Molecular mechanisms regulating hormone-sensitive lipase and lipolysis.
By C. Holm. Biochemical Society Transactions, 2003
679 citations recorded by the source corpus.
Subfields: Biochemistry, Molecular Biology, Surgery
View Paper: https://www.semanticscholar.org/paper/eeda8f7fc7d37625a773841fdd35e70632b80a4b
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Citations in the corpus
- Meeting the energetic demands of insect diapause: nutrient storage and utilization. (2007, background): “While best known for affecting metabolic flux in mammalian systems, PKA-like enzymes have been identified in multiple insect species where they appear to play similar roles (Foster et al., 1984; Holm et al., 2000; Pan and Hardie, 2002; Pfister and Storey, 2002; Andersson et al., 2004; Apfeld et al.,”
- Lipolysis – A highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores (2011, background): “The hydrolysis of the primary and secondary ester bonds between long chain fatty acids and the glycerol backbone in TAG is called ‘‘lipolysis’’ and depends on specific hydrolases commonly designated lipases [8,9].”
- Regulatory role for the arginine-nitric oxide pathway in metabolism of energy substrates. (2006, background): “Glucagon (in young rodents but not in humans) and h-adrenergic agonists (including catecholamines) increase intracellular cAMP levels by activating adenylyl cyclase, whereas insulin reduces intracellular cAMP concentrations by stimulating phosphodiesterase-3B activity [50].”
- Regulation of lipolysis in adipocytes. (2007, neutral): “Relative fatty acyl hydrolase activity of HSL in vitro is elevenfold greater against DAG than TAG, and twofold greater against CEs (51).”