@article {698,
	title = {PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.},
	journal = {J Biol Chem},
	volume = {280},
	year = {2005},
	month = {2005 Mar 11},
	pages = {9489-97},
	abstract = {Glycosylphosphatidylinositol (GPI) is a glycolipid that anchors many proteins to the eukaryotic cell surface. The biosynthetic pathway of GPI is mediated by sequential additions of sugars and other components to phosphatidylinositol. Four mannoses in the GPI are transferred from dolichol-phosphate-mannose (Dol-P-Man) and are linked through different glycosidic linkages. Therefore, four Dol-P-Man-dependent mannosyltransferases, GPI-MT-I, -MT-II, -MT-III, and -MT-IV for the first, second, third, and fourth mannoses, respectively, are required for generation of GPI. GPI-MT-I (PIG-M), GPI-MT-III (PIG-B), and GPI-MT-IV (SMP3) were previously reported, but GPI-MT-II remains to be identified. Here we report the cloning of PIG-V involved in transferring the second mannose in the GPI anchor. Human PIG-V encodes a 493-amino acid, endoplasmic reticulum (ER) resident protein with eight putative transmembrane regions. Saccharomyces cerevisiae protein encoded in open reading frame YBR004c, which we termed GPI18, has 25\% amino acid identity to human PIG-V. Viability of the yeast gpi18 deletion mutant was restored by human PIG-V cDNA. PIG-V has two functionally important conserved regions facing the ER lumen. Taken together, we suggest that PIG-V is the second mannosyltransferase in GPI anchor biosynthesis.},
	keywords = {Amino Acid Sequence, Animals, Cell Line, Tumor, CHO Cells, Cloning, Molecular, Conserved Sequence, Cricetinae, DNA Primers, Glioma, Glycosylphosphatidylinositols, Humans, Mannose, Mannosyltransferases, Molecular Sequence Data, Open Reading Frames, Rats, Restriction Mapping, Saccharomyces cerevisiae, Sequence Alignment, Sequence Homology, Amino Acid},
	issn = {0021-9258},
	doi = {10.1074/jbc.M413867200},
	author = {Kang, Ji Young and Hong, Yeongjin and Ashida, Hisashi and Shishioh, Nobue and Murakami, Yoshiko and Morita, Yasu S and Maeda, Yusuke and Kinoshita, Taroh}
}
@article {716,
	title = {Caveolin-2 associates with intracellular chlamydial inclusions independently of caveolin-1.},
	journal = {BMC Infect Dis},
	volume = {4},
	year = {2004},
	month = {2004 Jul 22},
	pages = {23},
	abstract = {BACKGROUND: Lipid raft domains form in plasma membranes of eukaryotic cells by the tight packing of glycosphingolipids and cholesterol. Caveolae are invaginated structures that form in lipid raft domains when the protein caveolin-1 is expressed. The Chlamydiaceae are obligate intracellular bacterial pathogens that replicate entirely within inclusions that develop from the phagocytic vacuoles in which they enter. We recently found that host cell caveolin-1 is associated with the intracellular vacuoles and inclusions of some chlamydial strains and species, and that entry of those strains depends on intact lipid raft domains. Caveolin-2 is another member of the caveolin family of proteins that is present in caveolae, but of unknown function.

METHODS: We utilized a caveolin-1 negative/caveolin-2 positive FRT cell line and laser confocal immunofluorescence techniques to visualize the colocalization of caveolin-2 with the chlamydial inclusions.

RESULTS: We show here that in infected HeLa cells, caveolin-2, as well as caveolin-1, colocalizes with inclusions of C. pneumoniae (Cp), C. caviae (GPIC), and C. trachomatis serovars E, F and K. In addition, caveolin-2 also associates with C. trachomatis serovars A, B and C, although caveolin-1 did not colocalize with these organisms. Moreover, caveolin-2 appears to be specifically, or indirectly, associated with the pathogens at the inclusion membranes. Using caveolin-1 deficient FRT cells, we show that although caveolin-2 normally is not transported out of the Golgi in the absence of caveolin-1, it nevertheless colocalizes with chlamydial inclusions in these cells. However, our results also show that caveolin-2 did not colocalize with UV-irradiated Chlamydia in FRT cells, suggesting that in these caveolin-1 negative cells, pathogen viability and very likely pathogen gene expression are necessary for the acquisition of caveolin-2 from the Golgi.

