دورية أكاديمية
أعرض في EDS

N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis.

التفاصيل البيبلوغرافية
العنوان: N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis.
المؤلفون: Uematsu S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, Japan., Goto Y; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, Japan., Suzuki T; Global Research Cluster, RIKEN, Wako 351-0198, Japan., Sasazawa Y; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, Japan., Dohmae N; Global Research Cluster, RIKEN, Wako 351-0198, Japan., Simizu S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, Japan.
المصدر: FEBS open bio [FEBS Open Bio] 2014 Oct 12; Vol. 4, pp. 879-85. Date of Electronic Publication: 2014 Oct 12 (Print Publication: 2014).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 101580716 Publication Model: eCollection Cited Medium: Print ISSN: 2211-5463 (Print) Linking ISSN: 22115463 NLM ISO Abbreviation: FEBS Open Bio Subsets: PubMed not MEDLINE
أسماء مطبوعة: Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam : Elsevier, 2011-
مستخلص: Extracellular matrix protein 1 (ECM1) is expressed in a wide variety of tissues and plays important roles in extracellular matrix formation. Additionally, ECM1 gene mutations cause lipoid proteinosis (LP), a rare skin condition of genetic origin. However, an effective therapeutic approach of LP is not established. Here, we showed that ECM1 gene mutation observed in LP patients significantly suppresses its secretion. As ECM1 has three putative N-glycosylation sites and most of mutated ECM1 observed in LP patients are defective in these N-glycosylation sites, we investigated the correlation between LP and N-glycosylation of ECM1. We identified that the Asn(354) and Asn(444) residues in ECM1 were N-glycosylated by mass spectrometry analysis. In addition, an N-linked glycan at Asn(354) negatively regulated secretion of ECM1, contrary to LP patient-derived mutants. These results indicate that the defect of N-glycosylation in ECM1 is not involved in the aberration of secretion of LP-derived mutated ECM1.
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فهرسة مساهمة: Keywords: CBB, Coomassie Brilliant Blue; ECM1, extracellular matrix protein 1; ER, endoplasmic reticulum; Extracellular matrix protein 1; LP, lipoid proteinosis; Lipoid proteinosis; MALDI-TOF MS, matrix-assisted laser desorption time flight mass spectrometry; N-Glycosylation; PBS, phosphate-buffered saline; PNGase F, peptide N-glycosidase F; SDS, sodium dodecyl sulfate; Secretion
تواريخ الأحداث: Date Created: 20141108 Date Completed: 20141107 Latest Revision: 20181113
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC4215116
DOI: 10.1016/j.fob.2014.10.004
PMID: 25379385
قاعدة البيانات: MEDLINE
الوصف
تدمد:2211-5463
DOI:10.1016/j.fob.2014.10.004