Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets

<p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p< Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Rønning Helle [verfasserIn] Osmundsen Harald [verfasserIn] Svindland Aud [verfasserIn] Brodal Bjørn P [verfasserIn] Eliassen Knut A [verfasserIn] Djurovic Srdjan [verfasserIn] Berg Kåre [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2005

Übergeordnetes Werk:	In: Lipids in Health and Disease - BMC, 2003, 4(2005), 1, p 23
Übergeordnetes Werk:	volume:4 ; year:2005 ; number:1, p 23

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1186/1476-511X-4-23

Katalog-ID:	DOAJ065904354

Internformat


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520			\|a <p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p<
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912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
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912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
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912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
951			\|a AR
952			\|d 4 \|j 2005 \|e 1, p 23

Indexfelder

author_variant	r h rh o h oh s a sa b b p bbp e k a eka d s ds b k bk
matchkey_str	article:1476511X:2005----::ciiyfeoioaezmsnlvloplaieilarngn
hierarchy_sort_str	2005
callnumber-subject-code	RC
publishDate	2005
allfields	10.1186/1476-511X-4-23 doi (DE-627)DOAJ065904354 (DE-599)DOAJ7d0f209f7c514954bd474942956fbc2c DE-627 ger DE-627 rakwb eng RC620-627 Rønning Helle verfasserin aut Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p< Nutritional diseases. Deficiency diseases Osmundsen Harald verfasserin aut Svindland Aud verfasserin aut Brodal Bjørn P verfasserin aut Eliassen Knut A verfasserin aut Djurovic Srdjan verfasserin aut Berg Kåre verfasserin aut In Lipids in Health and Disease BMC, 2003 4(2005), 1, p 23 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:4 year:2005 number:1, p 23 https://doi.org/10.1186/1476-511X-4-23 kostenfrei https://doaj.org/article/7d0f209f7c514954bd474942956fbc2c kostenfrei http://www.lipidworld.com/content/4/1/23 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1, p 23
spelling	10.1186/1476-511X-4-23 doi (DE-627)DOAJ065904354 (DE-599)DOAJ7d0f209f7c514954bd474942956fbc2c DE-627 ger DE-627 rakwb eng RC620-627 Rønning Helle verfasserin aut Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p< Nutritional diseases. Deficiency diseases Osmundsen Harald verfasserin aut Svindland Aud verfasserin aut Brodal Bjørn P verfasserin aut Eliassen Knut A verfasserin aut Djurovic Srdjan verfasserin aut Berg Kåre verfasserin aut In Lipids in Health and Disease BMC, 2003 4(2005), 1, p 23 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:4 year:2005 number:1, p 23 https://doi.org/10.1186/1476-511X-4-23 kostenfrei https://doaj.org/article/7d0f209f7c514954bd474942956fbc2c kostenfrei http://www.lipidworld.com/content/4/1/23 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1, p 23
allfields_unstemmed	10.1186/1476-511X-4-23 doi (DE-627)DOAJ065904354 (DE-599)DOAJ7d0f209f7c514954bd474942956fbc2c DE-627 ger DE-627 rakwb eng RC620-627 Rønning Helle verfasserin aut Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p< Nutritional diseases. Deficiency diseases Osmundsen Harald verfasserin aut Svindland Aud verfasserin aut Brodal Bjørn P verfasserin aut Eliassen Knut A verfasserin aut Djurovic Srdjan verfasserin aut Berg Kåre verfasserin aut In Lipids in Health and Disease BMC, 2003 4(2005), 1, p 23 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:4 year:2005 number:1, p 23 https://doi.org/10.1186/1476-511X-4-23 kostenfrei https://doaj.org/article/7d0f209f7c514954bd474942956fbc2c kostenfrei http://www.lipidworld.com/content/4/1/23 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1, p 23
allfieldsGer	10.1186/1476-511X-4-23 doi (DE-627)DOAJ065904354 (DE-599)DOAJ7d0f209f7c514954bd474942956fbc2c DE-627 ger DE-627 rakwb eng RC620-627 Rønning Helle verfasserin aut Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p< Nutritional diseases. Deficiency diseases Osmundsen Harald verfasserin aut Svindland Aud verfasserin aut Brodal Bjørn P verfasserin aut Eliassen Knut A verfasserin aut Djurovic Srdjan verfasserin aut Berg Kåre verfasserin aut In Lipids in Health and Disease BMC, 2003 4(2005), 1, p 23 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:4 year:2005 number:1, p 23 https://doi.org/10.1186/1476-511X-4-23 kostenfrei https://doaj.org/article/7d0f209f7c514954bd474942956fbc2c kostenfrei http://www.lipidworld.com/content/4/1/23 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1, p 23
allfieldsSound	10.1186/1476-511X-4-23 doi (DE-627)DOAJ065904354 (DE-599)DOAJ7d0f209f7c514954bd474942956fbc2c DE-627 ger DE-627 rakwb eng RC620-627 Rønning Helle verfasserin aut Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p< Nutritional diseases. Deficiency diseases Osmundsen Harald verfasserin aut Svindland Aud verfasserin aut Brodal Bjørn P verfasserin aut Eliassen Knut A verfasserin aut Djurovic Srdjan verfasserin aut Berg Kåre verfasserin aut In Lipids in Health and Disease BMC, 2003 4(2005), 1, p 23 (DE-627)355987694 (DE-600)2091381-3 1476511X nnns volume:4 year:2005 number:1, p 23 https://doi.org/10.1186/1476-511X-4-23 kostenfrei https://doaj.org/article/7d0f209f7c514954bd474942956fbc2c kostenfrei http://www.lipidworld.com/content/4/1/23 kostenfrei https://doaj.org/toc/1476-511X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2005 1, p 23
