低血脂样本文章.pdfVIP

Research article Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans 1 1,2 3 4,5 Stefano Romeo, Wu Yin, Julia Kozlitina, Len A. Pennacchio, 6 1,2 1,7 Eric Boerwinkle, Helen H. Hobbs, and Jonathan C. Cohen 1Donald W. Reynolds Cardiovascular Clinical Research Center and Eugene McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center, Dallas, Texas, USA. 2Howard Hughes Medical Center, University of Texas Southwestern Medical Center, Dallas, Texas, USA. 3 Department of Statistical Sciences, Southern Methodist University, Dallas, Texas, USA. 4Genomics Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA. 5 US Department of Energy Joint Genome Institute, Walnut Creek, California, USA. 6Human Genetics Center and Institute for Molecular Medicine, University of Texas Health Science Center, Houston, Texas, USA. 7Center for Human Nutrition, University of Texas Southwestern Medical Center, Dallas, Texas, USA. The relative activity of lipoprotein lipase (LPL) in different tissues controls the partitioning of lipoprotein- derived fatty acids between sites of fat storage (adipose tissue) and oxidation (heart and skeletal muscle). Here we used a reverse genetic strategy to test the hypothesis that 4 angiopoietin-like proteins (ANGPTL3, -4, -5, and -6) play key roles in triglyceride (TG) metabolism in humans. We re-sequenced the coding regions of the genes encoding th