<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Stuart, Elizabeth S</style></author><author><style face="normal" font="default" size="100%">Webley, Wilmore C</style></author><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells.</style></title><secondary-title><style face="normal" font="default" size="100%">Exp Cell Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Exp. Cell Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anti-Bacterial Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolae</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Chlamydia</style></keyword><keyword><style  face="normal" font="default" size="100%">Chlamydia Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Cholesterol</style></keyword><keyword><style  face="normal" font="default" size="100%">Dose-Response Relationship, Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Eukaryotic Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Filipin</style></keyword><keyword><style  face="normal" font="default" size="100%">HeLa Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Host-Parasite Interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Microdomains</style></keyword><keyword><style  face="normal" font="default" size="100%">Nystatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2003 Jul 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">287</style></volume><pages><style face="normal" font="default" size="100%">67-78</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Obligate intracellular bacterial pathogens of the genus Chlamydia are reported to enter host cells by both clathrin-dependent and clathrin-independent processes. C. trachomatis serovar K recently was shown to enter cells via caveolae-like lipid raft domains. We asked here how widespread raft-mediated entry might be among the Chlamydia. We show that C. pneumoniae, an important cause of respiratory infections in humans that additionally is associated with cardiovascular disease, and C. psittaci, an important pathogen in domestic mammals and birds that also infects humans, each enter host cells via cholesterol-rich lipid raft microdomains. Further, we show that C. trachomatis serovars E and F also use these domains to enter host cells. The involvement of these membrane domains in the entry of these organisms was indicated by the sensitivity of their entry to the raft-disrupting agents Nystatin and filipin, and by their intracellular association with caveolin-1, a 22-kDa protein associated with the formation of caveolae in rafts. In contrast, caveolin-marked lipid raft domains do not mediate entry of C. trachomatis serovars A, 36B, and C, nor of LGV serovar L2 and MoPn. Finally, we show that entry of each of these chlamydial strains is independent of cellular expression of caveolin-1. Thus, entry via the Nystatin and filipin-sensitive pathway is dependent on lipid rafts containing cholesterol, rather than invaginated caveolae per se.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12799183?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kröger, H</style></author><author><style face="normal" font="default" size="100%">Donner, I</style></author><author><style face="normal" font="default" size="100%">Skiello, G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Influence of a new virostatic compound on the induction of enzymes in rat liver.</style></title><secondary-title><style face="normal" font="default" size="100%">Arzneimittelforschung</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Arzneimittelforschung</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adrenalectomy</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antiviral Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Cortisone</style></keyword><keyword><style  face="normal" font="default" size="100%">Culture Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Dose-Response Relationship, Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Induction</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Imidazoles</style></keyword><keyword><style  face="normal" font="default" size="100%">Liver</style></keyword><keyword><style  face="normal" font="default" size="100%">Piperazines</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Tryptophan Oxygenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine Transaminase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">25</style></volume><pages><style face="normal" font="default" size="100%">1426-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/24?dopt=Abstract</style></custom1></record></records></xml>