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UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactose
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactose
-
minimum requirement for acceptor structure
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactose
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactose
-
best substrate
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-(Gly)Ser-(Gly-Glu)
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-(Gly)Ser-(Gly-Glu)
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser-peptide
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-xylosyl-1-O-Ser-peptide
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,4-beta-D-glucose
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,4-beta-D-glucose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
additional information
?
-
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
i.e. linkage tetrasaccharide, synthetic substrate
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
best acceptor substrate together with chondroitin polysaccharide
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1,3-beta-D-galactosyl-beta-D-xylose-O-methoxyphenyl
transfers GalNAc to GlcA at the non-reducing terminus of the linkage tetrasacharide
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
UDP + N-acetyl-D-galactosamine-1,4-beta-D-glucuronyl-1,3-beta-D-galactosyl-1-O-C2H4-NH-benzyloxycarbonyl
-
-
-
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
a phosphorylated tetrasaccharide linkage structure in ChGn-1-/- growth plate cartilage but not in ChGn-2-/- or wild-type growth plate cartilage, preferred substrate of ChGn-1
-
-
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
a phosphorylated tetrasaccharide linkage structure in ChGn-1-/- growth plate cartilage but not in ChGn-2-/- or wild-type growth plate cartilage, preferred substrate of ChGn-1
-
-
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
-
-
-
?
UDP-N-acetyl-D-galactosamine + GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
UDP + N-acetyl-D-galactosaminyl-1-4beta-D-GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin
-
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
-
acceptors are tri- or disaccharides with terminal glucuronyl residue and a galactosyl residue in penultimate position, transfers acetylgalactosamine in beta-linkage, no substrates are glucuronic acid or disaccharides with terminal galactosyl residues
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminyl-1,4-beta-D-glucuronylgalactosyl glycosides
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
involved in chondroitin sulfate biosynthesis: transfer of the first N-acetylgalactosamine residue
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in chondroitin initiation and elongation
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
-
-
?
additional information
?
-
-
GalNAcT activity of the recombinant enzyme is determined using a trisaccharide analogue of the linkage region linked to a chromophoric aglycone, GlcA-beta1,3-Gal-beta1,3-Gal-O-methoxyphenyl, i.e. GlcA-Gal-Gal-OMP, as a acceptor substrate, Km is 3.8 mM, and with only the trisaccharide GlcA-beta1,3-Gal-beta1,3-Gal, Km 3.39 mM, no activity with Gal-Gal-OMP. The enzyme activity is even higher with 4- and 6-sulfated GlcA-Gal-Gal-OMP, kM values are 0.6 mM and 1.0 mm, respectively, no activity with 6-disulfated GlcA-Gal-Gal-OMP
-
-
?
additional information
?
-
-
in vitro chondroitin polymerization does not occur on the non-reducing terminal GalNAc-linkage pentasaccharide structure
-
-
?
additional information
?
-
no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
-
-
?
additional information
?
-
no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
-
-
?
additional information
?
-
no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
-
-
?
additional information
?
-
no activity with GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)-1-O-thrombomodulin and GlcUAbeta1-3Galbeta1-3Galbeta1-4Xyl(2-O-phosphate)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
additional information
?
-
-
in vitro chondroitin polymerization does not occur on the non-reducing terminal GalNAc-linkage pentasaccharide structure
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
?
UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan
UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
involved in chondroitin sulfate biosynthesis: transfer of the first N-acetylgalactosamine residue
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
-
involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in chondroitin initiation and elongation
-
-
?
UDP-N-acetyl-D-galactosamine + glucuronylgalactosyl glycosides
UDP + N-acetyl-D-galactosaminylglucuronylgalactosyl glycosides
involved in the biosynthesis of chodroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core.
