Dataset Information

Deletion of intestinal Hdac3 remodels the lipidome of enterocytes and protects mice from diet-induced obesity

ABSTRACT: Deletion of intestinal Hdac3 remodels the lipidome of enterocytes and protects mice from diet-induced obesity

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Intestinal Epithelium, Small Intestine

SUBMITTER: Suresh Mathivanan

LAB HEAD: Prof John Mariadason

PROVIDER: PXD015738 | Pride | 2020-01-13

REPOSITORIES: Pride

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Deletion of intestinal Hdac3 remodels the lipidome of enterocytes and protects mice from diet-induced obesity.

Dávalos-Salas Mercedes M Montgomery Magdalene K MK Reehorst Camilla M CM Nightingale Rebecca R Ng Irvin I Anderton Holly H Al-Obaidi Sheren S Lesmana Analia A Scott Cameron M CM Ioannidis Paul P Kalra Hina H Keerthikumar Shivakumar S Tögel Lars L Rigopoulos Angela A Gong Sylvia J SJ Williams David S DS Yoganantharaja Prusoth P Bell-Anderson Kim K Mathivanan Suresh S Gibert Yann Y Hiebert Scott S Scott Andrew M AM Watt Matthew J MJ Mariadason John M JM

Nature communications 20191122 1

Histone deacetylase 3 (Hdac3) regulates the expression of lipid metabolism genes in multiple tissues, however its role in regulating lipid metabolism in the intestinal epithelium is unknown. Here we demonstrate that intestine-specific deletion of Hdac3 (Hdac3<sup>IKO</sup>) protects mice from diet induced obesity. Intestinal epithelial cells (IECs) from Hdac3<sup>IKO</sup> mice display co-ordinate induction of genes and proteins involved in mitochondrial and peroxisomal β-oxidation, have an incr ...[more]

PMID: 31757939

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Project description:HDL particles vary in lipidome and proteome, which dictate their individual physicochemical properties, metabolism, and biological activities. HDL dysmetabolism in nondiabetic hypertriglyceridemia (HTG) involves subnormal HDL-cholesterol and apoAI levels. Metabolic anomalies may impact the qualitative features of both the HDL lipidome and proteome. Whether particle content of bioactive lipids and proteins may differentiate HDL subclasses (HDL2b, 2a, 3a, 3b, and 3c) in HTG is unknown. Moreover, little is known of the effect of statin treatment on the proteolipidome of hypertriglyceridemic HDL and its subclasses. Nondiabetic, obese, HTG males (n = 12) received pitavastatin calcium (4 mg/day) for 180 days in a single-phase, unblinded study. ApoB-containing lipoproteins were normalized poststatin. Individual proteolipidomes of density-defined HDL subclasses were characterized prestatin and poststatin. At baseline, dense HDL3c was distinguished by marked protein diversity and peak abundance of surface lysophospholipids, amphipathic diacylglycerol and dihydroceramide, and core cholesteryl ester and triacylglycerol, (normalized to mol phosphatidylcholine), whereas light HDL2b showed peak abundance of free cholesterol, sphingomyelin, glycosphingolipids (monohexosylceramide, dihexosylceramide, trihexosylceramide, and anionic GM3), thereby arguing for differential lipid transport and metabolism between subclasses. Poststatin, bioactive lysophospholipid (lysophosphatidylcholine, lysoalkylphosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylinositol) cargo was preferentially depleted in HDL3c. By contrast, baseline lipidomic profiles of ceramide, dihydroceramide and related glycosphingolipids, and GM3/phosphatidylcholine were maintained across particle subclasses. All subclasses were depleted in triacylglycerol and diacylglycerol/phosphatidylcholine. The abundance of apolipoproteins CI, CII, CIV, and M diminished in the HDL proteome. Statin treatment principally impacts metabolic remodeling of the abnormal lipidome of HDL particle subclasses in nondiabetic HTG, with lesser effects on the proteome.

			Action	DRS
	HDAC3_KO_1.raw	Raw
	HDAC3_KO_1.xml	Xml
	HDAC3_KO_12.raw	Raw
	HDAC3_KO_12.xml	Xml
	HDAC3_KO_13.raw	Raw