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Age-specific evaluation of primary human papillomavirus screening vs conventional cytology in a randomized setting.

https://arctichealth.org/en/permalink/ahliterature147457
Source
J Natl Cancer Inst. 2009 Dec 2;101(23):1612-23
Publication Type
Article
Date
Dec-2-2009
Author
Maarit Leinonen
Pekka Nieminen
Laura Kotaniemi-Talonen
Nea Malila
Jussi Tarkkanen
Pekka Laurila
Ahti Anttila
Author Affiliation
Mass Screening Registry, Finnish Cancer Registry, Pieni Roobertinkatu 9, FI-00130 Helsinki, Finland. maarit.leinonen@cancer.fi
Source
J Natl Cancer Inst. 2009 Dec 2;101(23):1612-23
Date
Dec-2-2009
Language
English
Publication Type
Article
Keywords
Adult
Age Factors
Aged
Aging
Alphapapillomavirus - genetics - isolation & purification
Cell Transformation, Neoplastic
Cell Transformation, Viral
Cervical Intraepithelial Neoplasia - diagnosis - prevention & control - virology
Colposcopy
Confounding Factors (Epidemiology)
DNA, Viral - isolation & purification
Early Detection of Cancer
Female
Finland
Humans
Mass Screening - methods
Middle Aged
Odds Ratio
Papillomavirus Infections - complications - diagnosis - virology
Population Surveillance
Predictive value of tests
Referral and Consultation
Reproducibility of Results
Risk assessment
Risk factors
Sensitivity and specificity
Triage
Tumor Virus Infections - complications - diagnosis - virology
Uterine Cervical Neoplasms - diagnosis - prevention & control - virology
Vaginal Smears - methods
Abstract
Human papillomavirus (HPV) DNA testing has shown higher sensitivity than cytology for detecting cervical lesions, but it is uncertain whether the higher sensitivity is dependent on the age of the woman being screened. We compared the age-specific performance of primary HPV DNA screening with that of conventional cytology screening in the setting of an organized population-based cervical cancer screening program in Finland.
From January 1, 2003, to December 31, 2005, randomized invitations were sent to women aged 25-65 years for routine cervical cancer screening by primary high-risk HPV DNA testing (n = 54 207) with a Hybrid Capture 2 assay followed by cytology triage for women who were HPV DNA positive or by conventional cytology screening (n = 54 218). In both screening arms, cytology results of low-grade squamous intraepithelial lesion or worse triggered a referral for colposcopy. Relative rates (RRs) of detection to assess test sensitivity, specificity, and positive predictive values (PPVs) with 95% confidence intervals (CIs) were calculated for the histological endpoints of cervical intraepithelial neoplasia (CIN) grade 1 or higher (CIN 1+), CIN grade 2 or higher (CIN 2+), and CIN grade 3 or higher (CIN 3+). All statistical tests were two-sided.
The overall frequency of colposcopy referrals was 1.2% in both screening arms. Women younger than 35 years were referred more often in the HPV DNA screening vs the conventional screening arm (RR = 1.27, 95% CI = 1.01 to 1.60). The prevalence of histologically confirmed CIN or cancer was 0.59% in the HPV DNA screening arm vs 0.43% in the conventional screening arm. The relative rates of detection for CIN 1, CIN 2, and CIN 3+ for HPV DNA screening with cytology triage vs conventional screening were 1.44 (95% CI = 0.99 to 2.10), 1.39 (95% CI = 1.03 to 1.88), and 1.22 (95% CI = 0.78 to 1.92), respectively. The specificity of the HPV DNA test with cytology triage was equal to that of conventional screening for all age groups (99.2% vs 99.1% for CIN 2+, P = .13). Among women aged 35 years or older, the HPV DNA test with cytology triage tended to have higher specificity than conventional screening. The PPVs for HPV DNA screening with cytology triage were consistently higher than those for conventional screening. In both screening arms, the test specificities increased with increasing age of the women being screening, whereas the highest PPVs were observed among the youngest women being screened. Overall, 7.2% of women in the HPV DNA screening arm vs 6.6% of women in the conventional screening arm were recommended for intensified follow-up, and the percentages were highest among 25- to 29-year-olds (21.9% vs 10.0%, respectively).
Primary HPV DNA screening with cytology triage is more sensitive than conventional screening. Among women aged 35 years or older, primary HPV DNA screening with cytology triage is also more specific than conventional screening and decreases colposcopy referrals and follow-up tests.
