Two Isoforms of Trimming Glucosidase II Exist in Mammalian Tissues and Cell Lines but Not in Yeast and Insect Cells

Ziak, Martin; Meier, Mirjam; Etter, Kay-Sara; Roth, Jürgen

doi:10.1006/bbrc.2000.4082

Cited by 17 publications

(13 citation statements)

References 21 publications

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“…␣-Glucosidase (Figs. 2 and 5, spot 67), a protein with a Ca 2ϩ -binding EF-hand domain, is involved in protein folding quality control of N-glycosylated proteins (26).…”

Section: Resultsmentioning

confidence: 99%

Analysis of Signal-dependent Changes in the Proteome of Drosophila Blood Cells During an Immune Response

Loseva

Engström

2004

Molecular & Cellular Proteomics

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Innate immunity is based on the recognition of cell-surface molecules of infecting agents. Microbial substances, such as peptidoglycan, lipopolysaccharide, and ␤-1,3-glucans, produce functional responses in Drosophila hemocytes that contribute to innate immunity. We have used two-dimensional gel electrophoresis and MS to resolve lipopolysaccharide-induced changes in the protein profile of a Drosophila hemocytic cell line. We identified 24 intracellular proteins that were up-or down-regulated, or modified, in response to immune challenge. Several proteins with predicted immune functions, including lysosomal proteases, actin-binding/remodeling proteins, as well as proteins involved in cellular responses to oxidative stress, were affected by the immune assault. Intriguingly, a number of the proteins identified in this study have recently been implicated in phagocytosis in higher vertebrates. We suggest that phagocytosis is activated in Drosophila hemocytes by the presence of microbial substances, and that this activation constitutes an evolutionarily conserved arm of innate immunity. In addition, a number of proteins involved in calcium-regulated signaling, mRNA processing, and nuclear transport were affected, consistent with a possible role in reprogramming of gene expression. In conclusion, the present proteome analysis identified many proteins previously not linked to innate immunity, demonstrating that differential protein profiling of Drosophila hemocytes is a valuable tool for identification of new players in immune-related cellular processes.

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“…␣-Glucosidase (Figs. 2 and 5, spot 67), a protein with a Ca 2ϩ -binding EF-hand domain, is involved in protein folding quality control of N-glycosylated proteins (26).…”

Section: Resultsmentioning

confidence: 99%

Analysis of Signal-dependent Changes in the Proteome of Drosophila Blood Cells During an Immune Response

Loseva

Engström

2004

Molecular & Cellular Proteomics

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“…In general, -glucosidases are classified into two families according to their substrate specificities. The first family consists of bacterial, yeast (Saccharomyces cerevisiae), and insect enzymes, named -glucosidase I, which hydrolyze heterogeneous substrates or glucosyl structures, such as p-nitrophenyl -glucoside 14,15 . Those from mold, plant, and mammalian tissues are called -glucosidase II, and recognize maltooligosaccharides or maltosyl structures 16 .…”

Section: Discussionmentioning

confidence: 99%

A series of cinnamic acid derivatives and their inhibitory activity on intestinal α-glucosidase

Adisakwattana¹,

Chantarasinlapin

Thammarat

et al. 2009

Journal of Enzyme Inhibition and Medicinal Chemistry

185

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“…The enzyme apparently forms a complex with a 80-kDa protein (so-called β subunit) that contains an ER retention sequence (D'Alessio et al 1999;Trombetta et al 1996). In mammalian cells, but not in yeast and insects, glucosidase II exists in two isoforms due to alternative splicing (Arendt et al 1999;Pelletier et al 2000;Ziak et al 2001). As schematically illustrated in Fig.…”

Section: Figmentioning

confidence: 99%

“…It is well known that the hydrolysis of the first α1,3-linked glucose residue occurs very rapidly whereas the second α1,3-linked glucose is removed more slowly (Hubbard and Robbins 1979;Jakob et al 1998a). It remains to be established if this is related to different affinities to the two substrates, the possible presence of two different substrate binding sites of glucosidase II (Alonso et al 1993), two enzyme isoforms (Arendt et al 1999;Pelletier et al 2000;Ziak et al 2001), or is a consequence of transient protein reglucosylation by UDP-Glc:glycoprotein glucosyltransferase (Trombetta and Parodi 1992).…”

Section: Figmentioning

confidence: 99%

“…Ultrathin cryosections, protein A-gold technique. Bars a 0.29 µm; b 0.12 µm tein which, like glucosidase II (Flura et al 1997;Ziak et al 2001) and glucosyltransferase (Parodi 2000a), seems to be ubiquitously expressed in mammalian tissues (Gonzalez et al 1999;Tremblay and Herscovics 1999). In yeast, evidence was obtained that the product of the ER α1,2-mannosidase I action, the Man 8 GlcNAc 2 B isomer ( Fig.…”

Section: Figmentioning

confidence: 99%

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The importance of trimming reactions on asparagine-linked oligosaccharides for protein quality control

Roth

Zuber

Guhl

et al. 2002

Histochem Cell Biol

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Although the biochemistry of early trimming reactions by glucosidases and ER mannosidases occurring on asparagine-linked oligosaccharides has been known for a long time, their involvement in quality control of protein folding has become apparent only more recently. Here we review the evidence for the involvement of specific oligosaccharide trimming intermediates such as Glc(1)Man(9)GlcNAc(2) and Man(8)GlcNAc(2) B isomer in this fundamental cellular process and the subcellular distribution of components of the protein quality control machinery which indicates the involvement of both the ER and pre-Golgi intermediates in this process. In addition, recent studies on the subcellular distribution of endomannosidase in conjunction with previously obtained biochemical data will be reviewed which demonstrate that an alternative deglucosylation pathway exists in pre-Golgi intermediates and the Golgi apparatus.

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Two Isoforms of Trimming Glucosidase II Exist in Mammalian Tissues and Cell Lines but Not in Yeast and Insect Cells

Cited by 17 publications

References 21 publications

Analysis of Signal-dependent Changes in the Proteome of Drosophila Blood Cells During an Immune Response

Analysis of Signal-dependent Changes in the Proteome of Drosophila Blood Cells During an Immune Response

A series of cinnamic acid derivatives and their inhibitory activity on intestinal α-glucosidase

The importance of trimming reactions on asparagine-linked oligosaccharides for protein quality control

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