Overexpression of SND p102, a rat homologue of p100 coactivator, promotes the secretion of lipoprotein phospholipids in primary hepatocytes

Palacios, Lourdes; Ochoa, Begoña; Gómez-Lechón, Marı́a José; Castell, José V.; Fresnedo, Olatz

doi:10.1016/j.bbalip.2006.05.005

Cited by 34 publications

(44 citation statements)

References 55 publications

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“…Interestingly, the staphylococcal nuclease domain-containing protein 1, termed SND1 or p100 coactivator, was also identified as syt11-binding protein via N-terminal and C-terminal peptides. SND1 has been implicated in various cell functions in addition to its role as a transcriptional coactivator, namely in the secretion of lipid droplets in mammary epithelial cells and hepatocytes [19,26,27] and as part of the RISC complex by interacting with Argonaute 2 [28]. The protein is expressed in primary pancreatic a-and b-cells (data not shown).…”

Section: Resultsmentioning

confidence: 99%

“…Several antibodies were kindly donated: the monoclonal anti-FMRP antibody 1C3 (Dr. Mazroui, Université Laval, Québec, Canada); a rabbit polyclonal anti-CaBP1/PDIA6 (Dr. Nguyen Van, Universität Göttingen, Germany), a monoclonal anti-Ago2 (851) (Dr. Hobman, University of Alberta, Edmonton, Canada), a monoclonal anti-EEA1 (Dr. Grunberg, Genève, Switzerland), a monoclonal anti-LAMP1 (Dr. Malosio, Milano), a rabbit polyclonal anti-syntaxin5, antisyntaxin18 and anti-D12/Use1p (Dr. Hatsuzawa, Fukushima Medical University, Japan). The rabbit polyclonal anti SND1/p102 had been described previously [19].…”

Section: Methodsmentioning

confidence: 99%

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Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

et al. 2014

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a b s t r a c tSynaptotagmins are two C 2 domain-containing transmembrane proteins. The function of calciumsensitive members in the regulation of post-Golgi traffic has been well established whereas little is known about the calcium-insensitive isoforms constituting half of the protein family. Novel binding partners of synaptotagmin 11 were identified in b-cells. A number of them had been assigned previously to ER/Golgi derived-vesicles or linked to RNA synthesis, translation and processing. Whereas the C2A domain interacted with the Q-SNARE Vti1a, the C2B domain of syt11 interacted with the SND1, Ago2 and FMRP, components of the RNA-induced silencing complex (RISC). Binding to SND was direct via its N-terminal tandem repeats. Our data indicate that syt11 may provide a link between gene regulation by microRNAs and membrane traffic. Structured summary of protein interactions:Syt11C2A physically interacts with Vti1a by pull down (View interaction) Syt11C2B physically interacts with SND1, PDIA6, Vti1b, Vti1a, Ago2 and FMRP by pull down (View interaction) syt11C2B binds to SND1 by filter binding (View interaction) Syt11C2B physically interacts with EIF3A, PDIA6, NPM1, EIF3B, NCL, RS3, RS3A, CBR1, ANP32B, LOC683961, SET, SND1, TBB2C, RS10 and RS18 by pull down (View interaction) SND1 physically interacts with Ago2 by anti bait coip (View interaction)

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

et al. 2014

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“…Immunocytochemistry was performed basically as described elsewhere (33). Briefly, hepatocytes were incubated on coverslips for 4 h, washed and fixed with formaldehyde, permeabilized with Triton X-100, and blocked with newborn calf serum.…”

Section: Methodsmentioning

confidence: 99%

High insulin levels are required for FAT/CD36 plasma membrane translocation and enhanced fatty acid uptake in obese Zucker rat hepatocytes