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(E)-2-hydroxy-3-isopentyl-4-methoxy-6-styrylbenzoic acid
-
(E)-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoic acid
-
(E)-2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)vinyl)-benzoic acid
-
(E)-3-(3,7-dimethylocta-2,6-dienyl)-2-hydroxy-4-methoxy-6-phenethylbenzoic acid
-
(E)-3-c-6-hydroxy-4-methoxy-5-prenyl-2-styrylbenzoic acid
-
(E)-3-methoxy-4-(3-methylbut-2-enyl)-5-styrylphenol
i.e. longistyline C
(E)-6-(2-chlorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(2-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(3-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(4-fluorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(4-hydroxystyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(4-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-6-(but-1-enyl)-2-hydroxy-4-methoxy-3-prenylbenzoic acid
-
(E)-ethyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
(E)-isopropyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
(E)-methyl 2-hydroxy-3-isopentyl-4-methoxy-6-styrylbenzoate
-
(E)-methyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-(2-phenylprop-1-enyl)benzoate
-
(E)-methyl 2-hydroxy-4-methoxy-3-prenyl-6-(2-(thiophen-2-yl)-vinyl)benzoate
-
(E)-methyl 6-(2-chlorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(2-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(3-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-(tert-butyldimethylsilyloxy)styryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-fluorostyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-hydroxystyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(4-methylstyryl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-(but-1-enyl)-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-methyl 6-styryl-2-hydroxy-4-methoxy-3-prenylbenzoate
-
(E)-N-cyclopropyl-2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzamide
-
(E)-tert-butyl 2-hydroxy-4-methoxy-3-(3-methylbut-2-enyl)-6-styrylbenzoate
-
2-hydroxy-3-isopentyl-4-methoxy-6-phenethylbenzoic acid
-
2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoic acid
-
2-hydroxy-4-methoxy-3-prenyl-6-phenethylbenzoic acid
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cajanine
cajanine is a stilbenic component isolated from Cajanus cajan, it is identified as a potent hepatitis C virus (HCV) inhibitor by phenotypic screening with EC50 of 0.00317 mM. Cajanine inhibits HCV infection by targeting cellular CSGalNAcT-1 protein destabilizing the protein. Cajanine does not inhibit HCV replication at the replicative steps of HCV life cycle. CSGalNAcT-1 is important to support HCV replication at the early stage. Structure-activity relationships and the mechanism of action, and analysis of cajanine derivatives, EC50 values, overview. Cajanine might inhibit HCV replication at early steps of the viral life cycle via downregulating of cellular CSGalNAcT-1
methyl 2-hydroxy-4-methoxy-3-prenyl-6-((1E,3E)-4-phenylbuta-1,3-dienyl)benzoate
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methyl 2-hydroxy-4-methoxy-3-prenyl-6-phenethylbenzoate
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additional information
2-hydroxy-4-methoxy-6-[(E)-2-phenylethenyl]benzoic acid is not inhibitory
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additional information
heparan sulfate-synthesis enzymes inhibits chondroitin sulfate as extracellular inhibitor of axon growth
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evolution
the CSGALNACT1 and CSGALNACT2 isozymes enzymes both have a GT7 catalytic domain with beta(1->4)-N-acetylgalactosaminyl transferase
malfunction
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chondroitin sulfate production is reduced by approximately half in CSGalNAcT1-null mice, and the amount of short-chain CS is also reduced compared to wild-type mice. CSGalNAcT1-null mice have reduced skeletal growth, thickness of the growth plate is reduced, and the cartilage of the null mice is significantly smaller than that of wild-type mice, phenotype, overview
malfunction
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Chsy1-/- mice show a profound limb patterning defect in which orthogonally shifted ectopic joints form in the distal digits. Associated with the digit-patterning defect is a shift in cell orientation and an imbalance in chondroitin sulfation. Chondrogenesis is impaired as early as E13.5 in Chsy1-/- embryos. Ectopic, split digit phenotype, overview
malfunction
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CSS2 knockout chondrocyte culture systems, together with siRNA of CSS1, reveal the presence of two CS chain species in length, suggesting two steps of CS chain polymerization; i.e., elongation from the linkage region up to Mr of about 10000 and further extension
malfunction
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deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the numbers of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Knockdown of ChGn-1 decreases chondroitin sulfate levels in L cells, chondroitin sulfate chain lengths in L-shRNAChGn-1-1, L-shRNA ChGn-1-2, and mock-transfected murine L cells, overview
malfunction
missense mutations are found in gene ChGn-1 in exon 5, H234R, and exon 10, M509R, respectively, in two patients with neuropathy. The mutations might be associated with the pathogenetic mechanisms of the peripheral neuropathies
malfunction
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the growth plate of Csgalnact1-/- mice contains shorter and slightly disorganized chondrocyte columns with a reduced volume of the extracellular matrix principally in the proliferative layer. Immunohistochemical analysis reveals that the level of both aggrecan and link protein 1 are decreased in Csgalnact1-/- cartilage with an increase in processed forms of aggrecan core protein, phenotype, overview
