| pubmed-article:1317874 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1317874 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:1317874 | lifeskim:mentions | umls-concept:C0077716 | lld:lifeskim |
| pubmed-article:1317874 | lifeskim:mentions | umls-concept:C0320458 | lld:lifeskim |
| pubmed-article:1317874 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1317874 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:1317874 | pubmed:dateCreated | 1992-7-6 | lld:pubmed |
| pubmed-article:1317874 | pubmed:abstractText | The kinetic properties of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) partially purified from the soil amoeba Acanthamoeba castellanii have been studied. The transferase phosphorylated the lysosomal enzymes uteroferrin and cathepsin D 3-90-fold better than nonlysosomal glycoproteins and 16-83-fold better than a Man9GlcNAc oligosaccharide. Deglycosylated uteroferrin was a potent competitive inhibitor of the phosphorylation of intact uteroferrin (Ki of 48 microM) but did not inhibit the phosphorylation of RNase B or the simple sugar alpha-methylmannoside. Deglycosylated RNase (RNase A) did not inhibit the phosphorylation of RNase B or uteroferrin. These results indicate that purified amoeba GlcNAc-phosphotransferase recognizes a protein domain present on lysosomal enzymes but absent in most nonlysosomal glycoproteins. The transferase also exhibited a marked preference for oligosaccharides containing mannose alpha 1,2-mannose sequences, but this cannot account for the high affinity binding to lysosomal enzymes. A. castellanii extracts do not contain detectable levels of N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, the second enzyme in the biosynthetic pathway for the mannose 6-phosphate recognition marker. We conclude that A. castellanii does not utilize the phosphomannosyl sorting pathway despite expression of very high levels of GlcNAc-phosphotransferase. | lld:pubmed |
| pubmed-article:1317874 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1317874 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317874 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1317874 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1317874 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1317874 | pubmed:author | pubmed-author:KornfeldSS | lld:pubmed |
| pubmed-article:1317874 | pubmed:author | pubmed-author:KetchamC MCM | lld:pubmed |
| pubmed-article:1317874 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1317874 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1317874 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1317874 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1317874 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1317874 | pubmed:pagination | 11654-9 | lld:pubmed |
| pubmed-article:1317874 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
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| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:meshHeading | pubmed-meshheading:1317874-... | lld:pubmed |
| pubmed-article:1317874 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1317874 | pubmed:articleTitle | Characterization of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase from Acanthamoeba castellanii. | lld:pubmed |
| pubmed-article:1317874 | pubmed:affiliation | Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110. | lld:pubmed |
| pubmed-article:1317874 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1317874 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1317874 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1317874 | lld:pubmed |
