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Interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1): Implication of N-glycosylation in FAM5C secretion.
Terao, Yuya; Fujita, Hidenobu; Horibe, Sayo; Sato, Junya; Minami, Satomi; Kobayashi, Miwako; Matsuoka, Ichiro; Sasaki, Naoto; Satomi-Kobayashi, Seimi; Hirata, Ken-Ichi; Rikitake, Yoshiyuki.
Afiliação
  • Terao Y; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan; Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
  • Fujita H; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan.
  • Horibe S; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan.
  • Sato J; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan; Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
  • Minami S; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan.
  • Kobayashi M; Laboratory of Physiological Chemistry, College of Pharmaceutical Sciences, Matsuyama University, Matsuyama, Ehime 790-8578, Japan.
  • Matsuoka I; Laboratory of Physiological Chemistry, College of Pharmaceutical Sciences, Matsuyama University, Matsuyama, Ehime 790-8578, Japan.
  • Sasaki N; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan; Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
  • Satomi-Kobayashi S; Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
  • Hirata KI; Division of Cardiovascular Medicine, Department of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan.
  • Rikitake Y; Department of Medical Pharmaceutics, Kobe Pharmaceutical University, Kobe, Hyogo 658-8558, Japan; Division of Signal Transduction, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe, Hyogo 650-0017, Japan. Electronic address: rikitake@kobepharma-u.ac.
Biochem Biophys Res Commun ; 486(3): 811-816, 2017 05 06.
Article em En | MEDLINE | ID: mdl-28351617
N-glycosylation of proteins is important for protein folding and function. We have recently reported that FAM5C/BRINP3 contributes to the tumor necrosis factor-α-induced expression of leukocyte adhesion molecules in vascular endothelial cells (ECs). However, regulatory mechanism of the FAM5C biosynthesis is poorly understood. Co-immunoprecipitation assay revealed the interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), a glycoprotein folding-sensor enzyme. FAM5C ectopically expressed in HEK293 cells was localized to the endoplasmic reticulum and co-localized with endogenously expressed UGGT1. Molecular size of FAM5C was reduced by treatment with N-glycosidase F and in FAM5C-expressing cells cultured in the presence of the N-glycosylation inhibitor tunicamycin. FAM5C was secreted by the cells and the secretion of FAM5C was blocked by tunicamycin. Among six potential N-glycosylation sites, the potential site at Asn168 was not N-glycosylated, and Asn337, Asn456, Asn562, Asn609, and Asn641 mutants were poorly secreted by the cells. These results demonstrated that FAM5C is an N-glycosylated protein and N-glycosylation is necessary for the secretion of FAM5C.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Asparagina / Processamento de Proteína Pós-Traducional / Proteínas de Ligação a DNA / Glucosiltransferases Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Asparagina / Processamento de Proteína Pós-Traducional / Proteínas de Ligação a DNA / Glucosiltransferases Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article