Key result
Angiopoietin-like protein 4 (Angptl-4) converts catalytically active, dimeric lipoprotein lipase to inactive monomers, acting as a fasting-induced controller of LPL in adipose tissue.
Population
Rat adipose tissue and in vitro models studying lipoprotein lipase and Angiopoietin-like protein 4 interaction
Design
Preclinical
Authors
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Hypothesis-generating for LPL regulation in fasting; extends animal mechanistic data but leaves open human relevance.
Angptl-4 acts as a fasting-induced controller of LPL in adipose tissue by converting active LPL dimers into inactive monomers, providing mechanistic insight into lipoprotein metabolism regulation.
Sukonina et al. (2006) studied this question. Angiopoietin-like protein 4 (Angptl-4) was evaluated on Lipoprotein lipase (LPL) activity. Angiopoietin-like protein 4 (Angptl-4) converts catalytically active, dimeric lipoprotein lipase to inactive monomers, acting as a fasting-induced controller of LPL in adipose tissue.
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