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Analysis of Phosphorylation Sites in Perilipin 5
Author(s) -
Sumser Natalie M,
Tansey John T
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.490.15
Subject(s) - perilipin , phosphorylation , oxidative phosphorylation , forskolin , chemistry , biochemistry , lipid droplet , lipid metabolism , biology , microbiology and biotechnology , lipolysis , adipose tissue , receptor
In modern times, there has been a significant increase in metabolic disease. Obesity has been a growing concern in the U.S, leading to a rise in various health problems, such as type II diabetes and cardiovascular disease. One major factor in these diseases is lipid metabolism. The understanding of this process would lead to a better understanding of these diseases. Perilipins, a family of five proteins associated with lipid droplets, play an important role in lipid metabolism. Perilipin 5 is primarily seen in oxidative tissue, acting to regulate fatty acid storage and release, as well as fatty acid oxidation. It is known that phosphorylation partially regulates the activity of Perilipin 5, particularly due to PKA activation, and we hypothesized that there are multiple phosphorylation sites on the protein. Treatment of cells with forskolin and IBMX was used to increase cyclic AMP to activate PKA. This was followed by immunopreciptation and trypsin digestion of perilipin 5. Phosphopeptides are enriched through affinity chromatography with a Fe‐NTA column prior to conducting mass spectrometry on the samples to differentiate between phosphorylation sites. We hypothesize that both a combination of where perilipin 5 is phosphorylated and when the sites are phosphorylated cooperate to regulate the function of the protein. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .