| pubmed-article:2217175 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C1306589 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C1457869 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C2260943 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C0205257 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
| pubmed-article:2217175 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:2217175 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:2217175 | pubmed:dateCreated | 1990-11-9 | lld:pubmed |
| pubmed-article:2217175 | pubmed:abstractText | Congenital dyserythropoietic anemia type II, or hereditary erythroblastic multinuclearity with a positive acidified-serum-lysis test (HEMPAS), is a genetic anemia in humans inherited by an autosomally recessive mode. The enzyme defect in most HEMPAS patients has previously been proposed as a lowered activity of N-acetylglucosaminyltransferase II, resulting in a lack of polylactosamine on proteins and leading to the accumulation of polylactosaminyl lipids. A recent HEMPAS case, G.C., has now been analyzed by cell-surface labeling, fast-atom-bombardment mass spectrometry of glycopeptides, and activity assay of glycosylation enzymes. Significantly decreased glycosylation of polylactosaminoglycan proteins and incompletely processed asparagine-linked oligosaccharides were detected in the erythrocyte membranes of G.C. In contrast to the earlier studied HEMPAS cases, G.C. cells are normal in N-acetylglucosaminyltransferase II activity but are low in alpha-mannosidase II (alpha-ManII) activity. Northern (RNA) analysis of poly(A)+ mRNA from normal, G.C., and other unrelated HEMPAS cells all showed double bands at the 7.6-kilobase position, detected by an alpha-ManII cDNA probe, but expression of these bands in G.C. cells was substantially reduced (less than 10% of normal). In Southern analysis of G.C. and normal genomic DNA, the restriction fragment patterns detected by the alpha-ManII cDNA probe were indistinguishable. These results suggest that G.C. cells contain a mutation in alpha-ManII-encoding gene that results in inefficient expression of alpha-ManII mRNA, either through reduced transcription or message instability. This report demonstrates that HEMPAS is caused by a defective gene encoding an enzyme necessary for the synthesis of asparagine-linked oligosaccharides. | lld:pubmed |
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| pubmed-article:2217175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2217175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2217175 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2217175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2217175 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2217175 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2217175 | pubmed:author | pubmed-author:LuzzattoLL | lld:pubmed |
| pubmed-article:2217175 | pubmed:author | pubmed-author:FukudaM NMN | lld:pubmed |
| pubmed-article:2217175 | pubmed:author | pubmed-author:DellAA | lld:pubmed |
| pubmed-article:2217175 | pubmed:author | pubmed-author:MasriK AKA | lld:pubmed |
| pubmed-article:2217175 | pubmed:author | pubmed-author:MoremenK WKW | lld:pubmed |
| pubmed-article:2217175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2217175 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2217175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2217175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2217175 | pubmed:pagination | 7443-7 | lld:pubmed |
| pubmed-article:2217175 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2217175 | pubmed:meshHeading | pubmed-meshheading:2217175-... | lld:pubmed |
| pubmed-article:2217175 | pubmed:meshHeading | pubmed-meshheading:2217175-... | lld:pubmed |
| pubmed-article:2217175 | pubmed:meshHeading | pubmed-meshheading:2217175-... | lld:pubmed |
| pubmed-article:2217175 | pubmed:meshHeading | pubmed-meshheading:2217175-... | lld:pubmed |
| pubmed-article:2217175 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2217175 | pubmed:articleTitle | Incomplete synthesis of N-glycans in congenital dyserythropoietic anemia type II caused by a defect in the gene encoding alpha-mannosidase II. | lld:pubmed |
| pubmed-article:2217175 | pubmed:affiliation | La Jolla Cancer Research Foundation, CA 92037. | lld:pubmed |
| pubmed-article:2217175 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2217175 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
