| pubmed-article:3081505 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C0205054 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C0029297 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:3081505 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:3081505 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:3081505 | pubmed:dateCreated | 1986-4-4 | lld:pubmed |
| pubmed-article:3081505 | pubmed:abstractText | The effects of alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene (alpha-ManMNT) on the degradation and biosynthesis of oligosaccharide chains on alpha 1-acid glycoprotein (AGP) were studied. Addition of the triazene to a perfused liver prevented the complete degradation of endocytosed N-acetyl[14C]glucosamine-labeled asialo-AGP and caused the accumulation of Man2GlcNAc1 fragments in the lysosome-enriched fraction of the liver homogenate. This compound also reduced the reincorporation of lysosomally derived [14C]GlcNAc into newly secreted glycoproteins. Cultured hepatocytes treated with the inhibitor synthesized and secreted fully glycosylated AGP. However, the N-linked oligosaccharide chains on AGP secreted by the alpha-ManMNT-treated hepatocytes remained sensitive to digestion with endoglycosidase H, were resistant to neuraminidase, and consisted of Man9-7GlcNAc2 structures as analyzed by high resolution Bio-Gel P-4 chromatography. As measured by their resistance to cleavage by endoglycosidase H, the normal processing of all six carbohydrate chains on AGP to the complex form did not completely resume until nearly 24 h after triazene treatment. Since alpha-ManMNT is likely to irreversibly inactivate alpha-D-mannosidases, the return of normal AGP secretory forms after 24 h probably resulted from synthesis of new processing enzymes. | lld:pubmed |
| pubmed-article:3081505 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3081505 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3081505 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3081505 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:3081505 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3081505 | pubmed:author | pubmed-author:AronsonN... | lld:pubmed |
| pubmed-article:3081505 | pubmed:author | pubmed-author:MyersR WRW | lld:pubmed |
| pubmed-article:3081505 | pubmed:author | pubmed-author:BeMillerJ NJN | lld:pubmed |
| pubmed-article:3081505 | pubmed:author | pubmed-author:KurandaM JMJ | lld:pubmed |
| pubmed-article:3081505 | pubmed:author | pubmed-author:DochertyP APA | lld:pubmed |
| pubmed-article:3081505 | pubmed:author | pubmed-author:BohnJ AJA | lld:pubmed |
| pubmed-article:3081505 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3081505 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3081505 | pubmed:volume | 261 | lld:pubmed |
| pubmed-article:3081505 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3081505 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3081505 | pubmed:pagination | 3457-63 | lld:pubmed |
| pubmed-article:3081505 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:meshHeading | pubmed-meshheading:3081505-... | lld:pubmed |
| pubmed-article:3081505 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3081505 | pubmed:articleTitle | Effect of alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene on hepatic degradation and processing of the N-linked oligosaccharide chains of alpha 1-acid glycoprotein. | lld:pubmed |
| pubmed-article:3081505 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3081505 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3081505 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3081505 | lld:pubmed |
