The Experts below are selected from a list of 159 Experts worldwide ranked by ideXlab platform
Heiner Greten - One of the best experts on this subject based on the ideXlab platform.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:Abstract We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at ∼24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at approximately 24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
Rudolf Zechner - One of the best experts on this subject based on the ideXlab platform.
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mice lacking lipid droplet associated hydrolase a gene linked to human prostate cancer have normal CholEsterol Ester metabolism
Journal of Lipid Research, 2017Co-Authors: Nora Kory, Susanne Grond, Siddhesh S Kamat, Natalie Krahmer, Chandramohan Chitraju, Ping Zhou, Florian Frohlich, Ivana Semova, Christer S Ejsing, Rudolf ZechnerAbstract:Variations in the gene LDAH (C2ORF43), which encodes lipid droplet-associated hydrolase (LDAH), are among few loci associated with human prostate cancer. Homologs of LDAH have been identified as proteins of lipid droplets (LDs). LDs are cellular organelles that store neutral lipids, such as triacylglycerols and sterol Esters, as precursors for membrane components and as reservoirs of metabolic energy. LDAH is reported to hydrolyze CholEsterol Esters and to be important in macrophage CholEsterol Ester metabolism. Here, we confirm that LDAH is localized to LDs in several model systems. We generated a murine model in which Ldah is disrupted but found no evidence for a major function of LDAH in CholEsterol Ester or triacylglycerol metabolism in vivo, nor a role in energy or glucose metabolism. Our data suggest that LDAH is not a major CholEsterol Ester hydrolase, and an alternative metabolic function may be responsible for its possible effect on development of prostate cancer.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:Abstract We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at ∼24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at approximately 24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
Martin Merkel - One of the best experts on this subject based on the ideXlab platform.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:Abstract We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at ∼24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at approximately 24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
Franz Rinninger - One of the best experts on this subject based on the ideXlab platform.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:Abstract We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at ∼24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at approximately 24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
Jorg Heeren - One of the best experts on this subject based on the ideXlab platform.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:Abstract We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at ∼24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.
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inactive lipoprotein lipase lpl alone increases selective CholEsterol Ester uptake in vivo whereas in the presence of active lpl it also increases triglyceride hydrolysis and whole particle lipoprotein uptake
Journal of Biological Chemistry, 2002Co-Authors: Martin Merkel, Rudolf Zechner, Jorg Heeren, Wiebke Dudeck, Franz Rinninger, Herbert Radner, Jan L Breslow, Ira J Goldberg, Heiner GretenAbstract:We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective CholEsterol Ester uptake. In the current study, we have examined whether these functions can be performed by inactive LPL alone or require the presence of active LPL expressed in the same tissue. To study inactive LPL in the presence of active LPL in the same tissue, the Mck-N-LPL transgene was bred onto the heterozygous LPL-deficient (LPL1) background. At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. In adult mice, it reduced triglycerides by 40% and increased lipoprotein particle uptake into muscle by 60% and CholEsterol Ester uptake by 110%. To study inactive LPL alone, the Mck-N-LPL transgene was bred onto the LPL-deficient (LPL0) background. These mice die at approximately 24 h of age. At 18 h of age, in the absence of active LPL, inactive LPL expression did not diminish triglycerides nor did it result in the accumulation of muscle lipid droplets. To study inactive LPL in the absence of active LPL in the same tissue in adult animals, the Mck-N-LPL transgene was bred onto mice that only expressed active LPL in the heart (LPL0/He-LPL). In this case, Mck-N-LPL did not reduce triglycerides or increase the uptake of lipoprotein particles but did increase muscle uptake of chylomicron and very low density lipoprotein CholEsterol Ester by 40%. Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective CholEsterol Ester uptake. In the absence of active LPL in the same tissue, inactive LPL only mediates selective CholEsterol Ester uptake.