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Information on EC 2.4.1.145 - alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase and Organism(s) Homo sapiens
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2.4.1.145 alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferaseIUBMB Comments
Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
gnt-iv, gnt-iva, mgat4a, gnt-ivb, n-acetylglucosaminyltransferase iv, mgat4b, gnt iv, n-acetylglucosaminyltransferase-iv, n-acetylglucosaminyltransferase iva, glcnactase-iv, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferase
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beta-acetylglucosaminyltransferase IV
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GnT-IVa
GnT-IVb
N-acetylglucosaminyltransferase IV
N-acetylglucosaminyltransferase-IVa
N-acetylglucosaminyltransferase-IVb
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV
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uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase IV
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N-acetylglucosaminyltransferase IV
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-beta-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
CAS REGISTRY NUMBER
COMMENTARY
86498-16-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[integrin beta1]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[integrin beta1]
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-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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-
-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + biantennary N-glycan
?
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the enzyme transfers a N-acetyl-D-glucosamine from UDP-N-acetyl-D-glucosamine to the biantennary oligosaccharide and produces triantennary N-glycans with a beta1,4-N-acetyl-D-glucosamine on the alpha1,3-Man arm
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-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
UDP + ?
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-
-
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
i.e. LAMP-2, LAMP-2 has 16 N-glycans which play crucial roles in cell adhesion to ECM and metastasis of cancer cells because N-glycans configure cell surface ligands of cancer cells for galectin-1, galectin-3, and selectins on extracellular matrix or the membranes of the counter cell
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?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
i.e. LAMP-2
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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-
-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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-
-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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-
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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GnT-IVa is primarily responsible for the biosynthesis of complex-type N-glycans
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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GnT-IVb might contribute to the basal GnT-IV activity in cells
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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the enzyme is involved in the branch formation of Asn-linked sugar chains
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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N-acetylglucosaminyltransferase-IVa
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-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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N-acetylglucosaminyltransferase-IVb
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-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
-
N-acetylglucosaminyltransferase-IVa
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-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
-
N-acetylglucosaminyltransferase-IVb
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-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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N-acetylglucosaminyltransferase-IVa
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-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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N-acetylglucosaminyltransferase-IVb
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
i.e. LAMP-2, LAMP-2 has 16 N-glycans which play crucial roles in cell adhesion to ECM and metastasis of cancer cells because N-glycans configure cell surface ligands of cancer cells for galectin-1, galectin-3, and selectins on extracellular matrix or the membranes of the counter cell
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-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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-
-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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GnT-IVa is primarily responsible for the biosynthesis of complex-type N-glycans
-
-
