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Evidence of a Perilipin‐5 Splice Variant
Author(s) -
Ranzau Brodie L.,
DuBreuil Daniel M,
Hubbell Theresa,
Tansey John T
Publication year - 2016
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.30.1_supplement.1134.7
Subject(s) - perilipin , exon , intron , splice , rna splicing , alternative splicing , biology , genomic dna , messenger rna , genetics , microbiology and biotechnology , gene , biochemistry , adipose tissue , rna , lipolysis
The large diversity of proteins found within animals are made possible through alternative splicing of mRNA. This has been shown to occur within the perilipin family of lipid storage droplet proteins in both perilipins 1 and 3. In the course of our studies on perilipin 5, we observed a signal on an immunoblot corresponding to an approximately 35 kDa protein. We have hypothesized that this is a splice variant of perilipin 5 that we have termed perilipin 5b. The objective of the current study is to confirm the existence of this splice variant and characterize the protein it encodes. Western blots indicate that perilipin 5b is present in C2C12 cultured myoblasts and in heart and liver tissue from fed and fasted mice. Highest levels of the protein were present in heart tissue from fed mice. Analysis of murine genomic DNA sequences reveals stop codons found in the introns between exons 7 and 8 and 8 and 9. Failure to splice out either of these introns could give rise to a protein of approximately 35 kDa. Reverse trancriptase PCR yields products that are consistent with a splice variant. Finally, analysis of the murine genbank EST library yields several transcripts that indicate a read through event into an intron has occurred. Collectively these data indicate that, like other family members, perilipin 5 undergoes differential splicing to generate multiple protein products.