CONCLUSION: Caveolin-2 associates with the chlamydial inclusion independently of caveolin-1. The function of caveolin-2, either in the uninfected cell or in the chlamydial developmental cycle, remains to be elucidated. Nevertheless, this second caveolin protein can now be added to the small number of host proteins that are associated with the inclusions of this obligate intracellular pathogen.},
	keywords = {Animals, Blotting, Western, Caveolin 1, Caveolin 2, Caveolins, Cells, Cultured, Chlamydia, Fluorescent Antibody Technique, Golgi Apparatus, Guinea Pigs, HeLa Cells, Humans, Mice, Microscopy, Confocal, Rats, Vacuoles, Virulence},
	issn = {1471-2334},
	doi = {10.1186/1471-2334-4-23},
	author = {Webley, Wilmore C and Norkin, Leonard C and Stuart, Elizabeth S}
}
@article {800,
	title = {Norway rats as reservoir hosts for Lyme disease spirochetes on Monhegan Island, Maine.},
	journal = {J Infect Dis},
	volume = {168},
	year = {1993},
	month = {1993 Sep},
	pages = {687-91},
	abstract = {To determine whether the agent of Lyme disease, Borrelia burgdorferi, may be maintained in the absence of its usual white-footed mouse reservoir host, Ixodes dammini ticks from an island where mice are absent were examined. Prevalence of spirochetal infection was described for ticks removed from mammals, birds, and vegetation on Monhegan Island, Maine. Forty percent of adult I. dammini removed from vegetation were infected. Norway rats were heavily infested with ticks, and > 60\% of such ticks contained spirochetes. Other hosts were less frequently infested by ticks, and few such ticks were infected by spirochetes. The prevalence of antibody to B. burgdorferi was 23\% in dogs and cats; 4\% of island residents had Lyme disease. Thus, rats maintain Lyme disease spirochetes on Monhegan Island, and there may be transmission of this agent by I. dammini to island residents and their pets.},
	keywords = {Animals, Animals, Domestic, Antibodies, Bacterial, Borrelia burgdorferi Group, Cats, Disease Reservoirs, Disease Vectors, Dogs, Geography, Humans, Incidence, Lyme Disease, Maine, Rats, Ticks},
	issn = {0022-1899},
	author = {Smith, R P and Rand, P W and Lacombe, E H and Telford, S R and Rich, S M and Piesman, J and Spielman, A}
}
@article {1731,
	title = {Disposition of (15,16-3H)naltrexone in the central nervous system of the rat.},
	journal = {Drug Metab Dispos},
	volume = {4},
	year = {1976},
	month = {1976 May-Jun},
	pages = {276-80},
	abstract = {<p>After injection of (15,16-3H)naltrexone (10 mg/kg s.c.) in male Wistar rats, peak concentrations of drug occurred in brain and plasma within 0.5 hr. Levels of naltrexone were sustained in brain between 2 and 24 hr and were barely detectable at 48 hr. Significant amounts of metabolities were present in brain and plasma at longer time periods. The t1/2 of naltrexone in brain and plasma were approximately 8.0 and 11.4 hr. respectively. The brain/plasma ratios of naltrexone at earlier times (0.5-1 hr) were higher than those at later times. The binding of naltrexone in vitro with rat plasma proteins in concentrations of 1-10 mug/ml ranged between 41 and 59\% 6beta-Naltrexol was present in very small amounts in brain but not in plasma. In addition to 7,8-dihydro-14-hydroxynormophinone and 7,8-dihydro-14-hydroxynormophine, tentative evidence was obtained for three other metabolites of naltrexone in brain. These metabolites were also present in plasma in addition to free and conjugated naltrexone and its N-dealkylated metabolites.</p>},
	keywords = {Animals, Blood-Brain Barrier, Brain, Chromatography, Thin Layer, Male, Naloxone, Naltrexone, Rats},
	issn = {0090-9556},
	author = {Misra, A L and Bloch, R and Vardy, J and Mul{\'e}, S J and Verebely, K}
}
@article {1711,
