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http://purl.uniprot.org/citations/19536613http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19536613http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19536613http://www.w3.org/2000/01/rdf-schema#comment"Arylsulfatase A (ARSA) and B (ARSB) have been regarded as lysosomal enzymes because of their hydrolytic activity on synthetic aromatic substrates and the lysosomal localization of their enzymatic activity. Using sea urchin embryos, we previously demonstrated that the bulk of ARS is located on the cell surface of the epithelium, colocalizing with sulfated polysaccharides, and that it does not exhibit enzymatic activity. To examine whether ARSA and ARSB exist on the cell surface in mammalian tissues, we raised antibodies against ARSA and ARSB and examined immunohistochemically their localization in the liver using light and electron microscopy. Here we show that mammalian ARSA and ARSB exist on the cell surface of sinusoidal endothelial cells, hepatocytes, and sinusoidal macrophages (Kupffer cells), as well as in the lysosome. They are also colocalized with heparan sulfate proteoglycan. These results suggest that ARSA and ARSB also may function in the cell surface of mammals. This is the first report to show cell-surface localization of ARS in mammalian somatic cells. The extracellular localization of ARS will provide new insight for human ARS deficiency disorders, such as metachromatic leukodystrophy and mucopolysaccharidosis VI."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.org/dc/terms/identifier"doi:10.1007/s00795-009-0447-x"xsd:string
http://purl.uniprot.org/citations/19536613http://purl.org/dc/terms/identifier"doi:10.1007/s00795-009-0447-x"xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Kawakami H."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Kawakami H."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Akimoto Y."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Akimoto Y."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Akasaka K."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Akasaka K."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Kusunoki S."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Kusunoki S."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Mitsunaga-Nakatsubo K."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/author"Mitsunaga-Nakatsubo K."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/name"Med. Mol. Morphol."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/name"Med. Mol. Morphol."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/pages"63-69"xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/pages"63-69"xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/title"Cell-surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes, and Kupffer cells in mammalian livers."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/title"Cell-surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes, and Kupffer cells in mammalian livers."xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/19536613http://purl.uniprot.org/core/volume"42"xsd:string