malfunction
deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the number of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Accumulation of phosphorylated pentasaccharide and tetrasaccharide linkages in ChGn-1-/- growth plate cartilage
malfunction
knockdown of CSGalNAcT2 inhibits infectious bursal disease virus replication involving the integrity of the Golgi apparatus
malfunction
mice carrying a gene knockout for chondroitin sufate N-acetylgalactosaminyltransferase-1, mutant T1KO, recover more completely from spinal cord injury than wild-type mice and even chondroitinase ABC-treated mice. Synthesis of heparan sulfate, a glycosaminoglycan promoting axonal growth, is also upregulated in TI knockout mice because heparan sulfate-synthesis enzymes are induced in the mutant neurons. Chondroitinase ABC treatment never induces heparan sulfate upregulation. T1KO mice are viable, but they have abnormal bone development and 10% shorter bodies compared to wild-type mice. Reduced chondroitin sulfate levels are associated with reduced scar formation in T1KO mice. Phenotype of enzyme knockout mutant mice, overview
malfunction
the enzyme is downregulated in Kashin-Beck disease (KBD), an endemic degenerative osteoarthritis, and in primary osteoarthritis, both associated with extracellular matrix degradation. Enzyme CSGalNAcT-1 may be involved in the damage of articular cartilage of Kashin-Beck disease and osteoarthritis by regulating Hapln-1 in the Wnt/beta-catenin signalling pathway. Alterations of involved enzyme expressions in CSGalNAcT gene network in case of Kashin-Beck disease and osteoarthritis
malfunction
abnormalities in perineuronal nets and behavior are observed in mice lacking CSGalNAcT1. Loss of this enzyme reduces the amount of chondroitin sulfate (CS) by approximately 50% in various brain regions. The amount of CS in perineuronal nets (PNNs) is also diminished in T1KO compared to wild-type mice, although the amount of a major CS proteoglycan core protein, aggrecan, is not changed. In T1KO, abnormalities in several behavioral tests, including the open-field test, acoustic startle response, and social preference are observed. Phenotype, overview
malfunction
after silencing of endogenous CSGalNAcT-1 with specific siRNA, the intracellular hepatitis C virus (HCV) RNA load is largely reduced, and the HCV core protein is declined as well
malfunction
chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1) deficiency results in a mild skeletal dysplasia and joint laxity
malfunction
impaired chndroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality, whereas t2 KO mice show normal size and skeletal development. Col2-DKO mice survive to adulthood and show severe dwarfism. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. Phenotype of t2 null mice, overview
malfunction
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
malfunction
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
malfunction
t1 single knockout mice (t1 KO) exhibit slight dwarfism and a reduction in chondroitin sulfate (CS) content in cartilage compared with wild-type mice. Impaired chondroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality. Col2-DKO mice survive to adulthood and show severe dwarfism compared with t1 KO mice. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. The CS content in DKO cartilage is decreased compared with that in t1 KO cartilage
malfunction
T1KO mice show microscopic abnormalities in the CNS, but are fertile and viable. They have 10% smaller body sizes than wild-type mice due to abnormal skeletal development
malfunction
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the growth plate of Csgalnact1-/- mice contains shorter and slightly disorganized chondrocyte columns with a reduced volume of the extracellular matrix principally in the proliferative layer. Immunohistochemical analysis reveals that the level of both aggrecan and link protein 1 are decreased in Csgalnact1-/- cartilage with an increase in processed forms of aggrecan core protein, phenotype, overview
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malfunction
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saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1). rVAR2 inhibits cellular migration, invasion, and anchorage independent growth in cancer. rVAR2 interacts with chondroitin sulfate glycosaminoglycan (ofCS)-modified proteoglycans
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malfunction
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deficiency in chondroitin N-acetylgalactosaminyltransferase-1 reduces the number of chondroitin sulfate chains, leading to skeletal dysplasias in mice. Accumulation of phosphorylated pentasaccharide and tetrasaccharide linkages in ChGn-1-/- growth plate cartilage
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malfunction
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t1 single knockout mice (t1 KO) exhibit slight dwarfism and a reduction in chondroitin sulfate (CS) content in cartilage compared with wild-type mice. Impaired chondroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality. Col2-DKO mice survive to adulthood and show severe dwarfism compared with t1 KO mice. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. The CS content in DKO cartilage is decreased compared with that in t1 KO cartilage
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malfunction
