells. Furthermore, the BNML/CPR subline proved to be sensitive to phosphoramide mustard, both in vivo and in vitro.
PubMed ID
7857714 View in PubMed
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258 records – page 1 of 26.