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  1. NADPH Oxidase-Dependent Production of Reactive Oxygen Species Induces Endoplasmatic Reticulum Stress in Neutrophil-Like HL60 Cells.

    PLoS ONE 10(2):e0116410 (2015) PMID 25668518 PMCID PMC4323339

    Reactive oxygen species (ROS) primarily produced via NADPH oxidase play an important role for killing microorganisms in neutrophils. In this study we examined if ROS production in Human promyelocytic leukemia cells (HL60) differentiated into neutrophil-like cells (dHL60) induces ER stress and ac...
  2. SDF2L1 interacts with the ER-associated degradation machinery and retards the degradation of mutant proinsulin in pancreatic β-cells.

    Journal of Cell Science 126(Pt 9):1962 (2013) PMID 23444373

    Stromal cell-derived factor 2-like 1 (SDF2L1) is an endoplasmic reticulum (ER)-localized protein whose function is undefined. Here we show that SDF2L1 protein levels are increased in response to ER stress-inducing compounds, but not other cell stressors that we tested in insulinoma cell lines. S...
  3. A glucagon-like peptide-1 analog reverses the molecular pathology and cardiac dysfunction of a mouse model of obesity.

    Circulation 127(1):74 (2013) PMID 23186644

    Cardiac consequences of obesity include inflammation, hypertrophy, and compromised energy metabolism. Glucagon-like peptide-1 is an incretin hormone capable of cytoprotective actions that reduces inflammation and endoplasmic reticulum stress in other tissues. Here we examine the cardiac effects ...
  4. Transcriptional response to deletion of the phosphatidylserine decarboxylase Psd1p in the yeast Saccharomyces cerevisiae.

    PLoS ONE 8(10):e77380 (2013) PMID 24146988 PMCID PMC3795641

    In the yeast, Saccharomyces cerevisiae, the synthesis of the essential phospholipid phosphatidylethanolamine (PE) is accomplished by a network of reactions which comprises four different pathways. The enzyme contributing most to PE formation is the mitochondrial phosphatidylserine decarboxylase ...
  5. Diverse roles for the p24 family of proteins in eukaryotic cells.

    BioMolecular Concepts 3(6):561 (2012) PMID 25436559

    Abstract Members of the p24 protein family form a highly conserved family of type I transmembrane proteins that are abundant components of the early secretory pathway. Topologically, the proteins have a large luminal domain and a short cytoplasmic domain that allows for targeting to both coat pr...
  6. Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells.

    Journal of Biological Chemistry 287(1):43 (2012) PMID 22105075 PMCID PMC3249095

    For insulin synthesis, the proinsulin precursor is translated at the endoplasmic reticulum (ER), folds to include its three native disulfide bonds, and is exported to secretory granules for processing and secretion. Protein disulfide isomerase (PDI) has long been assumed to assist proinsulin in ...
  7. Endoplasmic reticulum redox state is not perturbed by pharmacological or pathological endoplasmic reticulum stress in live pancreatic β-cells.

    PLoS ONE 7(11):e48626 (2012) PMID 23144914 PMCID PMC3493583

    Accumulation of unfolded, misfolded and aggregated proteins in the endoplasmic reticulum (ER) causes ER stress. ER stress can result from physiological situations such as acute increases in secretory protein biosynthesis or pathological conditions that perturb ER homeostasis such as alterations ...
  8. A yeast mutant deleted ofGPH1bears defects in phospholipid metabolism

    Chemistry and Physics of Lipids 164:S45 (2011)

  9. Phosphatidylethanolamine synthesized by four different pathways is supplied to the plasma membrane of the yeastSaccharomyces cerevisiae

    Biochimica et Biophysica Acta (BBA) - Molecular... 1801(4):480 (2010) PMID 20044027

    In this study, we examined the contribution of the four different pathways of phosphatidylethanolamine (PE) synthesis in the yeast Saccharomyces cerevisiae to the supply of this phospholipid to the plasma membrane. These pathways of PE formation are decarboxylation of phosphatidylser...
  10. Phosphatidylserine decarboxylases, key enzymes of lipid metabolism.

    Iubmb Life 61(2):151 (2009) PMID 19165886

    Phosphatidylserine decarboxylases (PSDs) (E.C. are enzymes which catalyze the formation of phosphatidylethanolamine (PtdEtn) by decarboxylation of phosphatidylserine (PtdSer). This enzymatic activity has been identified in both prokaryotic and eukaryotic organisms. PSDs occur as two ty...