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impaired chndroitin sulfate (CS) content in cartilage and induction of abnormal endochondral ossification is caused by t1::t2 (CSGALNACT1/CSGALNACT2) double deficiency. DKO mice exhibit postnatal lethality, whereas t2 KO mice show normal size and skeletal development. Col2-DKO mice survive to adulthood and show severe dwarfism. Histological analysis of epiphyseal cartilage from Col2-DKO mice reveals disrupted endochondral ossification, characterized by drastic GAG reduction in the extracellular matrix. DKO cartilage has reduced chondrocyte proliferation and an increased number of apoptotic chondrocytes compared with wild-type cartilage. Conversely, primary chondrocyte cultures from Col2-DKO knee cartilage have the same proliferation rate as wild-type chondrocytes and low GAG expression levels, indicating that the chondrocytes themselves have an intact proliferative ability. Quantitative RT-PCR analysis of E18.5 cartilage shows that the expression levels of Col2a1 and Ptch1 transcripts tend to decrease in DKO compared with those in wild-type mice. Phenotype of t2 null mice, overview
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malfunction
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chondroitin sulfate production is reduced by approximately half in CSGalNAcT1-null mice, and the amount of short-chain CS is also reduced compared to wild-type mice. CSGalNAcT1-null mice have reduced skeletal growth, thickness of the growth plate is reduced, and the cartilage of the null mice is significantly smaller than that of wild-type mice, phenotype, overview
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metabolism
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chondroitin sulfate biosynthetic pathway and relevant glycosyltransferases, overview
metabolism
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CSS1 and CSS2 differently contribute to chondroitin sulfate biosynthesis, mechanism of chondroitin sulfate biosynthesis, overview. CSS1 participates in both the chondroitin sulfate chain initiation and polymerization, and CSS2 participates in the polymerization, especially in further extension
metabolism
chondroitin sulfate N-acetylgalactosaminyl-transferase-1 is a key enzyme in chondroitin sulfate biosynthesis
metabolism
the enzyme belongs to the zebrafish CS/DS glycosyltransferases are spatially and temporally expressed. Ooverlapping expression of multiple glycosyltransferases coincides with high CS/DS deposition. Efficient CS/DS biosynthesis requires a combination of several glycosyltransferases
metabolism
the enzyme belongs to the zebrafish CS/DS glycosyltransferases are spatially and temporally expressed. Overlapping expression of multiple glycosyltransferases coincides with high CS/DS deposition. Efficient CS/DS biosynthesis requires a combination of several glycosyltransferases
metabolism
CSGalNAcT-1 plays a role in chondroitin sulfate and dermatan sulfate synthesis
metabolism
CSGalNAcT1 is a key enzyme in chondroitin sulfate synthesis. Chondroitin sulfate (CS) is an important glycosaminoglycan and is mainly found in the extracellular matrix as CS proteoglycans. In the brain, CS proteoglycans are highly concentrated in perineuronal nets (PNNs), which surround synapses and modulate their functions
metabolism
six glycosyltransferases are known to coordinately synthesize the backbone structure of chondroitin sulfate (CS). Two glycosyltransferases, Csgalnact1 (t1) and Csgalnact2 (t2), are critical for initiation of CS synthesis in vitro. According to an in vitro enzymatic characterization, among the six CS glycosyltransferases, only t1 and t2 possessed the ability to independently initiate CS synthesis. t1 efficiently transfers GalNAc onto the linkage tetrasaccharide in vitro, which is common to both CS and heparin sulfate/heparin, and t1 initiation activity is stronger than that of t2
metabolism
the first step (GalNAc transfer) of chondroitin sulfate (CS) backbone synthesis is performed by at least two isoforms, CSGALNACT1 (T1) and CSGALNACT2 (T2), which are expressed in different organs, CS metabolism, roles of CS and perineuronal nets (PNNs) in brain function from the perspective of CS synthesis, overview
metabolism
the first step (GalNAc transfer) of chondroitin sulfate (CS) backbone synthesis is performed by at least two isoforms, CSGALNACT1 (T1) and CSGALNACT2 (T2), which are expressed in different organs, CS metabolism, roles of CS and perineuronal nets (PNNs) in brain function from the perspective of CS synthesis, overview
metabolism
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chondroitin sulfate biosynthetic pathway and relevant glycosyltransferases, overview
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metabolism
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six glycosyltransferases are known to coordinately synthesize the backbone structure of chondroitin sulfate (CS). Two glycosyltransferases, Csgalnact1 (t1) and Csgalnact2 (t2), are critical for initiation of CS synthesis in vitro. According to an in vitro enzymatic characterization, among the six CS glycosyltransferases, only t1 and t2 possessed the ability to independently initiate CS synthesis. t1 efficiently transfers GalNAc onto the linkage tetrasaccharide in vitro, which is common to both CS and heparin sulfate/heparin, and t1 initiation activity is stronger than that of t2
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physiological function
