International Hepatology Communications最新文献

{"title":"Adenomyomatosis of the gallbladder","authors":"E. Kyriacou, I.A.D. Bouchier","doi":"10.1016/0928-4346(96)00287-3","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00287-3","url":null,"abstract":"","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00287-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91690594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hepatic stimulator substance administration affects cadmium-induced hepatotoxicity in the rat","authors":"A. Margeli, S. Theocharis, C. Spiliopoulou, M. Horti, A. Koutselinis","doi":"10.1016/0928-4346(96)00290-3","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00290-3","url":null,"abstract":"","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84560418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Genetic polymorphism of the rat aldehyde dehydrogenase 2 and the severity of experimental alcohol-induced liver damage","authors":"M. Yamauchi, Y. Maezawa, S. Satoh, Y. Mizuhara, G. Toda","doi":"10.1016/0928-4346(96)00294-0","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00294-0","url":null,"abstract":"","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91237411","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Human liver mitochondrial RNA synthesized in isolated organelles","authors":"Acisclo Pérez-Martos ,&nbsp;Antonio L. Andreu ,&nbsp;Manuel J. López-Pérez ,&nbsp;Josep E. Murio ,&nbsp;Simón Schwartz ,&nbsp;Julio Montoya","doi":"10.1016/0928-4346(96)00289-7","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00289-7","url":null,"abstract":"<div><p>The study of alterations of mitochondrial DNA transcription could be of fundamental interest to understand the molecular mechanisms underlying the impairment of mitochondrial function in liver diseases related to hepatocyte energy production. We show that isolated normal human liver mitochondria, when incubated in the presence of [α-³²P]UTP in an appropriate incubation medium, in which the energy requirements are provided by exogenous ADP in the presence of oxidizable substrates, are able to support RNA synthesis in a way faithfully resembling the in vivo process. The autoradiographic pattern in agarosemethylmercury hydroxide gels of the newly synthesized RNA shows the presence of all the previously described RNAs coded in the mitochondrial genome (ribosomal, messenger and transfer RNAs). We conclude that this system could be of great value to investigate the role of the mitochondrial genome on human liver pathology related to mitochondrial damage.</p></div>","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00289-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91690593","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Retreatment with 24-week course of interferon-α for patients with chronic hepatitis C","authors":"Hideki Hagiwara,&nbsp;Norio Hayashi,&nbsp;Masahide Oshita,&nbsp;Kazuhiro Katayama,&nbsp;Akinori Kasahara,&nbsp;Hideyuki Fusamoto,&nbsp;Takenobu Kamada","doi":"10.1016/0928-4346(96)00291-5","DOIUrl":"10.1016/0928-4346(96)00291-5","url":null,"abstract":"<div><p>Twenty-nine patients with chronic hepatitis C were retreated with a 24-week course of natural interferon-α to evaluate the efficacy of retreatment with interferon for patients who were resistant to previous therapy. At 6 months after the end of retreatment, three patients (10%) had achieved sustained alanine aminotransferase normalization and sustained clearance of hepatitis C virus RNA in serum. Fifteen patients (52%) showed alanine aminotransferase normalization during retreatment but suffered from relapse during the 24 weeks after retreatment. In 11 patients (38%), no significant decrease of alanine aminotransferase was observed during and after retreatment. Three of ten patients with hepatitis C virus RNA of 2.3 × 10⁵ equivalents/ml or less became sustained responders but none of the patients with a higher virus level achieved a sustained response. These results indicate that retreatment with a 24-week course of interferon is not efficient and other approaches are needed to attain a higher rate of sustained response, especially in patients with high viral load.</p></div>","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00291-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89933701","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Genetic polymorphism of the rat aldehyde dehydrogenase 2 and the severity of experimental alcohol-induced liver damage","authors":"Masayoshi Yamauchi,&nbsp;Yoshihiko Maezawa,&nbsp;Shyunya Satoh,&nbsp;Yuji Mizuhara,&nbsp;Gotaro Toda","doi":"10.1016/0928-4346(96)00294-0","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00294-0","url":null,"abstract":"<div><p>In humans, alcoholic liver disease in the heterozygotes of the aldehyde dehydrogenase (ALDH) 2 gene is more severe than that in the normal homozygotes. Recently, a substitution (G for A) was identified in the cDNA of alcohol-nonpreferring (NP) rats which changes amino acid 67 from Gln (CAG codon; ALDH2^Q allele) to Arg (CGG codon; ALDH2^R allele). To determine whether the ALDH2 polymorphism was associated with the development of alcoholic liver damage in the each 15 alcohol-fed and control rats, we genotyped the ALDH2 locus by polymerase chain reaction (PCR) amplification followed by electrophoresis after digestion with <em>Dde</em>I. The frequencies of ALDH2 genotype in commercially available Sprague-Dawley rats were 36.7% for the <span><math><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>Q</mtext></mn></msup><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>Q</mtext></mn></msup></math></span>, 53.3% for the <span><math><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>Q</mtext></mn></msup><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>R</mtext></mn></msup></math></span> and 10.0% for the <span><math><mtext>ALDH2R</mtext><mtext>ALDH2R</mtext></math></span>, respectively. Hepatic collagen-bound hydroxyproline was higher in the ethanol-fed rats with <span><math><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>Q</mtext></mn></msup><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>R</mtext></mn></msup></math></span> or <span><math><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>R</mtext></mn></msup><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>R</mtext></mn></msup></math></span> than in the ethanol-fed rats with <span><math><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>Q</mtext></mn></msup><mtext>ALDH2</mtext><msup><mi></mi><mn><mtext>R</mtext></mn></msup></math></span>. The ALDH2^R allele may be associated with the severity of experimental alcohol-induced liver damage.