|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
Pt 1
|
|
pubmed:dateCreated |
2002-9-20
|
|
pubmed:abstractText |
Deficiency of the endoplasmic reticulum enzyme dolichyl-phosphate mannose (Dol-P-Man):Man(7)GlcNAc(2)-PP-dolichyl mannosyltransferase leads to a new type of congenital disorder of glycosylation, designated type Ig. The patient 1 presented with a multisystemic disorder with microcephaly, developmental retardation, convulsions and dysmorphic signs. The isoelectric focusing pattern of the patient's serum transferrin showed the partial loss of complete N-glycan side chains. In skin fibroblasts from the patient, the activity of Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol mannosyltransferase was severely reduced leading to the accumulation of Man(7)GlcNAc(2)-PP-Dol, which was transferred to newly synthesized glycoproteins. Sequencing of the Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol mannosyltransferase cDNA revealed a compound heterozygosity for two point mutations, leading to the exchange of leucine(158) for a proline residue and a premature translation stop with loss of the C-terminal 74 amino acids. The parents were heterozygous for one of the two mutations. Retroviral expression of the wild-type Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol mannosyltransferase cDNA in patient's fibroblasts normalized the mannosyltransferase activity.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10336995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10358084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10359825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10581255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10642597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10642602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10788335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-10832578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11003549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11269317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11326279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11326280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11733556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11733564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11805072,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-11901181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-6157537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-6163773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-6697396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-7944531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-8449944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-8549746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-8808595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-9140401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-9451026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-9525984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12093361-9789065
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0264-6021
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
367
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
195-201
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:12093361-Chromatography, High Pressure Liquid,
pubmed-meshheading:12093361-DNA, Complementary,
pubmed-meshheading:12093361-DNA Mutational Analysis,
pubmed-meshheading:12093361-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12093361-Endoplasmic Reticulum,
pubmed-meshheading:12093361-Female,
pubmed-meshheading:12093361-Fibroblasts,
pubmed-meshheading:12093361-Genetic Complementation Test,
pubmed-meshheading:12093361-Genetic Diseases, Inborn,
pubmed-meshheading:12093361-Glycosylation,
pubmed-meshheading:12093361-Humans,
pubmed-meshheading:12093361-Isoelectric Focusing,
pubmed-meshheading:12093361-Mannosyltransferases,
pubmed-meshheading:12093361-Mutagenesis, Site-Directed,
pubmed-meshheading:12093361-Oligosaccharides,
pubmed-meshheading:12093361-Phenotype,
pubmed-meshheading:12093361-Point Mutation,
pubmed-meshheading:12093361-Retroviridae,
pubmed-meshheading:12093361-Transferrin
|
|
pubmed:year |
2002
|
|
pubmed:articleTitle |
Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig.
|
|
pubmed:affiliation |
Georg-August-Universität zu Göttingen, Abteilung Biochemie II, Heinrich-Düker-Weg 12, D-37073 Göttingen, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