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ChGn-1 initiates chondroitin sulfate biosynthesis by transferring the first N-acetylgalactosamine to the tetrasaccharide in the protein linkage region of chondroitin sulfate, overview. c-2 efficiently transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate to position 4 of non-reducing terminal GalNAc-linkage residues, and the number of chondroitin chains is regulated by the expression levels of C4ST-2 and of ChGn-1. C4ST-2 plays a key role in regulating levels of chondroitin sulfate synthesized via ChGn-1, overview
physiological function
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chondroitin sulfate N-acetylgalactosaminyltransferase 1, CSGalNAcT-1, participates in the chondroitin sulfate chain initiation and is necessary for normal endochondral ossification and aggrecan metabolism
physiological function
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chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required for normal cartilage development
physiological function
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chondroitin sulfate N-acetylgalactosaminyltransferase-1, CSGalNAcT-1, is involved in chondroitin sulfate initiation, but not in elongation
physiological function
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Chsy1 catalyzes the extension of chondroitin and dermatan sulfate glycosaminoglycans and is an essential regulator of joint patterning
physiological function
ChGn-1 is a key enzyme for production of chondroitin sulfate proteoglycans The clinical course of multiple sclerosis is influenced by the level of expression of the ChGn-1 gene. Chondroitin sulfate proteoglycans are a constituent of the matrix of the central nervous system (CNS), likely participating as regulatory molecules in the process of demyelination, remyelination, axonaldegeneration and regeneration in the CNS
physiological function
chondroitin N-acetylgalactosaminyltransferase-1 regulates the number of chondroitin sulfate chains for normal cartilage development. ChGn-1-mediated addition of N-acetylgalactosamine is accompanied by rapid 2-phosphoxylose phosphatase XYLP-dependent dephosphorylation during formation of the CS linkage region. ChGn-1 and XYLP cooperatively regulate the number of chondroitin sulfate chains in growth plate cartilage
physiological function
chondroitin sulfate N-acetylgalactosaminyl-transferase-1 is an essential enzyme in chondroitin sulfate metabolism and participates in chondroitin sulfate chain formation of aggrecan, and plays an important role in degenerative extracellular matrix of cartilage
physiological function
chondroitin sulfate N-acetylgalactosaminyltransferase-2 contributes to the replication of infectious bursal disease virus, IBDV, via interaction with capsid protein VP2. Overexpression of CSGalNAcT2 promotes IBDV replication in DF1 cells involving the integrity of the Golgi apparatus
physiological function
the enzyme is involved in chondroitin sulfate biosynthesis. Chondroitin/dermatan sulfate (CS/DS) proteoglycans present in the extracellular matrix have important structural and regulatory functions. CS/DS is a ubiquitous component of multicellular organisms with mechanical functions in cartilage, but also is required for fundamental processes such as cell division and cytokinesis. The CSGALNACT1 and CSGALNACT2 isozymes initiate CS/DS formation by the addition of a GalNAc residue to a proteoglycan tetrasaccharide linkage region attached to a core protein, but may also participate in the later steps of CS/DS polymerization
physiological function
the enzyme is involved in chondroitin sulfate biosynthesis. Chondroitin/dermatan sulfate (CS/DS) proteoglycans present in the extracellular matrix have important structural and regulatory functions. The CSGALNACT1 and CSGALNACT2 isozymes initiate CS/DS formation by the addition of a GalNAc residue to a proteoglycan tetrasaccharide linkage region attached to a core protein, but may also participate in the later steps of CS/DS polymerization
physiological function
both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. Enzyme t1 and t2 are known to function in both initiation and elongation activity. t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
physiological function
both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. t1 and t2 are known to function in both initiation and elongation activity. Enzyme t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
physiological function
chondroitin sulfate N-acetylgalactosaminyltransferase 1 initiates synthesis of chondroitin sulfate side chains attached to a core protein of aggrecan, which is a predominant disc matrix component
physiological function
CSGalNAcT-1 is essential for hepatitis C virus (HCV) replication in human cells
physiological function
CSGALNACT1 encodes chondroitin sulfate N-acetylgalactosaminyltransferase-1 (CSGalNAcT-1, ChGn-1), which initiates chondroitin sulfate (CS) chain biosynthesis on the so-called GAG-protein linker region tetrasaccharide
physiological function
enzyme CSGalNAcT1 is important for plasticity, probably due to regulation of CS-dependent perineuronal nets (PNNs). It plays an important role in supplying CS for PNN development and brain functions related to several characteristic behaviors
physiological function
enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
physiological function
the enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
physiological function
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chondroitin sulfate N-acetylgalactosaminyltransferase 1, CSGalNAcT-1, participates in the chondroitin sulfate chain initiation and is necessary for normal endochondral ossification and aggrecan metabolism
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physiological function
