Lipid droplets (LD) are highly recognized in biomedical research and pathology. These organells are found in nearly all cell types and tissues and the composition of lipidic material varies strongly, depending on their storage or transport function. LDs are linked to several diseases like diabetes, obesity, liposarcoma, atherosclerosis, lipid droplet biogenesis, viral and bacterial infection.
Perilipins / PAT family proteins
- 5 subtypes: perilipin 1-5 (PLIN1- PLIN5)
- located in the membrane of LDs
- characterization of LD subpopulations and multifunctional properties (lipid transport, lipogenesis and lypolysis)
- analysis of viral or bacterial infection pathways (targeting LDs)
"In the community of lipid droplet biology research, your antibodies are highly appreciated and many papers in this field rely on PROGEN antibodies." Prof. Dr. Matthijs Hesselink, Maastricht University Medical Center, The Netherlands
PROGEN offers a selection of different antibodies against all 5 perilipin subtypes (PLIN1-PLIN5) for a number of applications (western blot, IHC, IF and ICC).
Perilipin 1 (PLIN1)
- on the surfaces of intracellular lipid storage droplets
- adrenal gland, adipocytes of white/brown adipose tissue, cell culture e.g. 3T3-L1 adipocytes,steroidogenic adrenal cortical, Leydig cells
- useful pathological marker (de novo expressed in hepatocyte steatogenesis)
Perilipin 2 (PLIN2) or adipocyte differentiation-related protein (ADRP) / adipophilin
- tightly associated with the LD surface
- enhanced expression as marker for pathologies characterized by increased lipid droplet accumulation e.g. atheroma, steatosis, obesity and certain cases of liposarcoma
- considered to be a potent marker for atherosclerosis
Perilipin 3 (PLIN3) or TIP47 / placental protein 17 (PP17) / M6PR binding protein 1 (MP6PRBP1)
- sequence similarity to PLIN2
- binds to lipid storage droplets
- suggested to contribute to LD formation and stabilzation.
Perilipin 4 (PLIN4) or S3-12
- selectively expressed in adipocytes in the middle to late stage of differentiation
- might be involved in uptake of lipids and hydrophobic substances
Perilipin 5 (PLIN5) or OXPAT/MDLP
- functionally associated with lipid storage droplets
- found in muscle cell tissue
- supposed to be involved in the supply of energy to the mitochondria of muscle cells
- Heid, H. et al. Lipid droplets, perilipins and cytokeratins--unravelled liaisons in epithelium-derived cells. PLoS One 8, (2013).
- Fernández-Rojo, M. A. et al. Caveolin-1 Is Necessary for Hepatic Oxidative Lipid Metabolism: Evidence for Crosstalk between Caveolin-1 and Bile Acid Signaling. Cell Rep. 4, 238–247 (2013).
- Kuramoto, K. et al. Deficiency of a Lipid Droplet Protein, Perilipin 5, Suppresses Myocardial Lipid Accumulation, Thereby Preventing Type 1 Diabetes- Induced Heart Malfunction. Mol. Cell. Biol. 34, 2721–2731 (2014).
- Barquissau, V. et al. White-to-brite conversion in human adipocytes promotes metabolic reprogramming towards fatty acid anabolic and catabolic pathways. Mol. Metab. 5, 352–366 (2016).
- Gallardo-Montejano, V. I. et al. Nuclear Perilipin 5 integrates lipid droplet lipolysis with PGC-1a/SIRT1-dependent transcriptional regulation of mitochondrial function. Nat. Commun. 7, (2016).
- Inoue, J. et al. Identification of BCL11B as a regulator of adipogenesis. Sci. Rep. 6, 32750 (2016).
- Kaushik, S. & Cuervo, A. M. AMPK-dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA. Autophagy 12, 432–438 (2016).
- Furukawa, S., Nagaike, M. & Ozaki, K. Databases for technical aspects of immunohistochemistry. J. Toxicol. Pathol. 30, 79–107 (2017).
- Gemmink, A. et al. Dissociation of intramyocellular lipid storage and insulin resistance in trained athletes and type 2 diabetes patients; involvement of perilipin 5? J. Physiol. (2017).