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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GnT-IVb might contribute to the basal GnT-IV activity in cells
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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the enzyme is involved in the branch formation of Asn-linked sugar chains
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.532 - 3.35
GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
1.04 - 6.94
GlcNAcbeta1-2Man1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
0.971 - 5.72
GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
3.19 - 10.5
GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
0.532
GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
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37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
3.35
GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
1.04
GlcNAcbeta1-2Man1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
6.94
GlcNAcbeta1-2Man1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
0.971
GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
5.72
GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
3.19
GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
10.5
GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
0.118
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
0.242
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
0.341
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
0.358
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comparison between normal and malignant chorionic cells
additional information
-
comparison between normal and malignant pancreatic cells
additional information
differences between isozymes expressed in COS7 cells
additional information
-
comparison between normal and malignant kidney cortex cells
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high expression of GnT-IVa, profiles and structures of the cell-surface N-glycan of hepatocellular carcinoma cells, high levels of NA3Fb, a core-alpha-1,6-fucosylated triantennary glycan, overview
additional information
in epirubicin-resistant HLE cells, GnT-IVa expression is decreased
in epirubicin-resistant HLE cells, GnT-IVb expression is increased
Panc-1, PCI6, MIA PaCa-2, and BxPC3. Down-regulation of GnT-IVa in pancreatic cancer cells is due to an epigenetic abnormality in the gene. When pancreatic cancer cells are treated with 5-aza-C or butyrate, the expression of GnT-IVa is dramatically increased
Panc-1, PCI6, MIA PaCa-2, and BxPC3. Expression of GnT-IVb is increased in pancreatic cancer, compared to normal pancreatic tissues
additional information
-
isoform GnT-IVb is ubiquitously and constitutively expressed among tissues
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
N-acetylglucosaminyltransferase-IV synthesizes the GlcNAcbeta(1-4) branch structure on the Manalpha(1-3) arm of N-glycan core, and is essential for the production of multiantennary N-glycans cooperatively with N-acetylglucosaminyltransferase-V
physiological function
malfunction
aberrant glycosylation of the cell surface is associated with the malignant transformation of normal cells. Tumor-cell-surface glycans are closely associated with tumor-cell migration, adhesion, and metastasis4, profiling of specific cell surface N-glycans in hepatocellular carcinoma with clinical tissues (88 tumor and adjacent normal tissues) and the corresponding serum samples of hepatocellular carcinoma patients, overview. The level of core-alpha-1,6-fucosylated triantennary glycan (NA3Fb) increases both on the cell surface and in the serum samples of hepatocellular carcinoma patients, and mRNA and protein expression of N-acetylglucosaminyltransferase IVa (GnT-IVa), which is related to the synthesis of the NA3Fb, is substantially increased in hepatocellular carcinoma tissues. Knockdown of GnT-IVa leads to a decreased level of NA3Fb and decreased ability of invasion and migration in HCC cells. The high expression of GnT-IVa is the cause of the abnormal increase of NA3Fb on the HCC cell surface, which regulates cell migration
malfunction
GnT-IVa overexpression increases cell adhesion, migration and invasion abilities of Jar cells. GnT-IVa overexpression increases cellular interaction with ECM as demonstrated by the relative adhesion rates of mock cells and Jar-GnT4a cells on fibronectin, collagen type I and collagen type IV. GnT-IVa knockdown in choriocarcinoma cells suppresses migration and invasion and decreases cellular adhesion to extracellular matrix
physiological function
the enzyme is involved in synthesis of tetra-antennary N-linked glycans. Cell surface glycans play an important role in intercellular and intracellular processes, including cell adhesion and development, cell recognition, and cancer development and metastasis. Changes in cell surface glycosylation modulate cellular activity
physiological function