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enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) are key players in the core chondroitin sulfate (CS) synthesis. Oncofetal chondroitin sulfate glycosaminoglycans (ofCSs) are key players in integrin signaling and tumor cell motility, overview
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physiological function
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chondroitin N-acetylgalactosaminyltransferase-1 regulates the number of chondroitin sulfate chains for normal cartilage development. ChGn-1-mediated addition of N-acetylgalactosamine is accompanied by rapid 2-phosphoxylose phosphatase XYLP-dependent dephosphorylation during formation of the CS linkage region. ChGn-1 and XYLP cooperatively regulate the number of chondroitin sulfate chains in growth plate cartilage
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physiological function
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both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. Enzyme t1 and t2 are known to function in both initiation and elongation activity. t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
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physiological function
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both chondroitin sulfate N-acetylgalactosaminyltransferase 1 (t1) and chondroitin sulfate N-acetylgalactosaminyltransferase 2 (t2) are necessary for chondroitin sulfate (CS) synthesis and normal chondrocyte differentiation but are not sufficient for all CS synthesis in cartilage. CS biosynthesis is initiated by the transfer of GalNAc residues to the linkage region, which consists of tetrasaccharide units of GlcUA-beta1,3-galactose (Gal)-beta1,3-Gal-beta1,4-xylose (Xyl) attached to the serine residues of the core proteins. This triggers CS elongation by alternating addition of GalNAc and GlcUA residues, which is catalyzed by six glycosyltransferases in mammals. t1 and t2 are known to function in both initiation and elongation activity. Enzyme t1 exhibits stronger initiation activity than t2, indicating that t1 has a vital role in CS synthesis initiation
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physiological function
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chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required for normal cartilage development
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additional information
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the enzyme occurs in a heterooligomer complex, chondroitin sulfate synthase-1 (CSS1)/chondroitin synthase-1
additional information
proportion of linkage region saccharides from wild-type, ChGn-1-/-, or ChGn-2-/- cartilage, overview
additional information
proportion of linkage region saccharides from wild-type, ChGn-1-/-, or ChGn-2-/- cartilage, overview
additional information
quantitative analysis of six CS glycosyltransferase transcripts using real-time RT-PCR
additional information
quantitative analysis of six CS glycosyltransferase transcripts using real-time RT-PCR
additional information
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proportion of linkage region saccharides from wild-type, ChGn-1-/-, or ChGn-2-/- cartilage, overview
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additional information
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quantitative analysis of six CS glycosyltransferase transcripts using real-time RT-PCR
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H234R
naturally occuring mutation in exon 5 of gene ChGn1, the mutant shows neuropathy, Bells palsy and/or hereditary motor and sensory neuropathy, the mutant enzyme is inactive
M509R
naturally occuring mutation in exon 10 of gene ChGn1, the mutant shows neuropathy, Bells palsy and/or hereditary motor and sensory neuropathy, the mutant enzyme is inactive
P384R
site-directed mutagenesis, almost inactive mutant
S126L
naturally occuring inactive ChGN1 mutant
additional information
overexpression and siRNA-mediated knockdown of gene CSGalNAcT2 in DF1 cells
additional information
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overexpression and siRNA-mediated knockdown of gene CSGalNAcT2 in DF1 cells
additional information
bi-allelic loss-of-function mutations in CSGALNACT1 produce a skeletal dysplasia reminiscent of the skeletal dysplasia of Csgalnact1-/- mice, and adds to the genetic heterogeneity of Desbuquois dysplasia (DD)
additional information
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bi-allelic loss-of-function mutations in CSGALNACT1 produce a skeletal dysplasia reminiscent of the skeletal dysplasia of Csgalnact1-/- mice, and adds to the genetic heterogeneity of Desbuquois dysplasia (DD)
additional information
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycans (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
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saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core chondroitin sulfate (CS) synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycans (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
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in cmd mice (known as natural aggrecan-null mice) the heterozygote and homozygote cartilage exhibit about 50% and about 9% aggrecan gene transcription respectively. In the cmd heterozygote cartilage, chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression is dimnished to about 30% that of the wild type. In the cmd homozygote cartilage, chondroitin sulfate N-acetylgalactosaminyltransferase-1 expression furhter decreases to a low level.
