title: LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing tissues.
abstract: The PAT family (originally named for Perilipin, ADFP and TIP47) now includes four members: Perilipins, ADFP, TIP47 and S3-12. Significant primary sequence homology and the ability to associate with lipid storage droplets (LSDs) are well conserved within this family and across species. In this study, we have characterized a novel PAT protein, lipid storage droplet protein 5 (LSDP5) of 463 residues. A detailed sequence analysis of all murine PAT proteins reveals that LSDP5, TIP47 and ADFP share the highest order of sequence similarity, whereas perilipin and S3-12 have more divergent carboxyl- and amino-termini, respectively. Ectopically-expressed YFP-LSDP5 or flag-LSDP5 fusion proteins associate with LSDs. In accord with recent published data for perilipin, forced expression of LSDP5 in CHO cells inhibits lipolysis of intracellular LSDs. The LSDP5 gene is primarily transcribed in cells that actively oxidize fatty acids, such as heart, red muscle and liver. Expression of LSDP5 is stimulated by ligand activation of peroxisomal proliferator-activated receptor alpha (PPARalpha), and significantly reduced in liver and heart in the absence of this transcription factor. PPARalpha is generally required for regulation of fatty acid metabolism during fasting, but fasting induces LSDP5 mRNA in liver even in the absence of PPARalpha.
authors.affiliation: Department of Nutrition, Institute of Basic Medical Sciences, University of Oslo, P.O. Box 1046 Blindern, N-0316 Oslo, Norway. dalenk@mail.nih.gov
authors.forename: Knut Tomas
authors.initials: KT
authors.lastname: Dalen
authors.forename: Tuva
authors.initials: T
authors.lastname: Dahl
authors.forename: Elin
authors.initials: E
authors.lastname: Holter
authors.forename: Borghild
authors.initials: B
authors.lastname: Arntsen
authors.forename: Constantine
authors.initials: C
authors.lastname: Londos
authors.forename: Carole
authors.initials: C
authors.lastname: Sztalryd
authors.forename: Hilde I
authors.initials: HI
authors.lastname: Nebb
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D002352:Carrier Proteins; D002522:Chlorocebus aethiops; D002886:Chromosomes, Human, Pair 17; D005091:Exons; D005215:Fasting / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D008099:Liver / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D047493:PPAR alpha / Q000378:metabolism; D000070778:Perilipin-1; D000070797:Perilipin-5; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D011506:Proteins / Q000235:genetics* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
chemical_list: D002352:Carrier Proteins; D005227:Fatty Acids; D047493:PPAR alpha; D000070778:Perilipin-1; D000070797:Perilipin-5; D010750:Phosphoproteins; C511805:Plin5 protein, mouse; D011506:Proteins