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

• Protamine modulation of sulfotransferase activity from chicken embryo epiphyseal cartilages changes with the degree of sulfation of the acceptor [6].
• Purification and characterization of N-acetylglucosaminyl sulfotransferase from chick corneas [8].
• The expression of this sulfotransferase mRNA was also detected in skeletal muscle, but not other tissues [7].
• Glycosyltransferase and sulfotransferase activities in chick corneal stromal cells before and after in vitro culture [9].
• Stimulation of glycosaminoglycan sulfotransferase from chick embryo cartilage by basic proteins and polyamines [10].

Associations of LOC395933 with chemical compounds

• However, we speculate that GH activation of sulfotransferase activity could play a role in reducing concentrations of growth-antagonistic steroid hormones in GH target tissues [7].
• Sulfotransferase activity, using estradiol or corticosterone as substrate, is detected in cells transfected with an expression vector containing the full-length cDNA [7].
• Of these enzymes, the sulfotransferase activity toward degalactosylated, pyridylaminated lacto-N-neotetraose and N-acetyllactosamine dimer (probably GlcNAc-6-sulfotransferase) decreased markedly after in vitro culture, whereas the galactosyltransferase activity increased [9].
• N-Acetylglucosaminyl(GlcNAc) sulfotransferase, which transfers sulfate from adenosine 3'-phosphate 5'-phosphosulfate to GlcNAc at the nonreducing end of oligosaccharides, was purified 887-fold with a 8.4% yield from 2-day-old chick corneas by chromatography on CM-Sepharose, WGA-agarose, GlcNAc-agarose, and 3',5'-ADP-agarose columns [8].
• The Km value for 3'-phosphoadenosine 5'-phosphosulfate of the sulfotransferase, when chondroitin was used as acceptor, was 1 . 10(-6) M in the presence of 25 microgram/ml protamine, compared to 2 . 10(-5) M in the absence of protamine [10].

References