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Mariusz P Kowalewski - One of the best experts on this subject based on the ideXlab platform.
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, Mariusz P KowalewskiAbstract:ABSTRACT There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/plac...
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, B Hoffmann, Mariusz P KowalewskiAbstract:There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/placental expression of PGFS (AKR1C3) was identified in the superficial uterine glands throughout gestation and in the trophoblast cells within the feto-maternal contact zone during placentation, suggesting a possible role for PGFS (AKR1C3) in the trophoblast invasion. Utero-placental HPGD was up-regulated until postimplantation, lower at midgestation, and greatly suppressed at prepartum. Expression was routinely identified in the endometrial surface and glandular epithelia, and positive signals were also observed in the trophoblast cells at the feto-maternal contact zone. The Biochemical Activity of recombinant PGFS (AKR1C3) and HPGD was confirmed after its expression in a heterologous system. The colocalization of HPGD with PGFS (AKR1C3) expression suggests a modulatory role for HPGD as a gatekeeper of the supply of prostaglandin in the pregnant canine uterus.
Aykut Gram - One of the best experts on this subject based on the ideXlab platform.
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, Mariusz P KowalewskiAbstract:ABSTRACT There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/plac...
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, B Hoffmann, Mariusz P KowalewskiAbstract:There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/placental expression of PGFS (AKR1C3) was identified in the superficial uterine glands throughout gestation and in the trophoblast cells within the feto-maternal contact zone during placentation, suggesting a possible role for PGFS (AKR1C3) in the trophoblast invasion. Utero-placental HPGD was up-regulated until postimplantation, lower at midgestation, and greatly suppressed at prepartum. Expression was routinely identified in the endometrial surface and glandular epithelia, and positive signals were also observed in the trophoblast cells at the feto-maternal contact zone. The Biochemical Activity of recombinant PGFS (AKR1C3) and HPGD was confirmed after its expression in a heterologous system. The colocalization of HPGD with PGFS (AKR1C3) expression suggests a modulatory role for HPGD as a gatekeeper of the supply of prostaglandin in the pregnant canine uterus.
Alois Boos - One of the best experts on this subject based on the ideXlab platform.
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, Mariusz P KowalewskiAbstract:ABSTRACT There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/plac...
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, B Hoffmann, Mariusz P KowalewskiAbstract:There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/placental expression of PGFS (AKR1C3) was identified in the superficial uterine glands throughout gestation and in the trophoblast cells within the feto-maternal contact zone during placentation, suggesting a possible role for PGFS (AKR1C3) in the trophoblast invasion. Utero-placental HPGD was up-regulated until postimplantation, lower at midgestation, and greatly suppressed at prepartum. Expression was routinely identified in the endometrial surface and glandular epithelia, and positive signals were also observed in the trophoblast cells at the feto-maternal contact zone. The Biochemical Activity of recombinant PGFS (AKR1C3) and HPGD was confirmed after its expression in a heterologous system. The colocalization of HPGD with PGFS (AKR1C3) expression suggests a modulatory role for HPGD as a gatekeeper of the supply of prostaglandin in the pregnant canine uterus.
Urs Buchler - One of the best experts on this subject based on the ideXlab platform.
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, Mariusz P KowalewskiAbstract:ABSTRACT There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/plac...
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biosynthesis and degradation of canine placental prostaglandins prepartum changes in expression and function of prostaglandin f2alpha synthase pgfs akr1c3 and 15 hydroxyprostaglandin dehydrogenase hpgd
2013Co-Authors: Aykut Gram, Urs Buchler, Alois Boos, B Hoffmann, Mariusz P KowalewskiAbstract:There is no distinct explanation of the mechanism for the prepartal prostaglandin F2alpha (PGF2alpha) increase in pregnant dogs. Although the PGF2alpha-synthase (PGFS [AKR1C3]) mRNA expression and localization profiles have been previously investigated in canine utero/placental compartments, the availability and Biochemical Activity of the PGFS (AKR1C3) protein remain unknown. In order to better understand the regulation of canine uterine PGF2alpha availability and eventual prepartum release in luteolytic amounts in dogs, canine-specific PGFS (AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD) antibodies were generated and used to characterize the expression, cellular localization, and Biochemical properties of PGFS (AKR1C3) and HPGD in the utero/placental compartments and corpus luteum throughout pregnancy and at prepartum luteolysis. PGFS (AKR1C3) expression was weak or absent in luteal samples. Uterine PGFS (AKR1C3) was up-regulated postimplantation and declined prepartum. The utero/placental expression of PGFS (AKR1C3) was identified in the superficial uterine glands throughout gestation and in the trophoblast cells within the feto-maternal contact zone during placentation, suggesting a possible role for PGFS (AKR1C3) in the trophoblast invasion. Utero-placental HPGD was up-regulated until postimplantation, lower at midgestation, and greatly suppressed at prepartum. Expression was routinely identified in the endometrial surface and glandular epithelia, and positive signals were also observed in the trophoblast cells at the feto-maternal contact zone. The Biochemical Activity of recombinant PGFS (AKR1C3) and HPGD was confirmed after its expression in a heterologous system. The colocalization of HPGD with PGFS (AKR1C3) expression suggests a modulatory role for HPGD as a gatekeeper of the supply of prostaglandin in the pregnant canine uterus.
Kostya Ostrikov - One of the best experts on this subject based on the ideXlab platform.
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cold atmospheric plasma activated water as a prospective disinfectant the crucial role of peroxynitrite
2018Co-Authors: Renwu Zhou, Rusen Zhou, Karthika Prasad, Zhi Fang, Robert Speight, Kateryna Bazaka, Kostya OstrikovAbstract:The socio-economic, environmental, and health implications of diseases caused by pathogenic microorganisms and their treatment using conventional antimicrobials are significant. The increasing resistance to antibiotics and detrimental biological side effects of many common antibiotics on human health and on the ecosystem have driven the search for new cost-effective and highly-efficient sterilization treatments and agents that are more environmentally benign. Plasma activated water (PAW), a product of cold atmospheric plasma reacting with water, is a promising broad-spectrum biocidal agent whose Biochemical Activity is attributed to the presence of a rich diversity of highly reactive oxygen and nitrogen species (RONS). The transient Activity of PAW, where PAW reverts to water within days of storage and application, suggests that it can become a green alternative to conventional chemical treatment methods, yet the issues of scale up and the not fully understood mechanism of Activity remain. In this study, we sought to explore the antibiotic potential of PAW generated from a plasma jet in a continuous flow reactor and determine the individual and combined contribution of thus-generated reactive chemistries in PAW for organism inactivation. Treatment of Escherichia coli with PAW led to more than a 4-log reduction, while exposure to an equivalent single dose of hydrogen peroxide (H2O2), nitrate (NO3−) or nitrite (NO2−) to that found in PAW failed to attain the same level of reduction. Peroxynitrite was identified as a critical bioactive species, particularly under acidic conditions, originating from the synergistic plasma effects (like the reactions of H2O2, NO3−, NO2− and other existing short-lived species like OH radicals in PAW). This research successfully demonstrated the possibility of PAW being an effective environmentally benign disinfectant, the Activity of which is closely linked to the generation of peroxynitrite, providing much needed insights into the fundamental aspects of PAW chemistry required for optimisation of the Biochemical Activity of PAW and translation of this decontamination strategy into real life applications.