Notes
Comment In: J Natl Cancer Inst. 2012 Feb 8;104(3):166-722271766
Comment In: J Natl Cancer Inst. 2010 May 19;102(10):739; author reply 739-4020360534
Comment In: J Natl Cancer Inst. 2009 Dec 2;101(23):1600-119903806
PubMed ID
19903804 View in PubMed
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Association of topoisomerases I and II with the chromatin in SV40-infected monkey cells.

https://arctichealth.org/en/permalink/ahliterature4138
Source
Virology. 1991 Mar;181(1):408-11
Publication Type
Article
Date
Mar-1991
Author
R. Rainwater
K. Mann
Author Affiliation
Biology Department, University of Alaska, Anchorage 99508.
Source
Virology. 1991 Mar;181(1):408-11
Date
Mar-1991
Language
English
Publication Type
Article
Keywords
Animals
Cell Line
Cell Transformation, Viral
Cercopithecus aethiops
Chromatin - enzymology
DNA Topoisomerases, Type I - isolation & purification - metabolism
DNA Topoisomerases, Type II - isolation & purification - metabolism
Electrophoresis, Polyacrylamide Gel
Immunoblotting
Molecular Weight
Research Support, U.S. Gov't, P.H.S.
Simian virus 40 - enzymology
Subcellular Fractions - enzymology
Abstract
The subcellular localization of topoisomerase I and topoisomerase II has been compared in Simian virus (SV40)-infected and uninfected TC7 monkey cells. In SV40-infected cells, both of these enzymes are preferentially associated with the chromatin. Some topoisomerase I is associated with the nuclear matrix, whereas topoisomerase II shows no such association. In uninfected TC7 cells, topoisomerase I is present in both the chromatin and nuclear matrix fractions. Topoisomerase II, on the other hand, is not detected in any of the subcellular fractions of uninfected cells. After SV40 infection, there is a marked increase in the level of chromatin-associated topoisomerase II.
PubMed ID
1847264 View in PubMed
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Source
Int J Cancer. 1997 Jan 6;70(1):1-8
Publication Type
Article
Date
Jan-6-1997
Author
J. Avila-Cariño
N. Lewin
Y. Tomita
A. Szeles
A. Sandlund
S. Mosolits
H. Mellstedt
G. Klein
E. Klein
Author Affiliation
Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden. Javier.Avila-Carino@mtc.ki.se
Source
Int J Cancer. 1997 Jan 6;70(1):1-8
Date
Jan-6-1997
Language
English
Publication Type
Article
Keywords
Aged
Antigens, CD - metabolism
Cell Survival
Cell Transformation, Viral - physiology
Chromosomes, Human, Pair 18 - genetics
Chromosomes, Human, Pair 22 - genetics
Herpesvirus 4, Human - classification - immunology
Humans
Immunophenotyping
Leukemia, Lymphocytic, Chronic, B-Cell - genetics - immunology - pathology - virology
Male
Phenotype
T-Lymphocytes - immunology
T-Lymphocytes, Cytotoxic - immunology
Translocation, Genetic
Tumor Cells, Cultured
Tumor Markers, Biological - metabolism
Tumor Virus Infections - immunology
Viral Proteins - analysis
Abstract
In studies concerning the interaction of B-CLL cells and Epstein-Barr virus (EBV), we encountered one patient whose cells had several unusual properties. In addition to the B-cell markers, the CLL cells expressed the exclusive T-cell markers CD3 and CD8 and carried a translocation t(18,22)(q21;q11), involving the bcl-2 and Ig lambda loci. The patient represents the 4th reported CLL case with this translocation. The CLL cells could be infected and immortalized by the indigenous and by the prototype B958 virus in vitro. The T-cell markers were not detectable on the established lines. In all experiments the immortalized lines originated from the CLL cells. Their preferential emergence over virus-infected normal B cells may be coupled to the high expression of the bcl-2 gene due to the translocation. In spite of the sensitivity of CLL cells to EBV infection in vitro, no EBNA-positive cells were detected in the ex vivo population. In vitro, we could generate cytotoxic function in T-lymphocyte cultures which acted on autologous EBV-infected CLL cells. Therefore we assume that if such cells emerged in vivo they were eliminated by the T-cell response.
PubMed ID
8985083 View in PubMed
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Differential expression of cellular genes in Rauscher leukaemia.