</p></div>","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00294-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91732081","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alterations in some hepatic biochemical variables following repeated gallium arsenide administration in rats","authors":"S.J.S. Flora","doi":"10.1016/0928-4346(96)00285-X","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00285-X","url":null,"abstract":"<div><p>Gallium arsenide (GaAs), an intermetallic compound with superior semi-conductor properties, is finding extensive application in the electronic industry. Exposure to airborne particles in the GaAs industry may pose potential health hazards to workers. However, very little information is available so far regarding the possible toxic effects of this compound. The present study was planned to investigate the dose-dependent influence of repeated gallium arsenide (GaAs) administration (50, 100 or 200 mg/kg, orally through gastric intubation, 5 days a week for 3 weeks) on some biochemical indices in blood and hepatic tissues. The results indicate a significant dose-dependent inhibition of blood δ-aminolevulinic acid dehydratase (ALAD) activity, glutathione and an elevation in zinc protoporphyrin level. Blood haemoglobin level decreased only at the two higher dose levels. The effects of GaAs administration on hepatic biochemical variables indicates only moderate adverse effects on serum glutamic oxaloacetic (GOT) and glutamic pyruvic transaminase (GPT) following exposure at the highest dose (200 mg/kg). GaAs exposure also lead to a significant inhibition of hepatic ALAD activity, an elevation in MDA formation and alkaline phosphatase activity. Most of the above alterations occurred at the 200 mg/kg dose. Dose-dependent increases in blood and hepatic arsenic concentration were also noticed. The results confirm our earlier observation that GaAs had a marked influence on the haematopoietic system while it has only moderate effect on the hepatic organ.</p></div>","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00285-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90030162","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cold activation of complement enhancing with the duration of storage in sera from blood donors with hepatitis C virus RNA","authors":"Keiichi Itoh ,&nbsp;Hidenori Tanaka ,&nbsp;Jun-ichi Shiga ,&nbsp;Kazuya Hirakawa ,&nbsp;Fumio Tsuda ,&nbsp;Hiroaki Okamoto ,&nbsp;Yuzo Miyakawa ,&nbsp;Makoto Mayumi","doi":"10.1016/0928-4346(96)00267-8","DOIUrl":"10.1016/0928-4346(96)00267-8","url":null,"abstract":"<div><p>The cold activation of complement, determined by hemolytic activity of sera stored at low temperature, closely correlates with ongoing hepatitis C virus (HCV) injection. Of 53 189 blood units donated at a blood center in Japan, 187 (0.35%) were positive for antibody to HCV of which 65 (35% of the units with antibody) contained detectable HCV RNA. While sera from the 65 units with HCV RNA had been stored at 4°C, the cold activation of complement was observed in 43 (66%) at day 1, an additional 13 (20%) at day 4, and further in 4 (6%) at day 7. Thus, the cold activation was observed in 60 (92%) of 65 sera with HCV RNA during the storage at low temperature for 7 days. Cryoglobulins were detected only in 13 of the 43 sera which showed the cold activation at day 1, and the donors with cryoglobulinemia were older than the 52 viremic donors without it (mean ± S.D.: 47 ± 10 vs. 40 ± 11 years, <em>P</em> &lt; 0.05). There were no differences in the distribution of HCV genotypes in sera which showed the cold activation at day 1; they were 24 (69%) of 35 sera with genotype <span><math><mtext>II</mtext><mtext>1b</mtext></math></span>, 15 (68%) of 22 with <span><math><mtext>III</mtext><mtext>2a</mtext></math></span> and 4 (50%) of 8 with <span><math><mtext>IV</mtext><mtext>2b</mtext></math></span>. The results indicate that it would take up to a week before the cold activation is fully manifested in sera from persons infected with HCV.</p></div>","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00267-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89040130","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Adenomyomatosis of the gallbladder","authors":"E. Kyriacou, I. Bouchier","doi":"10.1016/0928-4346(96)00287-3","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00287-3","url":null,"abstract":"","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79599586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hepatic stimulator substance administration affects cadmium-induced hepatotoxicity in the rat","authors":"Alexandra P. Margeli,&nbsp;Stamatios E. Theocharis,&nbsp;Chara Spiliopoulou,&nbsp;Maria Horti,&nbsp;Antonios Koutselinis","doi":"10.1016/0928-4346(96)00290-3","DOIUrl":"https://doi.org/10.1016/0928-4346(96)00290-3","url":null,"abstract":"<div><p>The effect of hepatic stimulator substance (HSS) administration on cadmium (Cd) induced hepatotoxicity was studied in the rat. HSS was extracted from the liver of weanling rats (Hepatology 1988; 7: 100–106). Rats were injected with 2.5 mg CdCl₂/kg body weight to induce acute liver injury, evaluated 24 h later. Serum enzyme activities of alanine amino-transferase (ALT), aspartate aminotransferase (AST) and histological parameters were used for the estimation of Cd-induced hepatotoxicity. HSS, at doses of 10, 20 and 40 mg protein/kg body weight, injected 10 h after Cd administration, caused dose-dependent decrease of hepatic injury. HSS suppressed the elevation of AST and ALT induced by Cd, in a dose-dependent manner. Liver histological changes indicated that HSS reduced the severity of hepatic lesion induced by Cd administration and reversed Cd-induced hepatotoxicity. In conclusion, our results suggest that HSS administration protects the liver against Cd-induced injury.</p></div>","PeriodicalId":13746,"journal":{"name":"International Hepatology Communications","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0928-4346(96)00290-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91690592","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}