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Gene Review

LOC395933  -  sulfotransferase

Gallus gallus

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High impact information on LOC395933

  • These results suggest that HS with different sulfation patterns created with multiple sulfotransferase activities provides an appropriate extracellular environment for morphogenetic signal transduction [1].
  • In addition, the total amounts of both chondroitin sulfate chains and the sulfotransferase activities were highest during early embryonic stages and decreased sharply as the development reached completion [2].
  • Photoaffinity labeling of the purified enzyme with 2-azidoadenosine 3',5'-di[5'-32P]phosphate occurred only with the 75-kDa protein, confirming that this is the chondroitin 6-sulfotransferase/keratan sulfotransferase [3].
  • Chondroitin sulfate E from squid cartilage, dermatan, sulfate, and heparan sulfate hardly served as acceptors of the sulfotransferase [4].
  • Sulfotransferase activity was also found in a dual distribution similar to that of the chondroitin polymerization and GalNAc transferase, with a small reduction in activity in the trans-Golgi fractions of brefeldin A-treated cartilage [5].

Biological context of LOC395933

  • This sulfotransferase was activated by protamine, presenting Michaelis-Menten kinetics when transferring [35S]sulfate from [35S]3'-phosphoadenosine 5'-phosphosulfate to the totally desulfated chondroitin, whereas sigmoidal kinetics was observed when partially sulfated chondroitin 6-sulfate was employed as substrate [6].
  • We have used mRNA differential display to compare gene expression in normal and GH receptor-deficient dwarf chickens, and report here the characterization of one differentially expressed gene, which shows significant sequence identity to the sulfotransferase gene family [7].

Anatomical context of LOC395933


Associations of LOC395933 with chemical compounds


  1. Distinctive expression patterns of heparan sulfate O-sulfotransferases and regional differences in heparan sulfate structure in chick limb buds. Nogami, K., Suzuki, H., Habuchi, H., Ishiguro, N., Iwata, H., Kimata, K. J. Biol. Chem. (2004) [Pubmed]
  2. Developmental regulation of the sulfation profile of chondroitin sulfate chains in the chicken embryo brain. Kitagawa, H., Tsutsumi, K., Tone, Y., Sugahara, K. J. Biol. Chem. (1997) [Pubmed]
  3. Purification, photoaffinity labeling, and characterization of a single enzyme for 6-sulfation of both chondroitin sulfate and keratan sulfate. Sugumaran, G., Katsman, M., Drake, R.R. J. Biol. Chem. (1995) [Pubmed]
  4. Purification of chondroitin 6-sulfotransferase secreted from cultured chick embryo chondrocytes. Habuchi, O., Matsui, Y., Kotoya, Y., Aoyama, Y., Yasuda, Y., Noda, M. J. Biol. Chem. (1993) [Pubmed]
  5. Effects of brefeldin A on the localization of chondroitin sulfate-synthesizing enzymes. Activities in subfractions of the Golgi from chick embryo epiphyseal cartilage. Sugumaran, G., Katsman, M., Silbert, J.E. J. Biol. Chem. (1992) [Pubmed]
  6. Protamine modulation of sulfotransferase activity from chicken embryo epiphyseal cartilages changes with the degree of sulfation of the acceptor. Salac, M.L., Menezes, J.R., Mourão, P.A. Arch. Biochem. Biophys. (1984) [Pubmed]
  7. Cloning and expression of a novel chicken sulfotransferase cDNA regulated by GH. Cao, H., Agarwal, S.K., Burnside, J. J. Endocrinol. (1999) [Pubmed]
  8. Purification and characterization of N-acetylglucosaminyl sulfotransferase from chick corneas. Yamamoto, Y., Takahashi, I., Ogata, N., Nakazawa, K. Arch. Biochem. Biophys. (2001) [Pubmed]
  9. Glycosyltransferase and sulfotransferase activities in chick corneal stromal cells before and after in vitro culture. Nakazawa, K., Takahashi, I., Yamamoto, Y. Arch. Biochem. Biophys. (1998) [Pubmed]
  10. Stimulation of glycosaminoglycan sulfotransferase from chick embryo cartilage by basic proteins and polyamines. Habuchi, O., Miyata, K. Biochim. Biophys. Acta (1980) [Pubmed]
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