https://arctichealth.org/en/permalink/ahliterature26226
Source
Folia Biol (Praha). 1987;33(6):369-76
Publication Type
Article
Date
1987
Author
I A Smirnova
A G Tatosyan
S D Sherban
Z A Butenko
Author Affiliation
R.E. Kavetsky Institute for Oncology Problems, Ukrainian SSR Academy of Sciences.
Source
Folia Biol (Praha). 1987;33(6):369-76
Date
1987
Language
English
Publication Type
Article
Keywords
Animals
Cell Transformation, Viral
DNA - genetics
DNA, Neoplasm - analysis
Gene Expression Regulation
Leukemia, Experimental - genetics
Mice
Mice, Inbred BALB C - genetics
Nucleic Acid Hybridization
RNA, Heterogeneous Nuclear - analysis
RNA, Neoplasm - analysis
RNA, Viral - analysis
Rauscher Virus - physiology
Sequence Homology, Nucleic Acid
Spleen - pathology
Abstract
The methods of hybridization in solution and blot hybridization showed that spleen cells from BALB/c mice contain "silent" genes which can amplify and change their structure after infection by Rauscher leukaemia virus. The "silent" gene product is nuclear 35S RNA detectable by comparative electrophoretic analysis of the heterogeneous nuclear RNA from leukaemic and normal cells. About 7% of this 35S RNA is represented by the virus-specific sequences, but a major part is represented by the cellular sequences. In order to study the expression of the sequences homologous to 35S RNA in leukaemic and normal cells, hybridization in solution was used. Expression of the complete copies of 35S RNA was observed in nuclei of virus-infected cells, whereas this RNA in the cytoplasm is represented by the incomplete copies. The expression of the sequences homologous to this 35S RNA in normal mouse spleen cells was not revealed.
PubMed ID
3436464 View in PubMed
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Differential increase in topoisomerase II in simian virus 40-infected cells.

https://arctichealth.org/en/permalink/ahliterature4154
Source
J Virol. 1990 Feb;64(2):918-21
Publication Type
Article
Date
Feb-1990
Author
R. Rainwater
K. Mann
Author Affiliation
Biology Department, University of Alaska, Anchorage 99508.
Source
J Virol. 1990 Feb;64(2):918-21
Date
Feb-1990
Language
English
Publication Type
Article
Keywords
Animals
Antigens, Polyomavirus Transforming - genetics
Cell Line
Cell Transformation, Viral
DNA Replication
DNA Topoisomerases, Type I - biosynthesis
DNA Topoisomerases, Type II - biosynthesis
DNA, Viral - biosynthesis
Kinetics
Research Support, U.S. Gov't, P.H.S.
Simian virus 40 - enzymology - genetics - immunology
Abstract
The time course of expression of topoisomerase I, topoisomerase II, and simian virus 40 (SV40) large tumor (T) antigen was determined in whole-cell extracts of uninfected versus SV40-infected TC7 cells. After a minor increase, the level of topoisomerase I remained fairly constant throughout the time course in both uninfected and SV40-infected cells. In contrast, the level of topoisomerase II increased markedly in SV40-infected cells but not in uninfected cells following the appearance of SV40 T antigen.
PubMed ID
2153253 View in PubMed
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[Effect of isonicotinic acid derivates on reproduction of Epstein-Barr virus].

