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Literature summary for 2.4.1.144 extracted from

  • Pinho, S.S.; Figueiredo, J.; Cabral, J.; Carvalho, S.; Dourado, J.; Magalhaes, A.; Gaertner, F.; Mendonca, A.M.; Isaji, T.; Gu, J.; Carneiro, F.; Seruca, R.; Taniguchi, N.; Reis, C.A.
    E-cadherin and adherens-junctions stability in gastric carcinoma: Functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V (2012), Biochim. Biophys. Acta, 1830, 2690-2700.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene MGAT3, quantitative real-time PCR enzyme expression analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information GnT-III overexpression does not affect cell morphology. Gastric cells overexpressing GnT-III appears to exhibit a more focused immunolocalization at cell-cell borders than control cells. In GnT-III transfected cells there is a well-localized continuous staining of E-cadherin at the cell membrane that correlates with F-actin staining, suggesting co-localization, GnT-III overexpression prevents clathrin-dependent E-cadherin endocytosis, phenotype, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R Homo sapiens
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UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens Q09327 gene MGAT3
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Source Tissue

Source Tissue Comment Organism Textmining
epithelium
-
Homo sapiens
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gastric carcinoma cell
-
Homo sapiens
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MKN-45 cell
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Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R
-
Homo sapiens UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
-
?

Synonyms

Synonyms Comment Organism
GnT-III
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Homo sapiens
N-acetylglucosaminyltransferase III
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Homo sapiens
N-acetylglucosaminyltransferase-III
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Homo sapiens

General Information

General Information Comment Organism
metabolism existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview Homo sapiens
additional information GnT-III overexpression does not affect cell morphology Homo sapiens
physiological function the enzyme induces a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. The enzyme plays a role on E-cadherin-mediated tumor suppression Homo sapiens
physiological function GnT-III induced a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. Role of GnT-III on E-cadherin-mediated tumor suppression. GnT-III catalyzes the formation of a bisecting GlcNAc structure in N-glycans and is a metastases suppressor. E-cadherin is specifically modified with bisecting GlcNAc or beta1,6 GlcNAc branched structures Homo sapiens