| pubmed-article:7733883 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0001055 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C1550605 | lld:lifeskim |
| pubmed-article:7733883 | lifeskim:mentions | umls-concept:C0456205 | lld:lifeskim |
| pubmed-article:7733883 | pubmed:dateCreated | 1995-5-26 | lld:pubmed |
| pubmed-article:7733883 | pubmed:abstractText | The sulphatase family of enzymes have regions of sequence similarity, but relatively little is known about either the structure-function relationships of sulphatases, or the role of highly conserved amino acids. The sequence of amino acids CTPSR at position 91-95 of 4-sulphatase has been shown to be highly conserved in all of the sequenced sulphatase enzymes. The cysteine at amino acid 91 of 4-sulphatase was selected for mutation analysis due to its potential role in either the active site, substrate-binding site or part of a key structural domain of 4-sulphatase and due to the absence of naturally occurring mutations in this residue in mucopolysaccharidosis type VI (MPS VI) patients. Two mutations, C91S and C91T, altering amino acid 91 of 4-sulphatase were generated and expressed in Chinese hamster ovary cells. Biochemical analysis of protein from a C91S cell line demonstrated no detectable 4-sulphatase enzyme activity but a relatively normal level of 4-sulphatase polypeptide (180% of the wild-type control protein level). Epitope detection, using a panel of ten monoclonal antibodies, demonstrated that the C91S polypeptide had a similar immunoreactivity to wild-type 4-sulphatase, suggesting that the C91S substitution does not induce a major structural change in the protein. Reduced catalytic activity associated with normal levels of 4-sulphatase protein have not been observed in any of the MPS VI patients tested and all show evidence of structural modification of 4-sulphatase protein with the same panel of antibodies [Brooks, McCourt, Gibson, Ashton, Shutter and Hopwood (1991) Am. J. Hum. Genet. 48, 710-719]. The loss of enzyme activity without a detectable protein conformation change suggests that Cys-91 may be a critical residue in the catalytic process. In contrast, analysis of protein from a C91T cell line revealed low levels of catalytically inactive 4-sulphatase polypeptide (0.37% of the wild-type control protein level) which had missing or masked epitopes, suggesting an altered protein structure or conformation. Subcellular fractionation studies of the C91T cell line demonstrated a high proportion of 4-sulphatase polypeptide content in organelles characteristic of microsomes. The aberrant intracellular localization and the reduced cellular content of 4-sulphatase polypeptide was consistent with the observed structural modification leading to retention and degradation of the protein within an early vacuolar compartment. | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7733883 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7733883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733883 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7733883 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7733883 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:HopwoodJ JJJ | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:RobertsonD... | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:PetersCC | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:MorrisC PCP | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:LitjensTT | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:BrooksD ADA | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:AnikaM SMS | lld:pubmed |
| pubmed-article:7733883 | pubmed:author | pubmed-author:BindlossCC | lld:pubmed |
| pubmed-article:7733883 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7733883 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7733883 | pubmed:volume | 307 ( Pt 2) | lld:pubmed |
| pubmed-article:7733883 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7733883 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7733883 | pubmed:pagination | 457-63 | lld:pubmed |
| pubmed-article:7733883 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:meshHeading | pubmed-meshheading:7733883-... | lld:pubmed |
| pubmed-article:7733883 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7733883 | pubmed:articleTitle | Two site-directed mutations abrogate enzyme activity but have different effects on the conformation and cellular content of the N-acetylgalactosamine 4-sulphatase protein. | lld:pubmed |
| pubmed-article:7733883 | pubmed:affiliation | Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia. | lld:pubmed |
| pubmed-article:7733883 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7733883 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7733883 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7733883 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7733883 | lld:pubmed |
