Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q7LGC8 (HSD)
 3,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Based on sequence homology with a previously cloned human GlcNAc 6-O-sulfotransferase, we have identified an open reading frame (ORF) encoding a novel member of the Gal/GalNAc/GlcNAc 6-O-sulfotransferase (GST) family termed GST-5 on the human X chromosome (band Xp11). GST-5 has recently been characterized as a novel GalNAc 6-O-sulfotransferase termed chondroitin 6-sulfotransferase-2 (Kitagawa, H., Fujita, M., Itio, N., and Sugahara K. (2000) J. Biol. Chem. 275, 21075-21080). We have coexpressed a human GST-5 cDNA with a GlyCAM-1/IgG fusion protein in COS-7 cells and observed four-fold enhanced [(35)S]sulfate incorporation into this mucin acceptor. All mucin-associated [(35)S]sulfate was incorporated as GlcNAc-6-sulfate or Galbeta1-->4GlcNAc-6-sulfate. GST-5 was also expressed in soluble epitope-tagged form and found to catalyze 6-O-sulfation of GlcNAc residues in synthetic acceptor structures. In particular, GST-5 was found to catalyze 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc. In the mouse genome we have found a homologous ORF that predicts a novel murine GlcNAc 6-O-sulfotransferase with 88% identity to the human enzyme. This gene was mapped to mouse chromosome X at band XA3.1-3.2. GST-5 is the newest member of an emerging family of carbohydrate 6-O-sulfotransferases that includes chondroitin 6-sulfotransferase (GST-0), keratan-sulfate galactose 6-O-sulfotransferase (GST-1), the ubiquitously expressed GlcNAc 6-O-sulfotransferase (GST-2), high endothelial cell GlcNAc 6-O-sulfotransferase (GST-3), and intestinal GlcNAc 6-O-sulfotransferase (GST-4).
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PMID:Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5). 1095 61

Many common chronic inflammatory rhinosinusitis conditions (hypertrophic sinus disease [HSD]) have the histopathological profile of allergic or asthmatic inflammation. Allergic fungal sinusitis (AFS) is both a type of noninvasive fungal rhinosinusitis and a type of HSD. AFS has clinicopathological features that make it similar, but not identical, to allergic bronchopulmonary aspergillosis (ABPA). Allergic mucin is a defined pathological entity occurring in ABPA, AFS, and in the HSD "eosinophilic mucin rhinosinusitis (EMRS)." Diagnosis of AFS requires a careful review of surgical reports, histopathology, and culture results. Treatment includes surgery and aggressive postoperative medical management of allergic inflammatory disease. Prognosis is good with integrated medical-surgical follow-up, but recurrence remains problematic. The association of ABPA, AFS, and HSD with class II genes of the major histocompatibility complex places the initiation of these inflammatory diseases within the context of antigen presentation and the acquired immune response. Pathological immunomanipulation of this response by local microbial superantigens may be a common mechanism for disease pathogenesis. Future research into the molecular biology of these related conditions may offer insight into the pathogenesis of other chronic inflammatory diseases.
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PMID:Allergic fungal sinusitis. 1678 91

A novel mucin (qniumucin), which we recently discovered in jellyfish, was investigated by several NMR techniques. Almost all the peaks in the (13)C and proton NMR spectra were satisfactorily assigned to the amino acids in the main chain and to the bridging GalNAc, the major sugar in the saccharide branches. The amino acid sequence in the tandem repeat part (-VVETTAAP-) was reconfirmed by the cross-peaks between alpha protons and carbonyl carbons in the HMBC spectrum. A connectivity analysis around the O-glycoside bond (GalNAc-Thr) was also performed, and detailed information on the local configuration was obtained by the DPFGSE-NOE-HSD technique. The strategy and the results described in this paper can be extended to the structural analysis of general O-glycan chains, which are more complex than the present mucin. NMR analyses reveal the simple structure of qniumucin extracted by the present protocol, and the homogeneity and purity of qniumucin are probably the result of it being extracted from jellyfish, a primitive animal.
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PMID:NMR study on a novel mucin from jellyfish in natural abundance, Qniumucin from Aurelia aurita. 1937 Oct 80