https://arctichealth.org/en/permalink/ahliterature101694
Source
Mikrobiol Z. 2011 Mar-Apr;73(2):65-72
Publication Type
Article
Author
S D Zahorodnia
N V Nesterova
V P Danylenko
T A Bukhtiarova
H V Baranova
A V Holovan'
Source
Mikrobiol Z. 2011 Mar-Apr;73(2):65-72
Language
Ukrainian
Publication Type
Article
Keywords
Animals
Antiviral Agents - chemistry - pharmacology
Callithrix
Cell Line, Tumor
Cell Survival - drug effects
Cell Transformation, Viral
Dose-Response Relationship, Drug
Herpesvirus 4, Human - drug effects - physiology
Humans
Isonicotinic Acids - chemistry - pharmacology
Lymphocytes - virology
Molecular Structure
Structure-Activity Relationship
Virus Replication - drug effects
Abstract
Current approaches to the treatment of herpes infection, particularly Epstein-Barr virus (EBV), include the use of etiotropic medicines, as well as sensitizing therapy. This virus plays an important role in the etiology of nasopharyngeal carcinoma, adenocarcinoma of the parotid glands, gastric carcinoma, Burkitt's lymphoma and lymphoproliferative syndromes [1, 2, 3]. The spectrum of drugs active against EBV remains very limited, and gancyclovir and acyclovir are used in medical practice, so the search of new compounds active against EBV remains urgent. The purpose of this work was to study antiEBV activity of isonicotinic acid derivatives in the cultures of lymphoblastoid Raji cells, B95-8, Namalwa. The indices of cytotoxicity (CC50) which amounted to 840, 1250 and 3000 microg/ml and the concentration of drugs, which inhibit the virus (IC50) reproduction is 0.1, 2.5 and 50 microg/ml, respectively, in cell cultures were identified. It was detected, the drug 4-(n-benzyl)aminocarbonyl-1-methylpyridinium iodide (PV-1) had an ability to inhibit reproduction of the Epstein-Barr virus in all studied cells cultures. The compounds PV-2 and PV-10 were less toxic in respect of the initial preparation PV-1, but their antiviral activity was manifested at 25 and 500 times higher concentrations. It, respectively, influenced the decrease of their selectivity index, which was 8400 for PV-1, 400 and 440--for PV-2 and PV-10. These studies suggest possible ways of further modification of the PV-1 molecule to create highly specific inhibitors of Epstein-Barr virus. The paper is presented in Ukrainian.
PubMed ID
21598662 View in PubMed
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Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer.

https://arctichealth.org/en/permalink/ahliterature187745
Source
Biochem J. 2003 Feb 15;370(Pt 1):275-82
Publication Type
Article
Date
Feb-15-2003
Author
Mary Anna Carbone
Brian H Robinson
Author Affiliation
Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto, ON, Canada M5G 1X8.
Source
Biochem J. 2003 Feb 15;370(Pt 1):275-82
Date
Feb-15-2003
Language
English
Publication Type
Article
Keywords
Amino Acid Sequence
Base Sequence
Blotting, Western
Cell Line, Transformed
Cell Transformation, Viral
DNA Primers
Electrophoresis, Polyacrylamide Gel
Gene Transfer Techniques
Humans
Kinetics
Mitochondria - enzymology
Molecular Sequence Data
Protein Structure, Secondary
Pyruvate Carboxylase - chemistry - genetics - metabolism
Retroviridae - genetics
Reverse Transcriptase Polymerase Chain Reaction
Abstract
Type A pyruvate carboxylase (PC) deficiency presents mainly in the Amerindian population, specifically the Ojibwa, Cree and Micmac tribes of the Algonquin-speaking peoples. The gene for PC contains a homozygous founder mutation (G1828-->A) that results in an Ala610-->Thr amino acid substitution in Ojibwa with Type A PC deficiency. The mutation is located in the highly conserved pyruvate-binding domain of PC. The present paper describes a retroviral expression system for human PC used to analyse the effects of this mutation. We show, through immunoblot analysis, PC enzyme activity assays, reverse-transcription PCR and mitochondrial-import experiments, that this mutation is disease-causing in the Ojibwa population owing to its decreased catalytic activity, decreased steady-state levels of expression and inefficient import into the mitochondria. Our data suggest that this mutation may affect the stability of the protein, resulting in decreased steady-state levels of expression, and that it may also affect the secondary structure of the protein during the import process, thereby inhibiting proper translocation into the mitochondria, where PC is active.
