Some things just have to be done in vivo: GPIHBP1, caloric delivery, and the generation of remnant lipoproteins.
The recent discovery of a dysfunctional mutation of GPIHBP1 in a man with chylomicronemia implicates this protein in human physiology. GPIHBP1 can be placed in the larger context of other molecular participants in chylomicron docking and hydrolysis on microvascular endothelium, caloric delivery, and remnant lipoprotein generation. Critical questions include the regulation--and dysregulation--of these processes in states of overnutrition, underexertion, obesity, insulin resistance, and diabetes.
Williams
Kevin Jon
KJ
D000818:Animals; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D053298:Chylomicron Remnants / Q000235:genetics / Q000378:metabolism*; D042783:Endothelial Cells / Q000201:enzymology / Q000378:metabolism*; D002149:Energy Intake; D006720:Homozygote; D006801:Humans; D008072:Hyperlipoproteinemia Type I / Q000201:enzymology / Q000235:genetics; D015228:Hypertriglyceridemia / Q000201:enzymology / Q000235:genetics; D008071:Lipoprotein Lipase / Q000378:metabolism; D020125:Mutation, Missense; D010641:Phenotype; D011485:Protein Binding; D021381:Protein Transport; D018110:Receptors, Lipoprotein / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
D002352:Carrier Proteins; D053298:Chylomicron Remnants; C472779:GPI-HBP1 protein, mouse; C523701:GPIHBP1 protein, human; D018110:Receptors, Lipoprotein; D008071:Lipoprotein Lipase