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'''Figure 1:''' Conversion of triglyceride to diglyceride by LPL.
'''Figure 1:''' Conversion of triglyceride to diglyceride by LPL.
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LPL was identified more than 60 years ago and studied by biochemists and physiologists intensely since. It wasn’t until recently that LPL’s detailed structure was determined due to LPL’s hydrolase domain susceptibility to unfolding. LMF1 and GPIHBP1, '''glycosylphosphatidylinositol-anchored high-density lipoprotein–binding protein 1''' , were discovered to be required for proper folding and enzymatic activity of LPL. LMF1,''' lipase maturation factor 1''', is a chaperone protein that is responsible for proper folding and secretion of LPL. Through the use of X-ray crystallography, it was also discovered that LPL is a monomer rather than the previously believed homodimer <ref name="Birrane">PMID:30559189</ref>.
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LPL was identified more than 60 years ago and studied by biochemists and physiologists intensely since. It wasn’t until recently that LPL’s detailed structure was determined due to LPL’s hydrolase domain susceptibility to unfolding. LMF1 and GPIHBP1, '''glycosylphosphatidylinositol-anchored high-density lipoprotein–binding protein 1''' , were discovered to be required for proper folding and enzymatic activity of LPL. LMF1,''' lipase maturation factor 1''', is a [http://en.wikipedia.org/wiki/Chaperone_(protein) chaperone protein] that is responsible for proper folding and secretion of LPL. Through the use of X-ray crystallography, it was also discovered that LPL is a monomer rather than the previously believed homodimer <ref name="Birrane">PMID:30559189</ref>.
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Revision as of 15:54, 27 April 2021

Lipoprotein Lipase (LPL) complexed with GPIHBP1

Lipoprotein Lipase - 6E7K

Drag the structure with the mouse to rotate

References

  1. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 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:http://dx.doi.org/10.1073/pnas.1817984116
  2. 2.0 2.1 Wong H, Davis RC, Thuren T, Goers JW, Nikazy J, Waite M, Schotz MC. Lipoprotein lipase domain function. J Biol Chem. 1994 Apr 8;269(14):10319-23. PMID:8144612
  3. 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:http://dx.doi.org/10.1073/pnas.1820171116
  4. 4.0 4.1 Falko JM. Familial Chylomicronemia Syndrome: A Clinical Guide For Endocrinologists. Endocr Pract. 2018 Aug;24(8):756-763. doi: 10.4158/EP-2018-0157. PMID:30183397 doi:http://dx.doi.org/10.4158/EP-2018-0157


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