N-acetylglucosaminyltransferase IV (GnT-IV) is a glycosyltransferase which catalyses the formation of beta1,4GlcNAc branches on the mannose core of N-glycans. beta1,4GlcNAc branches on human chorionic gonadotropin (hCG) are detected in GTN but not in normal pregnancy or hydatidiform mole. N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma. Identification of target proteins for GnT-IVa glycosylation which contribute to the malignancy of choriocarcinoma, overview. GnT-IVa overexpression increases highly branched N-glycans on integrin beta1. Highly branched N-glycans resulting from the action of GnT-IVa are strongly detected in invasive mole and choriocarcinoma, in proportion to the GnT-IVa protein expression. GnT-IVa may play an important role in accelerating the malignancy of choriocarcinoma through addition of beta1,4GlcNAc branches to the N-glycans on some proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MGT4A_HUMAN
535
1
61544
Swiss-Prot
Secretory Pathway (Reliability: 2)
MGT4B_HUMAN
548
1
63198
Swiss-Prot
Secretory Pathway (Reliability: 1)
MGT4C_HUMAN
478
1
56061
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
knockdown of GnT-IVa in 1668 cells and HepG2 cells by transfection with GnT-IVa shRNA. The level of NA3Fb decreases and M8 increases in knockdown GnT-IVa/1668 cells compared with GnT-IVa/NC after 48 h transfection. The scratch healing rates of the GnT-IVa/1668 group decreases more than the GnT-IVa/NC group. High expression of GnT-IVa leads to a higher level of NA3Fb in the HCC cell surface, and the downregulation of GnT-IVa may modulate cell invasion and migration through NA3Fb glycan
additional information
-
knockdown of GnT-IVa in 1668 cells and HepG2 cells by transfection with GnT-IVa shRNA. The level of NA3Fb decreases and M8 increases in knockdown GnT-IVa/1668 cells compared with GnT-IVa/NC after 48 h transfection. The scratch healing rates of the GnT-IVa/1668 group decreases more than the GnT-IVa/NC group. High expression of GnT-IVa leads to a higher level of NA3Fb in the HCC cell surface, and the downregulation of GnT-IVa may modulate cell invasion and migration through NA3Fb glycan
additional information
establishment of a choriocarcinoma cell line with GnT-IVa overexpression (Jar-GnT4a), and examination of its malignant potential and target proteins for GnT-IVa glycosylation. GnT-IVa overexpression increases the cell migration and invasion (2.5 and 1.4fold) as well as the ability to adhere to the extracellular matrix (ECM) components, including fibronectin and collagen type I and IV. The tumour formation potential of Jar-GnT4a in mice is significantly higher than that of control, and the cumulative survival rate of mice with Jar-GnT4a is relatively lower than those with control. Immunoprecipitation studies show that beta1,4GlcNAc branches of N-glycans on integrin beta1 in choriocarcinoma cells are increased by GnT-IVa overexpression
additional information
-
establishment of a choriocarcinoma cell line with GnT-IVa overexpression (Jar-GnT4a), and examination of its malignant potential and target proteins for GnT-IVa glycosylation. GnT-IVa overexpression increases the cell migration and invasion (2.5 and 1.4fold) as well as the ability to adhere to the extracellular matrix (ECM) components, including fibronectin and collagen type I and IV. The tumour formation potential of Jar-GnT4a in mice is significantly higher than that of control, and the cumulative survival rate of mice with Jar-GnT4a is relatively lower than those with control. Immunoprecipitation studies show that beta1,4GlcNAc branches of N-glycans on integrin beta1 in choriocarcinoma cells are increased by GnT-IVa overexpression
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Spodoptera frugiperda and Trichoplusia ni cells by using a baculovirus expression vector
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recombinant full-length enzyme and soluble truncated form tagged with FLAG sequence at the N-terminus. expressed in COS7 cells, N-acetylglucosaminyltransferase-IVa
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recombinant full-length enzyme and soluble truncated form tagged with FLAG sequence at the N-terminus. expressed in COS7 cells, N-acetylglucosaminyltransferase-IVb
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
-
it is necessary to select appropriate host cell lines according to their glycosyltransferases activity balance to produce glycoproteins with an objective sugar chain structure. The descibed method of grouping cell lines according to their glycosyltransferases activity balance is useful to select appropriate host cells
medicine
-
enzyme activity in tissue from patients with extrahepatic bile duct carcinoma remains unchanged
medicine
-
enzyme activity is elevated in three choriocarcinoma cell lines compared to normal placenta. Activity in JEG-3 cells is 29 times higher than normal
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhu, T.Y.; Chen, H.L.; Gu, J.X.; Zhang, Y.F.; Zhang, Y.K.; Zhang, R.A.
Changes in N-acetylglucosaminyltransferase III, IV, and V in renal cell carcinoma
J. Cancer Res. Clin. Oncol.
123
296-299
1997
Homo sapiens
Yoshida, A.; Minowa, M.T.; Takamatsu, S.; Hara, T.; Ikenaga, H.; Takeuchi, M.
A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment
Glycoconjugate J.
15
1115-1123
1998
Homo sapiens (Q9UQ53), Homo sapiens
Nan, B.C.; Shao, D.M.; Chen, H.L.; Huang, Y.; Gu, J.X.; Zhang, Y.B.; Wu, Z.G.
Alteration of N-acetylglucosaminyltransferases in pancreatic carcinoma
Glycoconjugate J.
