N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway.

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Abstract Text:

Hongbo Zhao,Lidong Sun,Liying Wang,Zhibin Xu,Feng Zhou,Jianmin Su,Jiawei Jin,Yong Yang,Yali Hu,Xiliang Zha,Hongbo Zhao,Lidong Sun,Liying Wang,Zhibin Xu,Feng Zhou,Jianmin Su,Jiawei Jin,Yong Yang,Yali Hu,Xiliang Zha,

E-cadherin, which has a widely acknowledged role in mediating calcium-dependent cell-cell adhesion between epithelial cells, also functions as a tumor suppressor. The ectodomain of human E-cadherin contains four potential N-glycosylation sites at Asn residues 554, 566, 618, and 633. We investigated the role of E-cadherin N-glycosylation in cell cycle progression by site-directed mutagenesis. We showed previously that all four potential N-glycosylation sites of E-cadherin were N-glycosylated in human breast carcinoma MDA-MB-435 cells. Removal of N-glycan at Asn633 dramatically affected E-cadherin stability. In this study we showed that E-cadherin mutant missing N-glycans at Asn554, Asn566 and Asn618 failed to induce cell cycle arrest in G1 phase and to suppress cell proliferation in comparison with wild-type E-cadherin. Moreover, N-glycans at Asn554 and Asn566, but not at Asn618, seemed to be indispensable for E-cadherin-mediated suppression of cell cycle progression. Removal of N-glycans at either Asn554 or Asn566 of E-cadherin was accompanied with the activation of the extracellular signal-regulated protein kinase signaling pathway. After treatment with PD98059, an inhibitor of the extracellular signal-regulated protein kinase signaling pathway, wild-type E-cadherin transfected MDA-MB-435 and E-cadherin N-glycosylation-deficient mutant transfected MDA-MB-435 cells had equivalent numbers of cells in G1 phase. These findings implied that N-glycosylation might be crucial for E-cadherin-mediated suppression of cell cycle progression.

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Publishing Authors By Initials

H Zhao,L Sun,L Wang,Z Xu,F Zhou,J Su,J Jin,Y Yang,Y Hu,X Zha,H Zhao,L Sun,L Wang,Z Xu,F Zhou,J Su,J Jin,Y Yang,Y Hu,X Zha,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Acta biochimica et biophysica Sinica

VOLUME: 40

Page Numbers: 140-8

Journal Abbreviation: Acta Biochim. Biophys. Sin. (S

ISSN: 1745-7270

DAY: 31

MONTH: Feb

YEAR: 2008

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101206716

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway.

AFFILIATION: Key Laboratory of Glycoconjugate Research, Ministry of Health, Department of Biochemistry and Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, China. xlzha@shmu.edu.cn.

Country: China

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Acta Biochim Biophys Sin (Shan

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway Related Publications

• ATP-binding Cassette A1-mediated Lipidation of Apolipoprotein A-I Occurs at the Plasma Membrane and Not in the Endocytic Compartments.
• Absorbable collagen sponge combined with recombinant human basic fibroblast growth factor promotes nerve regeneration in rat sciatic nerve.
• Acceleration of wound healing in traumatic ulcers by absorbable collagen sponge containing recombinant basic fibroblast growth factor.
• Angiopoietin-like protein 3 modulates barrier properties of human glomerular endothelial cells through a possible signaling pathway involving phosphatidylinositol-3 kinase/protein kinase B and integrin alphaVbeta3.
• Antixenograft tumor activity of a humanized anti-insulin-like growth factor-I receptor monoclonal antibody is associated with decreased AKT activation and glucose uptake.
• CD8(+) T cells specific for both persistent and non-persistent viruses display distinct differentiation phenotypes but have similar level of PD-1 expression in healthy Chinese individuals.
• Evaluation of high-risk human papillomaviruses type distribution in cervical cancer in Sichuan province of China.
• Inhibition of cell growth and invasion by epidermal growth factor-targeted phagemid particles carrying siRNA against focal adhesion kinase in the presence of hydroxycamptothecin.
• Investigating light-use efficiency across a jack pine chronosequence during dry and wet years.
• Lymphocyte-Specific Compensation for XLF/Cernunnos End-Joining Functions in V(D)J Recombination.
• MAGI-2 Inhibits cell migration and proliferation via PTEN in human hepatocarcinoma cells.
• N-glycosylation affects the adhesive function of E-Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435.
• N-glycosylation at Asn residues 554 and 566 of E-cadherin affects cell cycle progression through extracellular signal-regulated protein kinase signaling pathway.
• Overexpression of integrin beta1 inhibits proliferation of hepatocellular carcinoma cell SMMC-7721 through preventing Skp2-dependent degradation of p27 via PI3K pathway.
• Prevention of Anastomotic Stricture with a Purse-string Suture Technique on the Gastric Side During Esophageal Carcinoma Operations: Retrospective Study of 463 Consecutive Cases.
• Restoring E-cadherin-mediated cell-cell adhesion increases PTEN protein level and stability in human breast carcinoma cells.
• Riemannian manifold learning.
• Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD.
• [Clinical analysis of primary facial nerve neuroma]
• [Comparative study on trace elements in natural colored cotton and white cotton]
• [Effects of CD4+ T cell transplantation on facial motoneuron survival in nude mice model with facial nerve axotomy]
• [Effects of nitrogen application rate on soil enzyme activities in wheat rhizosphere]
• [Expression of Snail and E-cadheein in pancreatic carcinoma and clinical significance thereof]
• [Expression of cystathionine gamma-lyase in cochlear spinal modiolar artery of rats]
• [Research advance in aerobic sludge granulation for wastewater biological treatment]
• [Retrospective analysis of 1062 cases consulted by an otolaryngology chief resident]
• [Treatment effects of the maxillary protraction in correction of maxillary deficiency: a comparative study between RPE group and no RPE group.]