Notes
Cites: Am J Hum Genet. 1987 Jan;40(1):50-93101494
Cites: J Biol Chem. 1963 Aug;238:2609-1414063280
Cites: Arch Biochem Biophys. 1991 Jan;284(1):98-1051989506
Cites: Pediatr Res. 1991 Jul;30(1):1-41909777
Cites: Biochem Biophys Res Commun. 1999 Dec 20;266(2):512-710600533
Cites: Acta Physiol Scand. 2000 Apr;168(4):657-6510759602
Cites: Semin Cell Dev Biol. 2000 Jun;11(3):141-810906270
Cites: Biochem Soc Trans. 2001 Aug;29(Pt 4):431-611498003
Cites: Clin Pediatr (Phila). 2001 Sep;40(9):519-2111583052
Cites: Arch Biochem Biophys. 2002 May 1;401(1):63-7212054488
Cites: Hum Mutat. 2002 Jul;20(1):48-5612112657
Cites: J Biol Chem. 1967 May 10;242(9):1983-76022848
Cites: Biochem J. 1972 Nov;130(2):391-64354325
Cites: J Biol Chem. 1979 Jan 25;254(2):420-30762069
Cites: J Biol Chem. 1983 May 25;258(10):6660-46406485
Cites: Am J Hum Genet. 1984 Mar;36(2):283-946424438
Cites: Prenat Diagn. 1985 Jan-Feb;5(1):67-713919380
Cites: Brain Res. 1985 Mar 11;329(1-2):364-73884090
Cites: Am J Physiol. 1993 Feb;264(2 Pt 1):C383-98383431
Cites: Biochem J. 1993 Mar 1;290 ( Pt 2):583-908452549
Cites: Am J Physiol. 1994 Aug;267(2 Pt 1):E273-78074207
Cites: Metabolism. 1995 Nov;44(11):1380-37476321
Cites: Biochem Mol Med. 1995 Oct;56(1):14-88593532
Cites: Biochemistry. 1996 Mar 26;35(12):3849-568620009
Cites: Methods Enzymol. 1996;266:525-398743704
Cites: J Inherit Metab Dis. 1996;19(4):452-628884569
Cites: Biochem Mol Med. 1996 Dec;59(2):134-78986635
Cites: J Inherit Metab Dis. 1997 Jul;20(3):401-39266366
Cites: J Biol Chem. 1997 Oct 17;272(42):26125-319334177
Cites: Pediatr Res. 1998 May;43(5):579-849585002
Cites: Am J Hum Genet. 1998 Jun;62(6):1312-99585612
Cites: J Neurosci Res. 1999 Aug 15;57(4):417-2810440891
Cites: J Biol Chem. 1951 Nov;193(1):265-7514907713
Cites: J Biol Chem. 1963 Aug;238:2603-814063279
Cites: Biochem J. 1989 Feb 1;257(3):913-62930495
PubMed ID
12437512 View in PubMed
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LMP1 strain variants: biological and molecular properties.

https://arctichealth.org/en/permalink/ahliterature81851
Source
J Virol. 2006 Jul;80(13):6458-68
Publication Type
Article
Date
Jul-2006
Author
Mainou Bernardo A
Raab-Traub Nancy
Author Affiliation
Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Source
J Virol. 2006 Jul;80(13):6458-68
Date
Jul-2006
Language
English
Publication Type
Article
Keywords
1-Phosphatidylinositol 3-Kinase - metabolism
Animals
Carcinoma - genetics - metabolism - virology
Cell Adhesion - genetics
Cell Line
Cell Transformation, Viral - genetics
Epstein-Barr Virus Infections - genetics - metabolism - virology
Fibroblasts - metabolism - virology
Hemolysis - genetics
Herpesvirus 4, Human - genetics - metabolism
Humans
NF-kappa B - metabolism
Nasopharyngeal Neoplasms - genetics - metabolism - virology
Oncogene Proteins, Viral - genetics - metabolism
Proto-Oncogene Proteins c-akt - metabolism
Rats
Signal Transduction - genetics
Species Specificity
Ubiquitin-Protein Ligases - metabolism
Variation (Genetics)
Viral Matrix Proteins - genetics - metabolism
Abstract
The ubiquitous herpesvirus Epstein-Barr virus (EBV) is linked to the development of several malignancies, including nasopharyngeal carcinoma. Latent membrane protein 1 (LMP1) is considered the EBV oncogene as it is necessary for EBV-induced transformation of B lymphocytes and is able to transform Rat-1 fibroblasts. LMP1 can activate a wide array of signaling pathways, including phosphatidylinositol 3-kinase (PI3K)-Akt and NF-kappaB. Six sequence variants of LMP1, termed Alaskan, China 1, China 2, Med+, Med-, and NC, have been identified, and individuals can be infected with multiple variants. The frequencies of detection of these variants differ for various EBV-associated malignancies from different geographic regions. In this study, the biological and signaling properties of the LMP1 variants have been characterized. All of the LMP1 variants transformed Rat-1 fibroblasts, induced increased motility of HFK cells, and induced increased homotypic adhesion of BJAB cells. While all the variants activated the PI3K-Akt signaling pathway to similar extents, the Alaskan, China 1, and Med+ variants had limited binding to the E3 ubiquitin ligase component homologue of Slimb and had slightly enhanced NF-kappaB signaling. These findings indicate that the signature amino acid changes of the LMP1 variants do not hinder or enhance their in vitro transforming potentials or affect their signaling properties.
PubMed ID
16775333 View in PubMed
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12 records – page 1 of 2.