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Protein kinase A-dependent phosphorylation of B/K protein
Chin, Hemin,Choi, Sung-Ho,Jang, Yoon-Seong,Cho, Sung-Min,Kim, Ho-Shik,Lee, Jeong-Hwa,Jeong, Seong-Whan,Kim, In-Kyung,Kim, Grace J,Kwon, Oh-Joo Springer Science and Business Media LLC 2006 Experimental and molecular medicine Vol.38 No.2
<P>We have previously isolated a novel protein 'B/K' that contains two C2-like domains. Here, we report the isolation and mRNA distribution of a human B/K isoform, and protein kinase A (PKA)-dependent phosphorylation of the B/K protein. The 1.5 kb human B/K cDNA clone exhibits 89% and 97% identities with rat B/K in the sequences of nucleotide and amino acid, respectively. Human B/K isoform encodes a 474 amino acid protein and shows structural features similar to the rat counterpart including two C2 domains, three consensus sequences for PKA, absence of a transmembrane region, and conservation of the N-terminal cysteine cluster. On Northern and dot blot analyses, a 3.0 kb B/K transcript was abundantly present in human brain, kidney, and prostate. Among the brain regions, strong signals were observed in the frontal and temporal lobes, the hippocampus, the hypothalamus, the amygdala, the substantia nigra, and the pituitary. Recombinant B/K proteins containing three consensus sites for PKA was very efficiently phosphorylated in vitro by PKA catalytic subunit. B/K protein which was overexpressed in LLC-PK1 cells was also strongly phosphorylated in vivo by vasopressin analog DDAVP, and PKA-specific inhibitor H 89 as well as type 2 vasopressin receptor antagonist specifically suppressed DDAVP-induced B/K phosphorylation. These results suggest that B/K proteins play a role as potential substrates for PKA in the area where they are expressed.</P>
Lee, Sang Kyu,Lee, Dong Ju,Jeong, Hemin,Bista, Sudeep R.,Kang, Mi Jeong,Lee, Eung Seok,Son, Jong Keun,Nam, Doo Hyun,Chang, Hyeun Wook,Lee, Seung Ho,Jahng, Yurngdong,Jeong, Tae Cheon Taylor Francis 2007 Journal of toxicology and environmental health. Pa Vol.70 No.15
<P> To determine a possible role of glutathione (GSH) conjugation in 1,3-dibromopropane (1,3-DBP)-induced hepatotoxicity and immunotoxicity, female BALB/c mice were treated orally with 1,3-DBP. Based on the liquid chromatography/electrospray ionization-tandem mass spectrometry (LC/ESI-MS) analyses, two forms of S-bromopropyl GSH were observed at m/z 427.9 and 429.9 in the positive ESI spectrum with a retention time of 5.29 and 5.23 min, respectively. Following single treatment of mice with 150, 300 or 600 mg/kg 1,3-DBP for 12 hr, the amount of S-bromopropyl GSH was detected maximally in liver homogenates at 600 mg/kg 1,3-DBP. Hepatic GSH levels were significantly decreased by treatment with 1,3-DBP. In a time course study, production of S-bromopropyl GSH rose maximally 6 hr after treatment and decreased gradually thereafter. The liver weights were significantly increased by treatment with 600 mg/kg 1,3-DBP. When mice were treated orally with 600 mg/kg 1,3-DBP for 12 hr, the activities of serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) were increased by 365- and 83-fold. In addition, oral 1,3-DBP significantly suppressed the antibody response to a T-dependent antigen at 600 mg/kg 1,3-DBP. 1,3-DBP elevated hepatic levels of malondialdehyde and suppressed the activities of some hepatic enzymes involved in anti-oxidation. Taken together, the formation of GSH conjugate with 1,3-DBP may deplete cellular GSH and, subsequently, produce hepatotoxicity and immunotoxicity via damage to the cellular anti-oxidative system.</P>
Sun Hee Hyun,Tae Won Jeon,Sang Kyu Lee,Chun Hwa Kim,Young Min Seo,Ju Hyun Kim,Hemin Jeong,Mi Jeong Kang,Jae Sung Lee,Tae Cheon Jeong 한국독성학회 2007 Toxicological Research Vol.23 No.2
Paecilomyces tenuipes (PT), one of the Ascomycetes family, has been used for medicinal purposes due to its broad pharmacological activities. The present study was undertaken to investigate the hepatoprotective effects of PT water extracts against CCl₄-induced hepatotoxicity in primary cultures of adult rat hepatocytes. When the extract of PT was directly added into the culture medium at 1, 2, and 5 mg/ml, the extracts not only reduce the CCl₄-induced elevation of aspartate aminotransferase (AST), alanine aminotransferase (ALT), lactate dehydrogenase, and lipid peroxide, but also protect cultured hepatocytes from CCl₄-induced reduction of reduced glutathione, glutathione reductase, glutathione- S-transferase, glutathione peroxidase, catalase and superoxide dismutase. In addition, the effects of PT water extracts on cytochrome P450 enzymes were relatively marginal, indicating that the hepatoprotective effects of PT extract against CCl₄-induced toxicity might not be due to the inhibition of CCl₄ activation. In conclusion, the PT extracts were effective in protecting against CCl₄- induced hepatotoxicity in hepatocyte cultures, at least in part, by scavenging free radicals, and by modulating enzyme systems involved in cellular oxidative stress.
The Effects of Rutaecarpine on the Pharmacokinetics of Acetaminophen in Rats
이상규,Sudeep R. Bista,Hemin Jeong,Dong Hyeon Kim,강미정,장영동,정태천 대한약학회 2007 Archives of Pharmacal Research Vol.30 No.12
Rutaecarpine, an alkaloid originally isolated from the unripe fruit of Evodia rutaecarpa, has been shown to be anti-inflammatory as it inhibits cyclooxygenase-2. It induces the activities of hepatic CYP 1A2, 2B, and 2E1 in rats. A possible interaction between rutaecarpine and acetaminophen (APAP) was investigated in male Sprague Dawley rats in the present study. When 25 mg/kg APAP was intravenously administered concurrently with 80 mg/kg rutaecarpine, the area under the curve of APAP in plasma was significantly decreased when compared to that of APAP alone. When the rats were pre-treated orally with 40 and 80 mg/kg rutaecarpine for 3 days, the % value of Cmax and area under the curve of acetaminophen-sulfate conjugate were significantly decreased to 56.4% and 61.7% of the vehicle control group, respectively. These results suggest that rutaecarpine might cause changes in the pharmacokinetic parameters of APAP in rats.