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Two dimensional gel electrophoresis of apolipoprotein C‐III and MALDI‐TOF MS are complementary techniques for the study of combined defects in N ‐ and mucin type O ‐glycan biosynthesis
Author(s) -
Bruneel Arnaud,
Morelle Willy,
Carre Yoann,
Habarou Florence,
Dupont Damien,
Hesbert Aurélie,
Durand Geneviève,
Michalski Jean Claude,
DrouinGarraud Valérie,
Seta Nathalie
Publication year - 2008
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200800089
Subject(s) - glycosylation , apolipoprotein b , cutis laxa , glycan , mucin , glycoprotein , gel electrophoresis , chemistry , biochemistry , microbiology and biotechnology , biology , genetics , cholesterol
In the field of diseases related to glycosylation disorders, congenital defects associated with abnormalities in both O ‐ and N ‐glycosylation of proteins constitute arising novel entities. Defects in subunits of the conserved oligomeric Golgi protein complex have been shown to be involved in an important part of previously unsolved CDG type II combining abnormalities in both mucin type core1 O ‐ and N ‐glycans; furthermore, recent studies revealed that autosomal recessive cutis laxa type II could also be associated with such combined glycosylation defects. Based on the studies of serum samples from three patients including a case of cutis laxa, we present here evidence that 2‐DE of apolipoprotein C‐III in combination with MALDI‐TOF‐MS analysis of serum O ‐ and N ‐glycans allow the detection and the biochemical characterization of these newly recognized glycosylation disorders.