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André Bensadoun
Researcher at Cornell University
Publications - 151
Citations - 11432
André Bensadoun is an academic researcher from Cornell University. The author has contributed to research in topics: Lipoprotein lipase & GPIHBP1. The author has an hindex of 53, co-authored 151 publications receiving 10986 citations. Previous affiliations of André Bensadoun include University of California, San Diego & University of California, San Francisco.
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Journal ArticleDOI
Secretion and degradation of lipoprotein lipase in cultured adipocytes. Binding of lipoprotein lipase to membrane heparan sulfate proteoglycans is necessary for degradation.
TL;DR: The hypothesis that the release of lipoprotein lipase from its receptor prevents its internalization and degradation and enhances enzyme efflux from the adipocyte is supported.
Journal ArticleDOI
Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defects.
Remco Franssen,Stephen G. Young,Frank Peelman,Jozef Hertecant,Jeroen A. Sierts,Alinda W. M. Schimmel,André Bensadoun,John J.P. Kastelein,Loren G. Fong,Geesje M. Dallinga-Thie,Anne P. Beigneux +10 more
TL;DR: It is shown that homozygosity for the C65Y or Q115P mutations is associated with low levels of LPL in the postheparin plasma, demonstrating that GPIHBP1 is important for plasma triglyceride metabolism in humans.
Journal ArticleDOI
The form of absorption of lipids in the chicken, Gallus domesticus.
André Bensadoun,Alan Rothfeld +1 more
TL;DR: It has been demonstrated with the use of a functionally hepatectomized preparation and in the presence of a lipoprotein lipase inhibitor, Triton WR 1339, that, in the chicken, long chain fatty acids are absorbed in the form of triglycerides as the major component of alipoprotein of density less than 1.006.
Journal ArticleDOI
Hepatic lipase is abundant on both hepatocyte and endothelial cell surfaces in the liver.
TL;DR: The distribution suggests that a majority of the hepatic lipase produced by the liver is associated with hepatocyte surfaces, consistent with the functions of this enzyme in lipoprotein metabolism.
Journal ArticleDOI
Angiopoietin-like 4 promotes intracellular degradation of lipoprotein lipase in adipocytes.
Wieneke Dijk,Anne P. Beigneux,Mikael Larsson,André Bensadoun,Stephen G. Young,Sander Kersten,Sander Kersten +6 more
TL;DR: It is concluded that ANGPTL4 promotes loss of intracellular LPL by stimulating LPL degradation after LPL processing in the ER.