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Lipin 3

lipin-3, LPIN3
Humans lipodystrophy is characterized by loss of body fat, fatty liver, hypertriglyceridemia, and insulin resistance. Mice carrying mutations in the fatty liver dystrophy (fld) gene have similar phenotypes. Through positional cloning, the mouse gene responsible for fatty liver dystrophy was isolated and designated Lpin1. The nuclear protein encoded by Lpin1 was named lipin. Lpin1 mRNA was expressed at high levels in adipose tissue and was induced during differentiation of preadipocytes. These results indicated that lipin is required for normal adipose tissue development and provided a candidate gene for human lipodystrophy. Through database searches, mouse and human EST and genomic sequences with similarities to Lpin1 were identified. These included two related mouse genes (Lpin2 and Lpin3) and three human homologs (LPIN1, LPIN2, and LPIN3). Human LPIN1 gene has been mapped to 2p25.; linkages of fat mass and serum leptin levels to this same region have been noted. Human LPIN2 and LPIN3 mapped to chromosomes 18p11 and 20q11-q12, respectively. The mouse genes encoding Lpin1, Lpin2, and Lpin3 mapped to chromosome 12, 17, and 2, respectively. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: LPIN2, PAP, Pap1, Insulin, ACID
Papers on lipin-3
Genome-wide significant association with seven novel multiple sclerosis risk loci.
New
Bertram et al., Berlin, Germany. In J Med Genet, Dec 2015
LPIN3 (rs6072343, p=7.16×10(-12)) and IFNGR2 (rs9808753, p=4.40×10(-10)).
Lipin-1 and lipin-3 together determine adiposity in vivo.
Reue et al., Los Angeles, United States. In Mol Metab, 2014
Physiological roles for lipin-1 and lipin-2 have been identified, but the role of lipin-3 has remained mysterious.
Variation in genes related to hepatic lipid metabolism and changes in waist circumference and body weight.
Boeing et al., Potsdam, Germany. In Genes Nutr, 2014
We analysed single nucleotide polymorphisms (SNPs) tagging the genetic variability of six candidate genes (ATF6, FABP1, LPIN2, LPIN3, MLXIPL and MTTP) involved in the regulation of hepatic lipid metabolism, an important regulatory site of energy balance for associations with body mass index (BMI) and changes in weight and waist circumference.
Lipins, lipinopathies, and the modulation of cellular lipid storage and signaling.
Review
Reue et al., Los Angeles, United States. In Prog Lipid Res, 2013
Lipin function has been evolutionarily conserved from a single ortholog in yeast to the mammalian family of three lipin proteins-lipin-1, lipin-2, and lipin-3.
Differential regulation of the expressions of the PGC-1α splice variants, lipins, and PPARα in heart compared to liver.
Brindley et al., Edmonton, Canada. In J Lipid Res, 2013
Lipin-1, lipin-2, lipin-3, carnitine palmitoyltransferase-1b (Cpt1b), and PGC-1α-b mRNA were increased by glucocorticoids and cAMP in neonatal rat cardiomyocytes.
Identification of a novel cell-penetrating peptide from human phosphatidate phosphatase LPIN3.
Choi et al., Seoul, South Korea. In Mol Cells, 2012
We report here on a newly identified novel cell-penetrating sequence (LPIN; RRKRRRRRK) from the nuclear localization sequence (NLS) of human nuclear phosphatase, LPIN3.
Study of LPIN1, LPIN2 and LPIN3 in rhabdomyolysis and exercise-induced myalgia.
de Lonlay et al., Paris, France. In J Inherit Metab Dis, 2012
METHODS: Coding regions of LPIN1, LPIN2 and LPIN3 genes were sequenced using genomic or complementary DNAs.
Lipin-1 phosphatidic phosphatase activity modulates phosphatidate levels to promote peroxisome proliferator-activated receptor γ (PPARγ) gene expression during adipogenesis.
Reue et al., Los Angeles, United States. In J Biol Chem, 2012
We demonstrate that PAP activity supplied by lipin-1, lipin-2, or lipin-3, but not lipin-1 coactivator activity, can rescue Pparg gene expression and lipogenesis during adipogenesis in lipin-1-deficient preadipocytes.
Fine metabolic regulation in ruminants via nutrient-gene interactions: saturated long-chain fatty acids increase expression of genes involved in lipid metabolism and immune response partly through PPAR-α activation.
Loor et al., Urbana, United States. In Br J Nutr, 2012
The expression of SPP1 and LPIN3 was increased by WY, with no evidence of a similar effect in the published literature, suggesting that both represent bovine-specific PPAR-α targets.
Lipin - The bridge between hepatic glycerolipid biosynthesis and lipoprotein metabolism.
Review
Yao et al., Ottawa, Canada. In Biochim Biophys Acta, 2010
Growing evidence links the three mammalian lipin proteins, i.e., lipin-1, lipin-2 and lipin-3, to metabolic and cardiovascular diseases such as noninsulin-dependent diabetes mellitus and atherosclerosis.
Lipin proteins form homo- and hetero-oligomers.
GeneRIF
Harris et al., Beijing, China. In Biochem J, 2010
Data revealed that lipin 1 formed stable homo-oligomers with itself and hetero-oligomers with lipin 2/3.
Suppression of cardiac phosphatidate phosphohydrolase 1 activity and lipin mRNA expression in Zucker diabetic fatty rats and humans with type 2 diabetes mellitus.
Kurz et al., Lübeck, Germany. In Biochem Biophys Res Commun, 2010
PAP(1) activity was highly related with cardiac lipin-1 and lipin-3 mRNA expression in ZDF rats (r=0.99 and 0.96).
The lipin family: mutations and metabolism.
Review
Reue, Los Angeles, United States. In Curr Opin Lipidol, 2009
The genes for lipin-1, lipin-2 and lipin-3 are expressed in key metabolic tissues, including adipose tissue, skeletal muscle and liver, but the physiological functions of each member of the family have not been fully elucidated.
Sumoylation regulates nuclear localization of lipin-1alpha in neuronal cells.
Gerace et al., Los Angeles, United States. In Plos One, 2008
We are unable to detect sumoylation of the related proteins lipin-2 and lipin-3.
Thematic Review Series: Glycerolipids. Multiple roles for lipins/phosphatidate phosphatase enzymes in lipid metabolism.
Review
Brindley et al., Los Angeles, United States. In J Lipid Res, 2008
PAP1 activity in mammals is determined by the lipin family of proteins, lipin-1, lipin-2, and lipin-3, which each have distinct tissue expression patterns and appear to have unique physiological functions.
The lipin protein family: dual roles in lipid biosynthesis and gene expression.
Review
Zhang et al., Los Angeles, United States. In Febs Lett, 2008
The physiological roles of lipin-2 and lipin-3 are less well defined, but are likely to carry out similar functions in glycerolipid biosynthesis and gene expression in a distinct tissue distribution.
Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns.
GeneRIF
Reue et al., Los Angeles, United States. In J Biol Chem, 2007
Lipin-3 exhibits phosphatidate phosphatase type-1 (PAP1) activity, which has a key role in glycerolipid synthesis.
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