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==Introduction== | ==Introduction== | ||
<scene name='87/877513/Original_scene/1'>Lipoprotein Lipase</scene>(LPL) is an important enzyme for the breakdown of triglycerides in the body (Figure 1).<ref name=”Arora”>PMID:31072929</ref> [[Image:Simple_mech.png|400 px|right|thumb|Figure 1: breakdown of a triglyceride into a diglyceride and creation of one free fatty acid by LPL]] A [https://en.wikipedia.org/wiki/Lipase lipase] is an enzyme that is capable of catalyzing the [https://en.wikipedia.org/wiki/Hydrolysis hydrolysis] of fats/lipids which are consumed through oils. It is encoded by the [https://www.genecards.org/cgi-bin/carddisp.pl?gene=LPL p22 region in chromosome 8]. Once synthesized, it is secreted into the interstitial space in several tissues. The main site of action for <scene name='87/877513/Original_scene/1'>LPL</scene> is in the [https://www.pnas.org/content/pnas/116/5/1480/F1.large.jpg capillary lumen] within muscle and adipose tissues.<ref name=”Birrane”>PMID:30559189</ref> The function of this lipase is to hydrolyze [https://en.wikipedia.org/wiki/Triglyceride triglycerides] of very-low-density lipoproteins ([https://qph.fs.quoracdn.net/main-qimg-8e874e647baeb69b00203c47165247e2 VLDL]) and to aid in the delivery of lipid nutrients to vital tissues.< | <scene name='87/877513/Original_scene/1'>Lipoprotein Lipase</scene>(LPL) is an important enzyme for the breakdown of triglycerides in the body (Figure 1).<ref name=”Arora”>PMID:31072929</ref> [[Image:Simple_mech.png|400 px|right|thumb|Figure 1: breakdown of a triglyceride into a diglyceride and creation of one free fatty acid by LPL]] A [https://en.wikipedia.org/wiki/Lipase lipase] is an enzyme that is capable of catalyzing the [https://en.wikipedia.org/wiki/Hydrolysis hydrolysis] of fats/lipids which are consumed through oils. It is encoded by the [https://www.genecards.org/cgi-bin/carddisp.pl?gene=LPL p22 region in chromosome 8]. Once synthesized, it is secreted into the interstitial space in several tissues. The main site of action for <scene name='87/877513/Original_scene/1'>LPL</scene> is in the [https://www.pnas.org/content/pnas/116/5/1480/F1.large.jpg capillary lumen] within muscle and adipose tissues.<ref name=”Birrane”>PMID:30559189</ref> The function of this lipase is to hydrolyze [https://en.wikipedia.org/wiki/Triglyceride triglycerides] of very-low-density lipoproteins ([https://qph.fs.quoracdn.net/main-qimg-8e874e647baeb69b00203c47165247e2 VLDL]) and to aid in the delivery of lipid nutrients to vital tissues.</ref> | ||
Revision as of 02:10, 28 April 2021
Lipoprotein Lipase coupled with GPIHBP1
<StructureSection load='6ob0' size='350' side='right' caption='Lipoprotein Lipase PDB' scene='87/877513/Original_scene/1'>
Introduction
Lipoprotein Lipase(LPL) is an important enzyme for the breakdown of triglycerides in the body (Figure 1).[1]

A lipase is an enzyme that is capable of catalyzing the hydrolysis of fats/lipids which are consumed through oils. It is encoded by the p22 region in chromosome 8. Once synthesized, it is secreted into the interstitial space in several tissues. The main site of action for LPL is in the capillary lumen within muscle and adipose tissues.[2] The function of this lipase is to hydrolyze triglycerides of very-low-density lipoproteins (VLDL) and to aid in the delivery of lipid nutrients to vital tissues.</ref>
- ↑ Arora R, Nimonkar AV, Baird D, Wang C, Chiu CH, Horton PA, Hanrahan S, Cubbon R, Weldon S, Tschantz WR, Mueller S, Brunner R, Lehr P, Meier P, Ottl J, Voznesensky A, Pandey P, Smith TM, Stojanovic A, Flyer A, Benson TE, Romanowski MJ, Trauger JW. Structure of lipoprotein lipase in complex with GPIHBP1. Proc Natl Acad Sci U S A. 2019 May 21;116(21):10360-10365. doi:, 10.1073/pnas.1820171116. Epub 2019 May 9. PMID:31072929 doi:https://dx.doi.org/10.1073/pnas.1820171116
- ↑ Birrane G, Beigneux AP, Dwyer B, Strack-Logue B, Kristensen KK, Francone OL, Fong LG, Mertens HDT, Pan CQ, Ploug M, Young SG, Meiyappan M. Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis. Proc Natl Acad Sci U S A. 2018 Dec 17. pii: 1817984116. doi:, 10.1073/pnas.1817984116. PMID:30559189 doi:https://dx.doi.org/10.1073/pnas.1817984116