	title = {Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase.},
	journal = {Biochem Pharmacol},
	volume = {24},
	year = {1975},
	month = {1975 Aug 15},
	pages = {1517-21},
	keywords = {Amidohydrolases, Animals, Esterases, Hydrogen-Ion Concentration, In Vitro Techniques, Isocarboxazid, Kinetics, Male, Metals, Microsomes, Liver, Phospholipids, Procaine, Proteins, Rats, Subcellular Fractions, Temperature},
	issn = {0006-2952},
	author = {Moroi, K and Sato, T}
}
@article {1706,
	title = {Digitoxin metabolism by rat liver microsomes.},
	journal = {Biochem Pharmacol},
	volume = {24},
	year = {1975},
	month = {1975 Sep 1},
	pages = {1639-41},
	keywords = {Animals, Chromatography, Thin Layer, Digitoxigenin, Digitoxin, Hydroxylation, In Vitro Techniques, Male, Microsomes, Liver, NADP, Rats, Time Factors},
	issn = {0006-2952},
	author = {Schmoldt, A and Benthe, H F and Haberland, G}
}
@article {1722,
	title = {Influence of a new virostatic compound on the induction of enzymes in rat liver.},
	journal = {Arzneimittelforschung},
	volume = {25},
	year = {1975},
	month = {1975 Sep},
	pages = {1426-9},
	abstract = {<p>The virostatic compound N,N-diethyl-4-[2-(2-oxo-3-tetradecyl-1-imidazolidinyl)-ethyl]-1-piperazinecarboxamide-hydrochloride (5531) was analyzed as to its effect on the induction of tryptophan-pyrrolase and tyrosineaminotransferase in rat liver. 1. The basic activity of the enzymes was not influenced by the substance either in normal or in adrenalectomized animals. 2. The induction of the enzymes by cortisone increased in the presence of the compound whereas the substrate induction remained unchanged. 3. The induction of tyrosine-aminotransferase by dexamethasonephosphate in tissue culture is inhibited if the dose of compound 5531 is higher than 5 mug/ml.</p>},
	keywords = {Adrenalectomy, Animals, Antiviral Agents, Cortisone, Culture Techniques, Dose-Response Relationship, Drug, Enzyme Induction, Female, Imidazoles, Liver, Piperazines, Rats, Time Factors, Tryptophan Oxygenase, Tyrosine, Tyrosine Transaminase},
	issn = {0004-4172},
	author = {Kr{\"o}ger, H and Donner, I and Skiello, G}
}
@article {1727,
	title = {Inhibition of aldehyde reductase isoenzymes in human and rat brain.},
	journal = {Biochem Pharmacol},
	volume = {24},
	year = {1975},
	month = {1975 Oct 15},
	pages = {1865-9},
	keywords = {Aldehyde Oxidoreductases, Animals, Anticonvulsants, Barbiturates, Brain, Glutethimide, Humans, Hydantoins, In Vitro Techniques, Isoenzymes, Kinetics, NAD, NADP, Rats, Succinimides},
	issn = {0006-2952},
	author = {Ris, M M and Deitrich, R A and Von Wartburg, J P}
}
@article {1704,
	title = {Maturation of the adrenal medulla--IV. Effects of morphine.},
	journal = {Biochem Pharmacol},
	volume = {24},
	year = {1975},
	month = {1975 Aug 15},
	pages = {1469-74},
	keywords = {Adrenal Medulla, Aging, Animals, Animals, Newborn, Body Weight, Catecholamines, Dopamine beta-Hydroxylase, Epinephrine, Female, Humans, In Vitro Techniques, Maternal-Fetal Exchange, Metaraminol, Morphine, Morphine Dependence, Pregnancy, Rats, Tyrosine 3-Monooxygenase},
	issn = {0006-2952},
	author = {Anderson, T R and Slotkin, T A}
}
@article {1713,
	title = {The relative importance of monoamine oxidase and catechol-O-methyl transferase on the physiologic response to administered norepinephrine in the turkey.},
	journal = {Comp Biochem Physiol C},
	volume = {52},
	year = {1975},
	month = {1975 Oct 1},
	pages = {35-9},
	keywords = {Animals, Blood Pressure, Catechol O-Methyltransferase, Chickens, Epinephrine, Heart, Kidney, Kinetics, Liver, Monoamine Oxidase, Myocardium, Norepinephrine, Organ Specificity, Rats, Species Specificity, Turkeys},
	issn = {0306-4492},
	author = {El Halawani, M E and Waibel, P E}
}