Buqué

Cano

Miquilena-Colina

et al. 2012

American Journal of Physiology-Endocrinology and Metabolism

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Buqué X, Cano A, Miquilena-Colina ME, García-Monzón C, Ochoa B, Aspichueta P. High insulin levels are required for FAT/CD36 plasma membrane translocation and enhanced fatty acid uptake in obese Zucker rat hepatocytes. Am J Physiol Endocrinol Metab 303: E504-E514, 2012. First published June 12, 2012; doi:10.1152/ajpendo.00653.2011In myocytes and adipocytes, insulin increases fatty acid translocase (FAT)/CD36 translocation to the plasma membrane (PM), enhancing fatty acid (FA) uptake. Evidence links increased hepatic FAT/CD36 protein amount and gene expression with hyperinsulinemia in animal models and patients with fatty liver, but whether insulin regulates FAT/CD36 expression, amount, distribution, and function in hepatocytes is currently unknown. To investigate this, FAT/CD36 protein content in isolated hepatocytes, subfractions of organelles, and density-gradient isolated membrane subfractions was analyzed in obese and lean Zucker rats by Western blotting in liver sections by immunohistochemistry and in hepatocytes by immunocytochemistry. The uptake of oleate and oleate incorporation into lipids were assessed in hepatocytes at short time points (30 -600 s). We found that FAT/CD36 protein amount at the PM was higher in hepatocytes from obese rats than from lean controls. In obese rat hepatocytes, decreased cytoplasmatic content of FAT/CD36 and redistribution from low-to middleto middle-to high-density subfractions of microsomes were found. Hallmarks of obese Zucker rat hepatocytes were increased amount of FAT/CD36 protein at the PM and enhanced FA uptake and incorporation into triglycerides, which were maintained only when exposed to hyperinsulinemic conditions (80 mU/l). In conclusion, high insulin levels are required for FAT/CD36 translocation to the PM in obese rat hepatocytes to enhance FA uptake and triglyceride synthesis. These results suggest that the hyperinsulinemia found in animal models and patients with insulin resistance and fatty liver might contribute to liver fat accumulation by inducing FAT/CD36 functional presence at the PM of hepatocytes. fatty acid translocase; steatosis; hyperinsulinemia; free fatty acid; nonalcoholic fatty liver disease; triglyceride FATTY ACID TRANSLOCASE (FAT)/CD36 has been recognized as the most important protein implicated in fatty acid (FA) uptake by skeletal muscle cells, cardiomyocytes, and adipocytes (36,8,16), being required at the plasma membrane (PM) for its function as FA transporter. In these cell types, FAT/CD36 cellular distribution is regulated by muscle contraction and/or insulin, which induce protein translocation to the PM from an intracellular pool (19,31,39). This particular regulation allows these tissues to respond to acute and chronic metabolic requirements, turning FAT/CD36 into a key regulator of whole body lipid homeostasis (8). In certain disorders characterized by a defective response to insulin action in muscular and adipose tissues, such as obesity and type 2 diabetes, when FAT/CD36 protein is increased at the PM, FA uptake also increases (19...

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“…The protein content of the samples was comparable and was estimated in 5 mg protein/100 mg tissue using Pierce reagent [21]. Lipids were exhaustively extracted from homogenates by a modified Bligh and Dyer procedure described earlier [22], with the extraction efficiency for the lipid classes averaging 95-99% according to radiometric analysis performed in parallel.…”

Section: Methodsmentioning

confidence: 99%

Anatomical Distribution of Lipids in Human Brain Cortex by Imaging Mass Spectrometry

Veloso

Astigarraga

Barreda-Gómez

et al. 2011

J. Am. Soc. Mass Spectrom.

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Molecular mass images of tissues will be biased if differences in the physicochemical properties of the microenvironment affect the intensity of the spectra. To address this issue, we have performedby means of MALDI-TOF mass spectrometry-imaging on slices and lipidomic analysis in extracts of frontal cortex, both from the same postmortem tissue samples of human brain. An external calibration was used to achieve a mass accuracy of 10 ppm (1σ) in the spectra of the extracts, although the final assignment was based on a comparison with previously reported species. The spectra recorded directly from tissue slices (imaging) show excellent s/n ratios, almost comparable to those obtained from the extracts. In addition, they retain the information about the anatomical distribution of the molecular species present in autopsied frozen tissue. Further comparison between the spectra from lipid extracts devoid of proteins and those recorded directly from the tissue unambiguously show that the differences in lipid composition between gray and white matter observed in the mass images are not an artifact due to microenvironmental influences of each anatomical area on the signal intensity, but real variations in the lipid composition.

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Overexpression of SND p102, a rat homologue of p100 coactivator, promotes the secretion of lipoprotein phospholipids in primary hepatocytes

Cited by 34 publications

References 55 publications

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

Synaptotagmin 11 interacts with components of the RNA‐induced silencing complex RISC in clonal pancreatic β‐cells

High insulin levels are required for FAT/CD36 plasma membrane translocation and enhanced fatty acid uptake in obese Zucker rat hepatocytes

Anatomical Distribution of Lipids in Human Brain Cortex by Imaging Mass Spectrometry

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