Alterations in subcellular PRIP distribution and HSL phosphorylation in explant adipose tissues. Toshiya Okumura Kae Harada Kana Oue Jun Zhang Satoshi Asano Masaki Hayashiuchi Akiko Mizokami Hiroto Tanaka Masahiro Irifune Nobuyuki Kamata Masato Hirata Takashi Kanematsu 10.1371/journal.pone.0100559.g003 https://plos.figshare.com/articles/figure/_Alterations_in_subcellular_PRIP_distribution_and_HSL_phosphorylation_in_explant_adipose_tissues_/1063233 <p>(A, B) Adrenaline stimulation (Adrn) induces HSL translocation from cytosol fraction (sup) to fat-cake fraction (fat) in WT and <i>PRIP</i>-DKO explant adipose tissues. The bars for fat (black) and sup (white) in B represent the floating fat-cake and supernatant fractions, respectively. The amount of total HSL in fat and sup fractions is expressed as 100%. All the data represent mean ±SEM. **<i>p</i><0.01 and n.s. (not significant) versus the corresponding WT value. Altered phosphorylation of HSL at Ser563 and Ser660 and perilipin at Ser492 in adipose explant lipolysis assays with or without stimulation by 1 µM adrenaline are also shown in (A). A representative image is shown; similar images were obtained from three independent experiments. (C, D) PRIP translocation to the lipid droplet fraction in response to 1 µM adrenaline (Adrn) stimulation. The bars for fat (black) and sup (white) in (D) represent the floating fat-cake and supernatant fractions, respectively. The amount of total PRIP in fat and sup fractions is expressed as 100%. Perilipin and β-actin are lipid droplet and cytosol marker proteins, respectively. A representative image is shown; similar images were obtained from three independent experiments (C). The data represent mean ±SEM. **<i>P</i><0.01 and ***<i>P</i><0.001 versus the corresponding values of PRIP1 and PRIP2 without adrenaline stimulation.</p> 2014-06-19 03:57:39 Biochemistry lipids fats Lipid metabolism metabolism subcellular prip hsl phosphorylation explant adipose