Perilipin

PLIN1
Identifiers
Aliases PLIN1, FPLD4, PERI, PLIN, perilipin 1
External IDs OMIM: 170290 MGI: 1890505 HomoloGene: 2001 GeneCards: PLIN1
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

5346

103968

Ensembl

ENSG00000166819

ENSMUSG00000030546

UniProt

O60240

Q8CGN5

RefSeq (mRNA)

NM_001145311
NM_002666

NM_001113471
NM_175640

RefSeq (protein)

NP_001138783.1
NP_002657.3

NP_001106942.1
NP_783571.2

Location (UCSC) Chr 15: 89.66 – 89.68 Mb Chr 7: 79.72 – 79.73 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Perilipin, also known as lipid droplet-associated protein or PLIN, is a protein that, in humans, is encoded by the PLIN gene.[3] 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.[4]

Function

Perilipin is a protein that coats lipid droplets in adipocytes,[5] the fat-storing cells in adipose tissue. Perilipin acts as a protective coating from the body’s natural lipases, such as hormone-sensitive lipase,[6] which break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis.[4] 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.[7]

Perilipin is hyperphosphorylated by PKA following β-adrenergic receptor activation.[4] 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.[4] 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.[8] 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.[9] 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.[10][11]

Perilipin family of proteins

Perilipin
Identifiers
Symbol Perilipin
Pfam PF03036
InterPro IPR004279

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), TIP47, and LSDP5 (also called MLDP and OXPAT). Insects express related proteins, LSD1 and LSD2, in fat bodies.[7]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ "Entrez Gene: PLIN perilipin".
  4. 1 2 3 4 Mobilization and Cellular Uptake of Stored Fats (with Animation)
  5. ↑ 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.
  6. ↑ Wong K (2000-11-29). "Making Fat-proof Mice". Scientific American. Retrieved 2009-05-22.
  7. 1 2 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 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.

Further reading

  • Brasaemle DL (December 2007). "Thematic review series: adipocyte biology. The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis". J. Lipid Res. 48 (12): 2547–59. doi:10.1194/jlr.R700014-JLR200. PMID 17878492. 
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