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http://purl.uniprot.org/citations/17405882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17405882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17405882http://www.w3.org/2000/01/rdf-schema#comment"Heparan sulfate (HS) plays critical roles in a variety of developmental, physiological, and pathogenic processes due to its ability to interact in a structure-dependent manner with numerous growth factors that participate in cellular signaling. The divergent structures of HS glycosaminoglycans are the result of the coordinate actions of several N- and O-sulfotransferases, C5-epimerase, and 6-O-endosulfatases. We have shown that 6-O-sulfation of the glucosamine residues in HS are catalyzed by the sulfotransferases HS6ST-1, -2, and -3. To determine the biological and physiological importance of HS6ST-1, we now describe the creation of transgenic mice that lack this sulfotransferase. Most of our HS6ST-1-null mice died between embryonic day 15.5 and the perinatal stage, and those mice that survived were considerably smaller than their wild-type littermates. Some of these HS6ST-1-null mice exhibited development abnormalities, and histochemical and molecular analyses of these mice revealed an approximately 50% reduction in the number of fetal microvessels in the labyrinthine zone of the placenta relative to that in the wild-type mice. Because we observed a modest reduction in VEGF-A mRNA and protein in the tissues of HS6ST-1-null mice, an HS-dependent defect in cytokine signaling probably contributes to increased embryonic lethality and decreased growth. Biochemical studies of the HS chains isolated from various organs of our HS6ST-1-null mice revealed a marked reduction of GlcNAc(6SO(4)) and HexA-GlcNSO(3)(6SO(4)) levels and a reduced ability to bind Wnt2. Thus, despite the presence of three closely related 6-O-sulfotransferase genes in the mouse genome, HS6ST-1 is the primary one used in HS biosynthesis in most tissues."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m607434200"xsd:string
http://purl.uniprot.org/citations/17405882http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m607434200"xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Kimata K."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Kimata K."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Stevens R.L."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Stevens R.L."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Habuchi H."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Habuchi H."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Nagai N."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Nagai N."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Sugaya N."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Sugaya N."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Atsumi F."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/author"Atsumi F."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/pages"15578-15588"xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/pages"15578-15588"xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/title"Mice deficient in heparan sulfate 6-O-sulfotransferase-1 exhibit defective heparan sulfate biosynthesis, abnormal placentation, and late embryonic lethality."xsd:string
http://purl.uniprot.org/citations/17405882http://purl.uniprot.org/core/title"Mice deficient in heparan sulfate 6-O-sulfotransferase-1 exhibit defective heparan sulfate biosynthesis, abnormal placentation, and late embryonic lethality."xsd:string
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