15
1033-1037
1998
Homo sapiens
Yoshida, A.; Minowa, M.T.; Takamatsu, S.; Hara, T.; Oguri, S.; Ikenaga, H.; Takeuchi, M.
Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase
Glycobiology
9
303-310
1999
Homo sapiens (Q9UM21), Homo sapiens
Takamatsu, S.; Oguri, S.; Minowa, M.T.; Yoshida, A.; Nakamura, K.; Takeuchi, M.; Kobata, A.
Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain
Cancer Res.
59
3949-3953
1999
Homo sapiens
Takamatsu, S.; Inoue, N.; Katsumata, T.; Nakamura, K.; Fujibayashi, Y.; Takeuchi, M.
The relationship between the branch-forming glycosyltransferases and cell surface sugar chain structures
Biochemistry
44
6343-6349
2005
Homo sapiens
Jin, X.L.; Liu, H.B.; Zhang, Y.; Wang, B.S.; Chen, H.L.
Alteration in N -acetylglucosaminyltransferase activities and glycan structure in tissue and bile glycoproteins from extrahepatic bile duct carcinoma
Glycoconj. J.
20
399-406
2004
Homo sapiens
Takamatsu, S.; Katsumata, T.; Inoue, N.; Watanabe, T.; Fujibayashi, Y.; Takeuchi, M.
Abnormal biantennary sugar chains are expressed in human chorionic gonadotropin produced in the choriocarcinoma cell line, JEG-3
Glycoconj. J.
20
473-481
2004
Homo sapiens
Ide, Y.; Miyoshi, E.; Nakagawa, T.; Gu, J.; Tanemura, M.; Nishida, T.; Ito, T.; Yamamoto, H.; Kozutsumi, Y.; Taniguchi, N.
Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer
Biochem. Biophys. Res. Commun.
341
478-482
2006
Homo sapiens (Q9UM21), Homo sapiens (Q9UQ53)
Oguri, S.; Yoshida, A.; Minowa, M.T.; Takeuchi, M.
Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes
Glycoconj. J.
23
473-480
2006
Homo sapiens
Kim, N.Y.; Kim, H.G.; Kim, Y.H.; Chung, I.S.; Yang, J.M.
Expression and characterization of human N-acetylglucosaminyltransferases and alpha2,3-sialyltransferase in insect cells for in vitro glycosylation of recombinant erythropoietin
J. Microbiol. Biotechnol.
18
383-391
2008
Homo sapiens
Kudo, T.; Nakagawa, H.; Takahashi, M.; Hamaguchi, J.; Kamiyama, N.; Yokoo, H.; Nakanishi, K.; Nakagawa, T.; Kamiyama, T.; Deguchi, K.; Nishimura, S.; Todo, S.
N-glycan alterations are associated with drug resistance in human hepatocellular carcinoma
Mol. Cancer
6
32
2007
Homo sapiens (Q9UM21), Homo sapiens (Q9UQ53), Homo sapiens
Nagels, B.; Van Damme, E.J.; Pabst, M.; Callewaert, N.; Weterings, K.
Production of complex multiantennary N-glycans in Nicotiana benthamiana plants
Plant Physiol.
155
1103-1112
2011
Homo sapiens
Ohtsubo, K.
Biological significance of N-acetylglucosaminyltransferase-IV-mediated protein glycosylation on the homeostasis of cellular physiological functions
Trends Glycosci. Glycotechnol.
23
103-105
2011
Bos taurus, Homo sapiens
-
Nie, H.; Liu, X.; Zhang, Y.; Li, T.; Zhan, C.; Huo, W.; He, A.; Yao, Y.; Jin, Y.; Qu, Y.; Sun, X.L.; Li, Y.
Specific N-glycans of hepatocellular carcinoma cell surface and the abnormal increase of core-alpha-1,6-fucosylated triantennary Glycan via N-acetylglucosaminyltransferases-IVa regulation
Sci. Rep.
5
16007
2015
Homo sapiens (Q9UM21), Homo sapiens
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