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Perilipin, also known as lipid droplet-associated protein, Perilipin 1, or PLIN, is a protein that, in humans, is encoded by the PLIN gene.[1] The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.[2]


Perilipin is a protein that coats lipid droplets in adipocytes,[3] the fat-storing cells in adipose tissue. Perilipin acts as a protective coating from the body’s natural lipases, such as hormone-sensitive lipase,[4] which break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis.[2] In humans, perilipin is expressed in three different isoforms, A, B, and C, and perilipin A is the most abundant protein associated with the adipocyte lipid droplets.[5]

Perilipin is hyperphosphorylated by PKA following β-adrenergic receptor activation.[2] Phosphorylated perilipin changes conformation, exposing the stored lipids to hormone-sensitive lipase-mediated lipolysis. Although PKA also phosphorylates hormone-sensitive lipase, which can increase its activity, the more than 50-fold increase in fat mobilization (triggered by epinephrine) is primarily due to perilipin phosphorylation[citation needed].

Clinical significance[edit]

Perilipin is an important regulator of lipid storage.[2] Perilipin expression is elevated in obese animals and humans. Perilipin-null mice eat more food than wild-type mice, but gain 1/3 less fat than wild-type mice on the same diet; perilipin-null mice are thinner, with more lean muscle mass.[6] Perilipin-null mice also exhibit enhanced leptin production and a greater tendency to develop insulin resistance than wild-type mice.

Polymorphisms in the human perilipin (PLIN) gene have been associated with variance in body-weight regulation and may be a genetic influence on obesity risk in humans.[7] In particular, variants 13041A>G and 14995A>T have been associated with increased risk of obesity in women and 11482G>A has been associated with decreased perilipin expression and increased lipolysis in women.[8][9]

Perilipin family of proteins[edit]


Perilipin is part of a gene family with five currently-known members. In vertebrates, closely related genes include adipophilin (also known as adipose differentiation-related protein or Perilipin 2), TIP47 (Perilipin 3), Perilipin 4 and Perilipin 5 (also called MLDP, LSDP5, or OXPAT). Insects express related proteins, LSD1 and LSD2, in fat bodies.[5] The yeast Saccharomyces cerevisiae expresses PLN1 (formerly PET10), that stabilizes lipid droplets and aids in their assembly.[10]


  1. ^ "Entrez Gene: PLIN perilipin".
  2. ^ a b c d Mobilization and Cellular Uptake of Stored Fats (with Animation)
  3. ^ Greenberg AS, Egan JJ, Wek SA, Garty NB, Blanchette-Mackie EJ, Londos C (June 1991). "Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets". J. Biol. Chem. 266 (17): 11341–6. PMID 2040638.
  4. ^ Wong K (2000-11-29). "Making Fat-proof Mice". Scientific American. Retrieved 2009-05-22.
  5. ^ a b Brasaemle DL, Subramanian V, Garcia A, Marcinkiewicz A, Rothenberg A (June 2009). "Perilipin A and the control of triacylglycerol metabolism". Mol. Cell. Biochem. 326 (1–2): 15–21. doi:10.1007/s11010-008-9998-8. PMID 19116774.
  6. ^, 19 June 2001, Highfield, Roger (2000-11-29). "Couch potato mice discover the lazy way to stay slim". The Daily Telegraph. London. Retrieved 2008-09-03.
  7. ^ Soenen S, Mariman EC, Vogels N, Bouwman FG, den Hoed M, Brown L, Westerterp-Plantenga MS (March 2009). "Relationship between perilipin gene polymorphisms and body weight and body composition during weight loss and weight maintenance". Physiol. Behav. 96 (4–5): 723–8. doi:10.1016/j.physbeh.2009.01.011. PMID 19385027.
  8. ^ Qi L, Shen H, Larson I, Schaefer EJ, Greenberg AS, Tregouet DA, Corella D, Ordovas JM (November 2004). "Gender-specific association of a perilipin gene haplotype with obesity risk in a white population". Obes. Res. 12 (11): 1758–65. doi:10.1038/oby.2004.218. PMID 15601970.
  9. ^ Corella D, Qi L, Sorlí JV, Godoy D, Portolés O, Coltell O, Greenberg AS, Ordovas JM (September 2005). "Obese subjects carrying the 11482G>A polymorphism at the perilipin locus are resistant to weight loss after dietary energy restriction". J. Clin. Endocrinol. Metab. 90 (9): 5121–6. doi:10.1210/jc.2005-0576. PMID 15985482.
  10. ^ Gao, Qiang; Binns, Derk D.; Kinch, Lisa N.; Grishin, Nick V.; Ortiz, Natalie; Chen, Xiao; Goodman, Joel M. (2017-10-02). "Pet10p is a yeast perilipin that stabilizes lipid droplets and promotes their assembly". The Journal of Cell Biology. 216 (10): 3199–3217. doi:10.1083/jcb.201610013. ISSN 1540-8140. PMC 5626530. PMID 28801319.

Further reading[edit]