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Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals,Drosophila, and Dictyostelium *
It is shown that GFP-tagged TIP47 co-localizes with isolated intracellular lipid droplets and that related proteins from species as diverse as Drosophila and Dictyostelium can also target mammalian or Drosophile lipid droplet surfaces in vivo, strongly indicating that they have a common function for lipid deposition and/or mobilization.
Perilipin ablation results in a lean mouse with aberrant adipocyte lipolysis, enhanced leptin production, and resistance to diet-induced obesity
The data reveal a major role for perilipin in adipose lipid metabolism and suggest perilipIn as a potential target for attacking problems associated with obesity.
Perilipin A Increases Triacylglycerol Storage by Decreasing the Rate of Triacylglycerol Hydrolysis*
- D. Brasaemle, Boris Rubin, Ingrid A. Harten, J. Gruia-Gray, A. Kimmel, C. Londos
- BiologyJournal of Biological Chemistry
- 8 December 2000
It is concluded that perilipin A increases the triacylglycerol content of cells by forming a barrier that reduces the access of soluble lipases to stored lipids, thus inhibiting triacyLglycersol hydrolysis.
Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells.
- C. Londos, D. Brasaemle, C. Schultz, J. Segrest, A. Kimmel
- BiologySeminars in Cell and Developmental Biology
- 1 February 1999
The properties, distribution, localization, and potential functions of perilipins and ADRP, as well as those of vimentin and the recently-described 'capsular' proteins, in lipid storage and metabolism are discussed.
Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation
It is shown that HSL is basally associated with lipid droplet surfaces at a low level in perilipin nulls, but that stimulated translocation from the cytosol to lipid droplets is absent in adipocytes derived from embryonic fibroblasts of perilip in-null mice.
A rapid and efficient method to generate multiple gene disruptions in Dictyostelium discoideum using a single selectable marker and the Cre-loxP system.
A robust system for the production of multiple gene mutations in Dictyostelium is described by recycling a single selectable marker, Blasticidin S resistance, using the Cre-loxP system and confirmed by generating a single cell carrying four separate gene disruptions.
Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins
- A. Kimmel, D. Brasaemle, M. McAndrews-Hill, C. Sztalryd, C. Londos
- BiologyJournal of Lipid Research
- 1 March 2010
Each gene member will incorporate the root term PERILIPIN (PLIN), the founding gene of the PAT family, with the different genes/proteins numbered sequentially, in a unifying nomenclature for the gene and protein family members.
On the Control of Lipolysis in Adipocytes
- C. Londos, D. Brasaemle, C. Rondinone
- BiologyAnnals of the New York Academy of Sciences
- 1 November 1999
The participation of perilipin A is indicated by the findings that this protein can protect neutral lipids within droplets from hydrolysis, but active participation in the lipolytic reaction is yet to be proved.
The Perilipins: Major Cytosolic Lipid Droplet-Associated Proteins and Their Roles in Cellular Lipid Storage, Mobilization, and Systemic Homeostasis.
The perilipin family is of ancient origin and has expanded to include five mammalian genes and a growing list of evolutionarily conserved members, and Universally, the perilipins modulate cellular lipid storage.