Perilipin is an intracellular neutral lipid droplet protein that is hormonally regulated. This protein is localized exclusively to the surface of lipid droplets. In response to lypotic stimuli, perilipin is phosphorylated by protein kinase A. Once activated, perilipin has inhibitory affects upon hormone-sensitive lipase (HSL), a protein that mediates the hydrolysis of triacylglycerol, the major form of stored energy in the body. Perilipin expression is limited to adipocytes and steroidogenic cells. There are currently two known isoforms, Perilipin A and B. Both of these proteins are encoded by a single-copy gene and are the result of differential splicing events.
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