language	English
source	In Lipids in Health and Disease 4(2005), 1, p 23 volume:4 year:2005 number:1, p 23
sourceStr	In Lipids in Health and Disease 4(2005), 1, p 23 volume:4 year:2005 number:1, p 23
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Nutritional diseases. Deficiency diseases
isfreeaccess_bool	true
container_title	Lipids in Health and Disease
authorswithroles_txt_mv	Rønning Helle @@aut@@ Osmundsen Harald @@aut@@ Svindland Aud @@aut@@ Brodal Bjørn P @@aut@@ Eliassen Knut A @@aut@@ Djurovic Srdjan @@aut@@ Berg Kåre @@aut@@
publishDateDaySort_date	2005-01-01T00:00:00Z
hierarchy_top_id	355987694
id	DOAJ065904354
language_de	englisch
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Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. 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author	Rønning Helle
spellingShingle	Rønning Helle misc RC620-627 misc Nutritional diseases. Deficiency diseases Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets
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topic_title	RC620-627 Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets
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title	Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets
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title_full	Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets
author_sort	Rønning Helle
journal	Lipids in Health and Disease
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author_browse	Rønning Helle Osmundsen Harald Svindland Aud Brodal Bjørn P Eliassen Knut A Djurovic Srdjan Berg Kåre
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doi_str_mv	10.1186/1476-511X-4-23
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title_sort	activity of peroxisomal enzymes, and levels of polyamines in lpa-transgenic mice on two different diets
callnumber	RC620-627
title_auth	Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets
abstract	<p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p<
abstractGer	<p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p<
abstract_unstemmed	<p<Abstract</p< <p<Background</p< <p<In man, elevated levels of plasma lipoprotein (a)(Lp(a)) is a cardiovascular risk factor, and oxidized phospholipids are believed to play a role as modulators of inflammatory processes such as atherosclerosis. Polyamines are potent antioxidants and anti-inflammatory agents. It was therefore of interest to examine polyamines and their metabolism in LPA transgenic mice.</p< <p<Concentration of the polyamines putrescine, spermidine and spermine as well as the activity of peroxisomal polyamine oxidase and two other peroxisomal enzymes, acyl-CoA oxidase and catalase were measured. The mice were fed either a standard diet or a diet high in fat and cholesterol (HFHC). Some of the mice in each feeding group were in addition given aminoguanidine (AG), a specific inhibitor of diamine oxidase, which catalyses degradation of putrescine, and also inhibits non-enzymatic glycosylation of protein which is implicated in the aetiology of atherosclerosis in diabetic patients. Non-transgenic mice were used as controls.</p< <p<Results</p< <p<Intestinal peroxisomal polyamine oxidase activity was significantly higher in LPA transgenic mice than in the non-transgenic mice, while intestinal peroxisomal catalase activity was significantly lower. Hepatic β-oxidation increased in Lp(a) transgenic mice fed the HFHC diet, but not in those on standard diet.</p< <p<Hepatic spermidine concentration was increased in all mice fed the HFHC diet compared to those fed a standard diet, while spermine concentration was decreased. With exception of the group fed only standard diet, transgenic mice showed a lower degree of hepatic steatosis than non-transgenic mice. AG had no significant effect on hepatic steatosis.</p< <p<Conclusion</p< <p<The present results indicate a connection between peroxisomal enzyme activity and the presence of the human LPA gene in the murine genome. The effect may be a result of changes in oxidative processes in lipid metabolism rather than resulting from a direct effect of the LPA construct on the peroximal gene expression.</p<
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title_short	Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets
url	https://doi.org/10.1186/1476-511X-4-23 https://doaj.org/article/7d0f209f7c514954bd474942956fbc2c http://www.lipidworld.com/content/4/1/23 https://doaj.org/toc/1476-511X
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Activity of peroxisomal enzymes, and levels of polyamines in LPA-transgenic mice on two different diets

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