<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hideaki Miyoshi</style></author><author><style face="normal" font="default" size="100%">James W Perfield</style></author><author><style face="normal" font="default" size="100%">Martin S Obin</style></author><author><style face="normal" font="default" size="100%">Andrew S Greenberg</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Adipose triglyceride lipase regulates basal lipolysis and lipid droplet size in adipocytes</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Cellular Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adenoviridae</style></keyword><keyword><style  face="normal" font="default" size="100%">Adipocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Carboxylic Ester Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cyclic AMP-Dependent Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphoproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sterol Esterase</style></keyword><keyword><style  face="normal" font="default" size="100%">Transgenic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/18980248</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">6</style></number><volume><style face="normal" font="default" size="100%">105</style></volume><pages><style face="normal" font="default" size="100%">1430–1436</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In adipocytes, lipid droplet {(LD)} size reflects a balance of triglyceride synthesis (lipogenesis) and hydrolysis (lipolysis). Perilipin A {(Peri} A) is the most abundant phosphoprotein on the surface of adipocyte {LDs} and has a crucial role in lipid storage and lipolysis. Adipose triglyceride lipase {(ATGL)} and hormone-sensitive lipase {(HSL)} are the major rate-determining enzymes for lipolysis in adipocytes. Each of these proteins {(Peri} A, {ATGL,} and {HSL)} has been demonstrated to regulate lipid storage and release in the adipocyte. However, in the absence of protein kinase A {(PKA)} stimulation (basal state), the lipases {(ATGL} and {HSL)} are located mainly in the cytoplasm, and their contribution to basal rates of lipolysis and influence on {LD} size are poorly understood. In this study, we utilize an adenoviral system to knockdown or overexpress {ATGL} and {HSL} in an engineered model system of adipocytes in the presence or absence of Peri A. We are able to demonstrate in our experimental model system that in the basal state, {LD} size, triglyceride storage, and fatty acid release are mainly influenced by the expression of {ATGL.} These results demonstrate for the first time the relative contributions of {ATGL,} {HSL,} and Peri A on determination of {LD} size in the absence of {PKA} stimulation.</style></abstract><notes><style face="normal" font="default" size="100%">{PMID:} 18980248</style></notes></record></records></xml>