additional information
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construction of CSGalNAcT1-null mice by homologous recombination using an embryonic stem cell line, RENKA, developed from the wild-type C57BL/6N strain
additional information
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construction of L-shRNA ChGn-1-1 and L-shRNA ChGn-1-2 transfected L cells, and analysis of chondroitin sulfate chain lengths. The silencing of the genes results in a 60-80% reduction in steady-state ChGn-1 mRNA and an 18-22% decrease in CS when compared with control L cells. Overexpression of ChGn-1 slightly increases CS levels in L cells
additional information
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downregulation of CSS1 by siRNA
additional information
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generation of Csgalnact1-/- mice by using a targeting vector for Csgalnact1 gene disruption
additional information
construction of enzyme knockout mutant ChGn-1-/-
additional information
construction of enzyme knockout mutant ChGn-1-/-
additional information
construction of enzyme knockout mutant ChGn-2-/-
additional information
construction of enzyme knockout mutant ChGn-2-/-
additional information
construction of RNAi-mediated gene Csgalnact1 knockout mice, mutant T1KO. T1KO mice are viable, but they have abnormal bone development and 10% shorter bodies compared to wild-type mice. Heparan sulfate synthesis increases in injured spinal cords of T1KO mice
additional information
generation of mice that are deficient in the CS synthesizing enzyme, CSGalNAcT1 (T1KO)
additional information
generation of single knockout T1 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, pgenotype, overview
additional information
generation of single knockout T1 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, pgenotype, overview
additional information
generation of single knockout T2 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, phenotype, overview
additional information
generation of single knockout T2 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, phenotype, overview
additional information
saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
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saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
additional information
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generation of Csgalnact1-/- mice by using a targeting vector for Csgalnact1 gene disruption
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additional information
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saturating concentrations of rVAR2 inhibit downstream integrin signaling, which is mimicked by knockdown of the core CS synthesis enzymes beta-1,3-glucuronyltransferase 1 (B3GAT1) and chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CSGALNACT1) via siRNA. The oncofetal chondroitin sulfate glycosaminoglycan chains (ofCS) modification is highly expressed in both human and murine metastatic lesions in situ and pre-incubation or early intravenous treatment of tumor cells with rVAR2-inhibited seeding and spreading of tumor cells in mice
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additional information
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construction of enzyme knockout mutant ChGn-1-/-
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additional information
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generation of single knockout T1 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, pgenotype, overview
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additional information
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construction of enzyme knockout mutant ChGn-2-/-
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additional information
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generation of single knockout T2 KO mutant and of double knockout mutant Col2-DKO, a chondrocyte-specific t1::t2 KO mutant, quantitative RT-PCR analysis of knee cartilage shows no or slight t1 and t2 gene expression in Col2-DKO mice compared with wild-type mice. t1::t2 double KO mice show severe dwarfism and postnatal lethality, phenotype, overview
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additional information
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construction of CSGalNAcT1-null mice by homologous recombination using an embryonic stem cell line, RENKA, developed from the wild-type C57BL/6N strain
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Homo sapiens (Q8TDX6), Homo sapiens
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