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LPIN1

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Template:PBB Lipin-1 is a protein that in humans is encoded by the LPIN1 gene.[1][2][3][4]

Function

Lipin-1 has phosphatidate phosphatase activity.[5][6][7]

Clinical significance

This gene represents a candidate gene for human lipodystrophy, characterized by loss of body fat, fatty liver, hypertriglyceridemia, and insulin resistance. Mouse studies suggest that this gene functions during normal adipose tissue development and may also play a role in human triglyceride metabolism.[4]

References

  1. ^ Peterfy M, Phan J, Xu P, Reue K (Jan 2001). "Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin". Nat Genet. 27 (1): 121–4. doi:10.1038/83685. PMID 11138012.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (Nov 1996). "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 3 (1): 17–24. doi:10.1093/dnares/3.1.17. PMID 8724849.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Finck BN, Gropler MC, Chen Z, Leone TC, Croce MA, Harris TE, Lawrence JC Jr, Kelly DP (Sep 2006). "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha regulatory pathway". Cell Metab. 4 (3): 199–210. doi:10.1016/j.cmet.2006.08.005. PMID 16950137.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ a b "Entrez Gene: LPIN1 lipin 1".
  5. ^ Han GS, Wu WI, Carman GM (April 2006). "The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme". J. Biol. Chem. 281 (14): 9210–8. doi:10.1074/jbc.M600425200. PMC 1424669. PMID 16467296.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  6. ^ Donkor J, Sariahmetoglu M, Dewald J, Brindley DN, Reue K (February 2007). "Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns". J. Biol. Chem. 282 (6): 3450–7. doi:10.1074/jbc.M610745200. PMID 17158099.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  7. ^ Harris TE, Huffman TA, Chi A, Shabanowitz J, Hunt DF, Kumar A, Lawrence JC Jr. (January 2007). "Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1". J. Biol. Chem. 282 (1): 277–86. doi:10.1074/jbc.M609537200. PMID 17105729.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)

Further reading

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