Macromolecular Interactions of Lipoprotein Lipase (LPL).
Angiopoietin-like protein
Apolipoprotein
CryoEM
Helix
Heparin
Lipase maturation factor 1
Lipoprotein lipase
Syndecan-1
Triglyceride
Journal
Sub-cellular biochemistry
ISSN: 0306-0225
Titre abrégé: Subcell Biochem
Pays: United States
ID NLM: 0316571
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
4
7
2024
pubmed:
4
7
2024
entrez:
4
7
2024
Statut:
ppublish
Résumé
Lipoprotein lipase (LPL) is a critical enzyme in humans that provides fuel to peripheral tissues. LPL hydrolyzes triglycerides from the cores of lipoproteins that are circulating in plasma and interacts with receptors to mediate lipoprotein uptake, thus directing lipid distribution via catalytic and non-catalytic functions. Functional losses in LPL or any of its myriad of regulators alter lipid homeostasis and potentially affect the risk of developing cardiovascular disease-either increasing or decreasing the risk depending on the mutated protein. The extensive LPL regulatory network tunes LPL activity to allocate fatty acids according to the energetic needs of the organism and thus is nutritionally responsive and tissue dependent. Multiple pharmaceuticals in development manipulate or mimic these regulators, demonstrating their translational importance. Another facet of LPL biology is that the oligomeric state of the enzyme is also central to its regulation. Recent structural studies have solidified the idea that LPL is regulated not only by interactions with other binding partners but also by self-associations. Here, we review the complexities of the protein-protein and protein-lipid interactions that govern LPL structure and function.
Identifiants
pubmed: 38963487
doi: 10.1007/978-3-031-58843-3_8
doi:
Substances chimiques
Lipoprotein Lipase
EC 3.1.1.34
Triglycerides
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
139-179Informations de copyright
© 2024. The Author(s), under exclusive license to Springer Nature Switzerland AG.
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