EC Number   |
General Information |
Reference |
|---|
    2.8.2.5 | evolution |
there are three major C4ST isoforms in Homo sapiens, C4ST-1, C4ST-2, and C4ST-3. Based on a general amino acid sequence analysis, C4STs contain a single cytoplasmic domain followed by helical transmembrane domain and a lumenal domain. C4ST-1 has two additional variants, and both are capable of sulfating unsulfated chondroitin and dermatan with a preference of D-glucuronic acid (GlcA)->GalNAc over L-iduronic acid (IdoA)->GalNAc. C4ST-2 has a lower activity towards unsulfated dermatan than does C4ST-1 |
760408 |
| 2.8.2.5 | malfunction |
arm regeneration is impaired by sulfate deprivation |
761216 |
| 2.8.2.5 | malfunction |
C4ST-1 activity and C4S production are upregulated in human glioma tissues, when compared to normal brain tissue, and the extent of upregulation positively correlates with glioma malignancy. Inhibition of expression of the two CS synthetic enzymes chondroitin 4-O-sulfotransferase-1 (C4ST-1/CHST11) and chondroitin 6-O-sulfotransferase-1 (C6ST-1/CHST3, EC 2.8.2.17) suppress cell viability, migration and invasion, reduce MMP-2 and MMP-9 expression, and reduce N-cadherin expression, but increase E-cadherin levels. Clinicopathological features, overview |
761061 |
| 2.8.2.5 | malfunction |
enzyme deletion mutants exhibit reduced survival rates after synchronization with sodium hypochlorite |
-, 738697 |
| 2.8.2.5 | malfunction |
even though C4ST-1 and C4ST-2 exhibit broad and overlapping mRNA expression patterns, indicating the functional redundancy of these enzymes, a deficiency or experimental knockdown of C4ST-1 results in a dramatic decrease of cellular and whole-body levels of chondroitin 4'-sulfate. The enzyme completely loses activity when deglycosylated by treatment with PNGase F |
760408 |
| 2.8.2.5 | malfunction |
the ratio of 4-O-sulfation to 6-O-sulfation (4S/6S) and CS chain length, that occur during the aging process, are decreased in polyamine-depleted cells. In addition, decreased levels of chondroitin synthase 1 (CHSY1, EC 2.4.1.175) and chondroitin 4-O-sulfotransferase 2 proteins are also observed on polyamine depletion. The destabilization of G4 structures by polyamines (i.e. putrescine, spermidine and spermine) stimulates CHSY1 synthesis and, at least in part, contributes to the maturation of CS chains |
760531 |
| 2.8.2.5 | metabolism |
C4ST-1 is believed to play a distinct regulatory role not only in CS 4-O-sulfation but also in the amount of CS synthesis since none of the other family member C4ST-2 and C4ST-3 can compensate for the loss of C4ST-1 |
760408 |
| 2.8.2.5 | metabolism |
chondroitin sulfate (CS) biosynthesis is initiated once GalNAc is transferred by CSGalNAcT1 or 2 to the common linkage tetrasaccharide, GlcAbeta1-3galactose (Gal)beta1-3Galbeta1-4xylose (Xyl)beta1-O-serine in proteoglycans and chain elongation is then catalyzed by the chondroitin synthase (CHSY) 1-3/chondroitin-polymerizing factor (CHPF) heterodimer. After synthase-catalyzed polymerization, the majority of the GalNAc residues are 4-O-sulfated by chondroitin 4-O-sulfotransferases (C4ST1, 2 and 3) or 6-O-sulfated by chondroitin 6-O-sulfotransferases (C6ST1 and 2). In addition, resulting A- or C-unit can be further sulfated by GalNAc 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) or chondroitin uronyl 2-O-sulfotransferase (UST), generating di-sulfated disaccharides, E-unit or D-unit, respectively. Structural changes in CS, particularly the ratio of 4-O-sulfation to 6-O-sulfation (4S/6S), occur during normal embryonic development, during growth, and in aging. For example, the 4S/6S ratios of CS (or DS) present in human skin and cartilage decrease from birth to age 20 |
760531 |
| 2.8.2.5 | metabolism |
the enzyme plays a key role in regulating levels of chondroitin sulfate synthesized via chondroitin N-acetylgalactosaminyltransferase-1 |
721534 |
| 2.8.2.5 | metabolism |
the enzyme regulates the length and amount of chondroitin sulfate chains in co-operation with chondroitin N-acetylgalactosaminyltransferase 2 |
721529 |
