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1.
Scand J Clin Lab Invest ; 64(3): 223-8, 2004.
Article in English | MEDLINE | ID: mdl-15222632

ABSTRACT

Though the concentration of serum lipoprotein(a) [Lp(a)] is mostly determined by genetic factors, secondary factors such as acute-phase response (APR) and end-stage renal disease (ESRD) also contribute to its increase. Lp(a) is known to be one of the acute-phase reactants and interleukin-6 (IL-6) is the key cytokine in the hepatic synthesis of acute-phase proteins. The serum concentrations of Lp(a) and IL-6 were measured in patients with APR and in patients with ESRD to investigate the relationship between Lp(a) and IL-6. A total of 180 patients were selected for the study: 60 patients were normal controls, 60 were patients with renal disease who had been on hemodialysis for more than 6 months [C-reactive protein (CRP)<4.0 mg/L], and 60 were APR patients who had a erythrocyte sedimentation rate (ESR) of over 50 mm/h. The three groups were age- and sex matched. The serum concentrations of Lp(a) and IL-6 were measured by ELISA. The serum concentrations of Lp(a) [median (interquartile range)] in normal controls, ESRD patients, and APR patients were 0.222 (0.103-0.364) g/L, 0.511 (0.308-0.755) g/L, and 0.546 (0.234-0.747) g/L, respectively; those of IL-6 were 1.0 (0.7-1.3) pg/mL, 2.1 (1.4-3.3) pg/mL, and 26.2 (15.2-35.6) pg/mL. The concentration of IL-6, which increases Lp(a) synthesis, was much lower in ESRD patients than in APR patients (p<0.001). However, there were no significant differences in Lp(a) concentration between the two groups (p=0.88). In APR patients, the increase in Lp(a) synthesis seems to play a significant role in the increase in blood Lp(a), but there might be different mechanisms that regulate the increment of serum Lp(a) concentrations in ESRD patients other than synthesis of Lp(a).


Subject(s)
Acute-Phase Reaction/blood , Interleukin-6/blood , Kidney Failure, Chronic/blood , Lipoprotein(a)/blood , C-Reactive Protein/analysis , Female , Humans , Interleukin-6/metabolism , Male , Middle Aged , Statistics, Nonparametric
2.
Exp Mol Med ; 32(4): 216-21, 2000 Dec 31.
Article in English | MEDLINE | ID: mdl-11190273

ABSTRACT

The protooncogene c-myc is known to be associated with both cell proliferation and apoptosis. The possible cellular affects of castration on the ventral prostate gland of rat as well as the relationship to a castration induced c-myc expression were examined. Levels of c-myc mRNA in the ventral prostate gland peaked at 6 h (early induction) and 48 h (late induction) after castration, respectively. Castration-induced DNA fragmentation was not observed at an early induction of c-myc mRNA. DNA fragmentation appeared to be testosterone-dependent. On the other hand, cellular DNA synthesis measured by [3H]thymidine uptake in the ventral prostate gland was increased to maximum at 6 h after castration. These results suggest that an early induction of c-myc mRNA in ventral prostate gland after castration is closely associated with cell proliferation of the gland.


Subject(s)
Orchiectomy , Prostate/cytology , Proto-Oncogene Proteins c-myc/genetics , Animals , Apoptosis , Cell Division , DNA Fragmentation , Male , Proto-Oncogene Proteins c-myc/biosynthesis , RNA, Messenger , Rats , Rats, Sprague-Dawley
3.
Biochem Mol Biol Int ; 46(1): 35-42, 1998 Sep.
Article in English | MEDLINE | ID: mdl-9784837

ABSTRACT

DNA topoisomerase II is a marker for the proliferation state of mammalian cells in culture, and the protein levels are markedly higher in exponentially growing cells than quiescent cells and can be downregulated by growth of the cells at high density and serum starvation. Correlation between ATF and TPA-repressed DNA topoisomerase II alpha (Topo II alpha) mRNA has been investigated during TPA-induced differentiation of HL-60 cells. Topo II alpha mRNA and unknotting activity were reduced at 24 hours in TPA-treated HL-60 cells. The level of Topo II alpha mRNA and the activity were gradually decreased in proportion to the concentration of TPA. Two DNA-protein complexes were formed by DNA mobility shift assay when ATF-binding site was incubated with nuclear extract prepared from TPA-free HL-60 cells, and the amount of ATF was vanished after TPA treatment. TPA-repressed Topo II alpha mRNA and ATF levels were partially restored after pretreatment of staurosporin. These results suggest that the reduced level of ATF may be important to the transcriptional repression of Topo II alpha gene during TPA-induced differentiation in HL-60 cells and related to protein kinase C signal pathway.


Subject(s)
Blood Proteins/metabolism , Cell Differentiation , DNA Topoisomerases, Type II , DNA Topoisomerases, Type II/genetics , Isoenzymes/genetics , Tetradecanoylphorbol Acetate/pharmacology , Transcription Factors/metabolism , Transcription, Genetic , Activating Transcription Factors , Antigens, Neoplasm , Binding Sites , Blotting, Northern , DNA/metabolism , DNA Topoisomerases, Type II/biosynthesis , DNA-Binding Proteins , Dose-Response Relationship, Drug , Enzyme Inhibitors/pharmacology , Enzyme Repression/drug effects , HL-60 Cells , Humans , Isoenzymes/biosynthesis , Promoter Regions, Genetic , Protein Binding , Protein Kinase C/antagonists & inhibitors , Protein Kinase C/metabolism , RNA, Messenger/genetics , RNA, Messenger/metabolism , Signal Transduction , Staurosporine/pharmacology , Transcription, Genetic/drug effects
4.
Biochem Mol Biol Int ; 45(3): 575-82, 1998 Jul.
Article in English | MEDLINE | ID: mdl-9679659

ABSTRACT

Epidermal growth factor (EGF) is a potent mitogen for rat hepatocytes and mammalian histone synthesis is functionally and temporally coupled to DNA replication. To gain an insight on the role of EGF in the regulation of H2B histone gene expression in primary hepatocyte cultures, the binding patterns of nuclear proteins to various elements in the H2B histone gene upstream region have been investigated. EGF induced H2B histone mRNA with maximal stimulation reached at 36 hours. The induction of H2B histone mRNA was dependent on the concentration of EGF and almost reduced by actinomycin-D pretreatment. In DNase I footprinting analysis, one nuclear factor (TATA element-binding protein, TBP) bound at -20 bp (TATA element) in either the absence or presence of EGF. One DNA-protein complex was formed by DNA mobility shift assay when TATA element was incubated with nuclear extract prepared from EGF-free hepatocytes, and the amount of TBP was increased after EGF treatment. These results suggest that TBP may be correlated with transcriptional regulation of H2B histone gene by EGF in primary hepatocytes.


Subject(s)
DNA-Binding Proteins/physiology , Epidermal Growth Factor/physiology , Gene Expression Regulation/physiology , Histones/genetics , Transcription Factors/physiology , Animals , Base Sequence , Binding Sites , Cells, Cultured , Dactinomycin/pharmacology , Dose-Response Relationship, Drug , Gene Expression Regulation/drug effects , Liver/cytology , Male , Molecular Sequence Data , Promoter Regions, Genetic/genetics , Protein Synthesis Inhibitors/pharmacology , RNA, Messenger/drug effects , RNA, Messenger/metabolism , Rats , Rats, Sprague-Dawley , TATA Box , TATA-Box Binding Protein
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