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Bruestle pointing at poster discussing with Dr. Blanchette



"siRNA Knockdown of a Lipid-droplet Associated Protein"

Daniel Bruestle
Mentor: Dr. Pamela Mertz
St. Mary's College of Maryland, 2006-2007

   Cells store fatty acids in the form of triacylgycerols packed into lipid droplets. These droplets are covered by a group of proteins known as the PAT (Perilipin, Adipose differentiation-related protein, Tail-interacting protein 47 kDa) family, which is characterized by amino acid sequence homology and an association with lipid droplets. Other PAT members include S3-12, PAT-1, and Prp19p. Most of these proteins are believed to be involved with regulating lipolysis and lipid droplet formation and breakdown. Perilipin is known to regulate the translocation of hormone sensitive lipase to the lipid droplet surface, but the specific functions of the remaining members are still unknown. The aim of this study was to try to determine the function of Tail-interacting protein 47 kDa, by knocking down expression using RNA interference in 3T3-L1 preadipocytes, and then differentiating the transfected cells. The treatment achieved partial gene knockdown in the cells, but I was unable to determine if there was any effect on the differentiation process.



 

 

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Webpage last updated July 21, 2005