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Characterization of a perilipin 5 splice variant
Author(s) -
Hubbell Theresa C.,
DuBreuil Daniel M.,
Tansey John T.
Publication year - 2013
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.27.1_supplement.1020.4
Subject(s) - perilipin , lipid droplet , microbiology and biotechnology , biology , rna splicing , alternative splicing , blot , messenger rna , gene , biochemistry , lipolysis , rna , adipose tissue
The perilipins are a family of five related genes that code for proteins which play seminal roles in lipid storage. At least one of these proteins (perilipin 1) has been shown to have several truncated forms that arise through differential mRNA splicing. Using western blotting we have identified a truncated form of perilipin 5 we have termed perilipin 5 b. This protein is found in murine heart tissue as well as cultured cells. We hypothesized that this was a novel splice variant of the perilipin 5 mRNA. Using RT‐PCR we have identified multiple amplicons suggesting that perilipin‐5b contains a read through of intron 8 of the murine perilipin 5 gene. shRNA studies conducted in cultured cells result in decreased levels of the protein. In addition, immunofluorescence microscopy revealed that perilipin‐5B is unable to bind to mature lipid droplets, but does form distinct puncta in the cytosol. Taken together, this data suggests that perilipin‐5B is a splice variant of perilipin‐5 found in oxidative tissues that is unable to bind to lipid droplets. The role of this protein in neutral lipid metabolism remains unclear.