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CHST14  -  carbohydrate (N-acetylgalactosamine 4-0)...

Homo sapiens

Synonyms: ATCS, Carbohydrate sulfotransferase 14, D4ST-1, D4ST1, Dermatan 4-sulfotransferase 1, ...
 
 
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High impact information on CHST14

  • 4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified [1].
  • Enzymatic analysis of the transferase reaction products showed that D4ST-1 far more efficiently transferred sulfate to GalNAc residues in -IdoUA-Gal-NAc-IdoUA-than in -GlcUA-GalNAc-GlcUA-sequences [1].
  • This hypothesis has recently been argued based on enzymological studies using microsomes that C5-epimerization precedes 4-O-sulfation, which was further supported by the specificity of the cloned D4ST-1 with predominant preference for IdoUA-GalNAc flanked by GlcUA-GalNAc over IdoUA-GalNAc flanked by IdoUA-GalNAc in exhaustively desulfated dermatan [1].
  • The properties of D4ST-1 indicate that sulfation of the GalNAc moieties in dermatan is mediated by a distinct GalNAc-4-O-sulfotransferase and occurs following epimerization of GlcUA to IdoUA [2].
  • The open reading frame of D4ST-1 is encoded by a single exon located on human chromosome 15q14 [2].
 

Anatomical context of CHST14

  • D4ST-1 message is expressed in virtually all tissues at some level but is most highly expressed in pituitary, placenta, uterus, and thyroid [2].
 

Associations of CHST14 with chemical compounds

  • D4ST-1 shows a strong preference in vitro for sulfate transfer to IdoUAalpha1,3GalNAcbeta1,4 that is flanked by GlcUAbeta1,3GalNAcbeta1,4 as compared with IdoUAalpha1,3GalNAcbeta1,4 flanked by IdoUAalpha1,3GalNAcbeta1,4 [2].
  • D4ST-1 transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl [2].
  • With the exception of HNK-1-ST, these sulphotransferases add sulphate to the C-4 hydroxy group of either terminal or non-terminal beta1,4-linked GalNAc [3].
 

Other interactions of CHST14

  • No change in activity in dermatan 4-O sulfotransferase was observed, and only a minor decrease in dermatan 4-O-sulfotransferase-1 (D4ST-1) mRNA was observed [4].

References

  1. Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor: implication of differential roles in dermatan sulfate biosynthesis. Mikami, T., Mizumoto, S., Kago, N., Kitagawa, H., Sugahara, K. J. Biol. Chem. (2003) [Pubmed]
  2. Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase. Evers, M.R., Xia, G., Kang, H.G., Schachner, M., Baenziger, J.U. J. Biol. Chem. (2001) [Pubmed]
  3. Glycoprotein hormone GalNAc-4-sulphotransferase. Baenziger, J.U. Biochem. Soc. Trans. (2003) [Pubmed]
  4. Regulation of the chondroitin/dermatan fine structure by transforming growth factor-beta1 through effects on polymer-modifying enzymes. Tiedemann, K., Olander, B., Eklund, E., Todorova, L., Bengtsson, M., Maccarana, M., Westergren-Thorsson, G., Malmström, A. Glycobiology (2005) [Pubmed]
 
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