Perilipin-1

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]

Function

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.

Clinical significance

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
Perilipin
Identifiers
SymbolPerilipin
PfamPF03036
InterProIPR004279

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]

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gollark: > [Edit] Worth to note is that Gradual was designed to be a strategy that outperforms Tit for Tat. It has similar properties in that it is willing to cooperate and retaliates against a defecting opponent. Unlike Tit for Tat, which only has a memory of the last round played, Gradual will remember the complete interaction and defect the number of times the opponent has defected so far. It will offer mutual cooperation afterwards again, though.
gollark: The *description* of "Gradual" is pretty understandable.
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References
  1. "Entrez Gene: PLIN perilipin".
  2. 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. 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. telegraph.co.uk, 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
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