Retraction Note to: Identification of CYP3A4 as the primary cytochrome P450 responsible for the metabolism of tandospirone by human liver microsomes.

The publisher has retracted this article [1] because it is an incorrect version that was published in error: Figures 5 and 6 are missing.

[Clinical evaluation of the risk factors for liver abscess after TACE or RFA].

Radiofrequency ablation(RFA)and transcatheter arterial chemoembolization (TACE) are widely enforced as a standard combined therapy for liver cancer. Liver abscess occurs occasionally as a complication. This clinical study was conducted to determine risk factors for liver abscess.

[Two cases of liver abscess caused by Clostridium perfringens after transcatheter arterial chemoembolization].

Case 1 involved a 74-year-old man. After transcatheter arterial chemoembolization( TACE) for hepatocellular carcinoma (HCC), abdominal computed tomography (CT) revealed a gas-containing lesion in the liver. The patient was diagnosed as having a gas-containing liver abscess, necessitating emergency drainage under laparotomy.

[A case report of GIST of the small intestine with multiple liver abscesses].

We report a case of a woman in her fifties presenting with abdominal pain, headache and high fever. Blood examination showed a high CRP level and liver dysfunction, and then abdominal CT scan showed multiple liver masses and a 5 cm submucosal tumor of the small intestine. We diagnosed the multiple liver masses as liver abscesses, so we administered antibiotics.

Identification of CYP3A4 as the primary cytochrome P450 responsible for the metabolism of tandospirone by human liver microsomes.

The present study was carried out to characterize the human P450 isoforms involved in the metabolism of tandospirone, an anxiolytic agent known for its superior efficacy and safety. Among 11 yeast-expressed recombinant P450 isoforms tested, CYP2D6 and CYP3A4 exhibited the highest tandospirone metabolic activity. Although there was no qualitative difference between the two isoforms, a quantitative difference in metabolite profiling was found i.

Identification of CYP3A4 as the primary cytochrome P450 responsible for the metabolism of tandospirone by human liver microsomes.

The present study was carried out to characterize the human P450 isoforms involved in the metabolism of tandospirone, an anxiolytic agent known for its superior efficacy and safety. Among 11 yeast-expressed recombinant P450 isoforms tested, CYP2D6 and CYP3A4 exhibited the highest tandospirone metabolic activity. Although there was no qualitative difference between the two isoforms, a quantitative difference in metabolite profiling was found i.

In vitro drug-drug interactions with perospirone and concomitantly administered drugs in human liver microsomes.

In vitro metabolism studies were conducted to assess drug-drug interactions between perospirone, an antipsychotic agent, and concomitantly administered drugs--biperiden, flunitrazepam, haloperidol, and diazepam--using human liver microsomes. The metabolism of perospirone in the presence of 100 microg/ml drugs was decreased to 45-73% of that in their absence, whereas no effects were observed with any of the drugs at 1 microg/ml or lower. The effects of perospirone on the metabolism of concomitantly administered drugs were also assessed, and no inhibitory effect was observed.

In vitro metabolism of perospirone in rat, monkey and human liver microsomes.

In vitro metabolism of perospirone was examined with rat, monkey and human liver S9, human liver microsomes and yeast microsomes expressing human P450, using 14C labeled perospirone. With rat liver S9, the major metabolites were MX9 and ID-11614, produced by cleavage at the butylene chain. However, some butylene non-cleavage and hydration of the cyclohexane ring were found, although limited in extent.