Molecular Cloning and Expression of anN-Acetylgalactosamine-4-O-sulfotransferase That Transfers Sulfate to Terminal and Non-terminal β1,4-LinkedN-Acetylgalactosamine
نویسندگان
چکیده
منابع مشابه
Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non-terminal beta 1,4-linked N-acetylgalactosamine.
We have identified and characterized an N-acetylgalactosamine-4-O-sulfotransferase designated GalNAc-4-ST2 (GenBank(TM) accession number ) based on its homology to HNK-1 sulfotransferase (HNK-1 ST). The cDNA predicts an open reading frame encoding a type II membrane protein of 443 amino acids with a 12-amino acid cytoplasmic domain, a 23-amino acid transmembrane domain, and a 408-amino acid lum...
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N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) is an enzyme which is known to help build up the GlcAbeta1-3GalNAc(4,6-bisSO4) unit of chondroitin sulfate E (CS-E). This enzymatic activity has been reported in squid cartilage and in human serum, but has never been reported as an enzyme required during early mouse development. On the other hand, CS-E has been shown to bind wi...
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Doug A. BROOKS,*: Daniel A. ROBERTSON,* Colleen BINDLOSS,* Tom LITJENS,* Don S. ANSON,* Christoph PETERS,t C. Phillip MORRIS* and John J. HOPWOOD* *Lysosomal Diseases Research Unit, Department of Chemical Pathology, Centre for Medical Genetics, The Women's and Children's Hospital, 72 King William Road, North Adelaide, South Australia, 5006, Australia and tBiochemie 11, Universitgt Gottingen, Go...
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N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) is a sulfotransferase responsible for biosynthesis of chondroitin sulfate E (CS-E). CS-E plays important roles in numerous biological events, such as neurite outgrowth. However, the role of GalNAc4S-6ST in tumor progression remains unknown. In the present study, we analyzed expression of GalNAc4S-6ST mRNA in colorectal cancer b...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m011560200