{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:47:07Z","timestamp":1781110027793,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"19","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1990,10]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1073\/pnas.87.19.7443","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:27:44Z","timestamp":1149060464000},"page":"7443-7447","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":77,"title":["Incomplete synthesis of N-glycans in congenital dyserythropoietic anemia type II caused by a defect in the gene encoding alpha-mannosidase II."],"prefix":"10.1073","volume":"87","author":[{"given":"M N","family":"Fukuda","sequence":"first","affiliation":[{"name":"La Jolla Cancer Research Foundation, CA 92037."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K A","family":"Masri","sequence":"additional","affiliation":[{"name":"La Jolla Cancer Research Foundation, CA 92037."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Dell","sequence":"additional","affiliation":[{"name":"La Jolla Cancer Research Foundation, CA 92037."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L","family":"Luzzatto","sequence":"additional","affiliation":[{"name":"La Jolla Cancer Research Foundation, CA 92037."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K W","family":"Moremen","sequence":"additional","affiliation":[{"name":"La Jolla Cancer Research Foundation, CA 92037."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1990,10]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.87.19.7443","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T13:23:20Z","timestamp":1649856200000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.87.19.7443"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,10]]},"references-count":0,"journal-issue":{"issue":"19","published-print":{"date-parts":[[1990,10]]}},"alternative-id":["10.1073\/pnas.87.19.7443"],"URL":"https:\/\/doi.org\/10.1073\/pnas.87.19.7443","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,10]]},"assertion":[{"value":"1990-10-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}