Unusual N-Glycan Structures in α-Mannosidase II/IIx Double Null Embryos Identified by a Systematic Glycomics Approach Based on Two-dimensional LC Mapping and Matrix-dependent Selective Fragmentation Method in MALDI-TOF/TOF Mass Spectrometry

Hato, Masakatsu; Nakagawa, Hiroaki; Kurogochi, Masaki; Akama, Tomoya O.; Marth, Jamey D.; Nishimura, Shin‐Ichiro

doi:10.1074/mcp.m600213-mcp200

Cited by 28 publications

(20 citation statements)

References 26 publications

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“…In fact, glycoproteins derived from mice embryos defect in α-mannosidase II activity show a tissue glycosylation pattern with increased hybrid glycans and decreased complex glycans [34] due to the partial compensation by α-mannosidase IIx. However, the oligosaccharide structural data with a defect starting with early Golgi processing but including processing steps located in the middle-and transGolgi associated with erythroblast differentiation and maturation containing a disturbance in the loss of organelles involved in N-glycosylation implicate a defect of the glycosylation apparatus in CDA II erythroblasts.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Denecke

Kranz

Nimtz³

et al. 2007

Glycoconj J

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Section: Discussionmentioning

confidence: 99%

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Denecke

Kranz

Nimtz³

et al. 2007

Glycoconj J

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“…However, ablation of both genes completely abrogates complex N-glycan formation with the accumulation of hybrid structures (25,38). The substantial loss of typical N-glycans primarily results in postnatal death within 2 days, and less frequently in embryonic lethality, with only a few mice surviving postnatally (ϾP21).…”

Section: Discussionmentioning

confidence: 99%

Respiratory Distress and Neonatal Lethality in Mice Lacking Golgi α1,2-Mannosidase IB Involved in N-Glycan Maturation

Tremblay

Kovács

Daniels

et al. 2007

Journal of Biological Chemistry

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There are three mammalian Golgi ␣1,2-mannosidases, encoded by different genes, that form Man 5 GlcNAc 2 from Man 8-9 GlcNAc 2 for the biosynthesis of hybrid and complex N-glycans. Northern blot analysis and in situ hybridization indicate that the three paralogs display distinct developmental and tissue-specific expression. The physiological role of Golgi ␣1,2-mannosidase IB was investigated by targeted gene ablation. The null mice have normal gross appearance at birth, but they display respiratory distress and die within a few hours. Histology of fetal lungs the day before birth indicate some delay in development, whereas neonatal lungs show extensive pulmonary hemorrhage in the alveolar region. No significant histopathological changes occur in other tissues. No remarkable ultrastructural differences are detected between wild type and null lungs. The membranes of a subset of bronchiolar epithelial cells are stained with lectins from Phaseolus vulgaris (leukoagglutinin and erythroagglutinin) and Datura stramonium in wild type lungs, but this staining disappears in lungs from null mice. Mass spectrometry of N-glycans from different tissues shows no significant changes in global N-glycans of null mice. Therefore, only a few glycoproteins required for normal lung function depend on ␣1,2-mannosidase IB for maturation. There are no apparent differences in the expression of several lung epithelial cell and endothelial cell markers between null and wild type mice. The ␣1,2-mannosidase IB null phenotype differs from phenotypes caused by ablation of other enzymes in N-glycan biosynthesis and from other mouse gene disruptions that affect pulmonary development and function.

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“…MALDI-TOF data were obtained using an Ultraflex time-of-flight mass spectrometer (Bruker Daltonics, Bremen, Germany) equipped with a LIFT-TOF/TOF facility controlled by FlexControl 2.0 software according to the general procedure reported previously (20,21). All spectra were obtained using a reflectron mode with an acceleration voltage of 25 kV, a reflector voltage of 26.3 kV, and a pulsed ion extraction of 160 ns in the positive ion mode.…”

Section: Maldi-tof Mass Spectrometrymentioning

confidence: 99%

Quantitative Glycomics of Human Whole Serum Glycoproteins Based on the Standardized Protocol for Liberating N-Glycans

Kita

Miura

Furukawa

et al. 2007

Molecular & Cellular Proteomics

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107

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Global glycomics of human whole serum glycoproteins appears to be an innovative and comprehensive approach to identify surrogate non-invasive biomarkers for various diseases. Despite the fact that quantitative glycomics is premised on highly efficient and reproducible oligosaccharide liberation from human serum glycoproteins, it should be noted that there is no validated protocol for which deglycosylation efficiency is proven to be quantitative. To establish a standard procedure to evaluate N-glycan release from whole human serum glycoproteins by peptide-N-glycosidase F (PNGase F) treatment, we determined the efficiencies of major N-glycan liberation from serum glycoproteins in the presence of reducing agents, surfactants, protease treatment, or combinations of pretreatments prior to PNGase F digestion. We show that de-N-glycosylation efficiency differed significantly depending on the condition used, indicative of the importance of a standardized protocol for the accumulation and comparison of glycomics data. Maximal de-N-glycosylation was achieved when serum was subjected to reductive alkylation in the presence of 2-hydroxyl-3-sulfopropyl dodecanoate, a surfactant used for solubilizing proteins, or related analogues, followed by tryptic digestion prior to PNGase F treatment. An optimized de-N-glycosylation protocol permitted relative and absolute quantitation of up to 34 major N-glycans present in serum glycoproteins of normal subjects for the first time. Moreover PNGase F-catalyzed de-

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Unusual N-Glycan Structures in α-Mannosidase II/IIx Double Null Embryos Identified by a Systematic Glycomics Approach Based on Two-dimensional LC Mapping and Matrix-dependent Selective Fragmentation Method in MALDI-TOF/TOF Mass Spectrometry

Cited by 28 publications

References 26 publications

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Respiratory Distress and Neonatal Lethality in Mice Lacking Golgi α1,2-Mannosidase IB Involved in N-Glycan Maturation

Quantitative Glycomics of Human Whole Serum Glycoproteins Based on the Standardized Protocol for Liberating N-Glycans

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