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Mannosidase, alpha, class 2A, member 1

alpha-mannosidase II, Golgi alpha-mannosidase II, man II
This gene encodes a protein which is a member of family 38 of the glycosyl hydrolases. The protein is located in the Golgi and catalyzes the final hydrolytic step in the asparagine-linked oligosaccharide (N-glycan) maturation pathway. Mutations in the mouse homolog of this gene have been shown to cause a systemic autoimmune disease similar to human systemic lupus erythematosus. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CD45, CAN, HAD, fibrillin-1
Papers on alpha-mannosidase II
Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs.
Arai et al., Tokyo, Japan. In Mol Biol Cell, 2013
Depletion of OSBP by small interfering RNA causes mislocalization of intra-Golgi v-SNAREs GS28 and GS15 throughout the cytoplasm without affecting the perinuclear localization of Golgi target-SNARE syntaxin5 and reduces the abundance of a Golgi enzyme, mannosidase II (Man II).
The effects of neuromuscular electrical stimulation on cardiopulmonary function in healthy adults.
Han et al., Cheju, South Korea. In Ann Rehabil Med, 2012
The electrical stimulation group received NMES on both sides of quadriceps muscle using a Walking Man II® in a sitting position for 30 minutes over 2 weeks.
Validation of the new intubation detector device: a manikin study.
Tim et al., India. In J Clin Monit Comput, 2012
The Sim Man II, (Laerdal Medical AS, Norway) manikin was used.
The gene, expression pattern and subcellular localization of chitin synthase B from the insect Ostrinia furnacalis.
Yang et al., Dalian, China. In Biochem Biophys Res Commun, 2011
Puncta structures of the recombinant OfCHSB were observed co-localized with Golgi marker Man II-GFP, suggesting a possible localization of chitin synthases under physiological conditions.
Molecular mechanism of the glycosylation step catalyzed by Golgi alpha-mannosidase II: a QM/MM metadynamics investigation.
Reilly et al., Ames, United States. In J Am Chem Soc, 2010
Golgi alpha-mannosidase II (GMII), a member of glycoside hydrolase family 38, cleaves two mannosyl residues from GlcNAcMan(5)GlcNAc(2) as part of the N-linked glycosylation pathway.
Variants in KCNQ1, AP3S1, MAN2A1, and ALDH7A1 and the risk of type 2 diabetes in the Chinese Northern Han population: a case-control study and meta-analysis.
Xin et al., Beijing, China. In Med Sci Monit, 2010
KCNQ and AP3S1, but not MAN2A1 or ALDH7A1 have a role in risk of type 2 diabetes in the Chinese Northern Han population
Structural investigation of the binding of 5-substituted swainsonine analogues to Golgi alpha-mannosidase II.
Rose et al., Toronto, Canada. In Chembiochem, 2010
Golgi alpha-mannosidase II (GMII) is a key enzyme in the N-glycosylation pathway and is a potential target for cancer chemotherapy.
Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidase.
Davies et al., York, United Kingdom. In Plos One, 2009
The most extensively studied of these enzymes is the Drosophila GH38 alpha-mannosidase II, which has been shown to be a retaining alpha-mannosidase that targets both alpha-1,3 and alpha-1,6 mannosyl linkages, an activity that enables the enzyme to process GlcNAc(Man)(5)(GlcNAc)(2) hybrid N-glycans to GlcNAc(Man)(3)(GlcNAc)(2). Far less well understood is the observation that many bacterial species, predominantly but not exclusively pathogens and symbionts, also possess putative GH38 alpha-mannosidases whose activity and specificity is unknown.
Studies toward new anti-cancer strategies based on alpha-mannosidase inhibition.
Juillerat-Jeanneret et al., Lausanne, Switzerland. In Chimia (aarau), 2009
Following the studies on swainsonine, a natural inhibitor of Golgi alpha-mannosidase II, which highlighted the inhibition of cellular mannosidases as a potential innovative approach for the treatment of cancer, several dihydroxylated pyrrolidines and analogues were developed as new potent inhibitors of alpha-mannosidases II able to induce antiproliferative effects in human cancer cells.
Human lysosomal alpha-mannosidases exhibit different inhibition and metal binding properties.
Rose et al., Toronto, Canada. In Protein Sci, 2009
hLM and hEpman were significantly inhibited by the class II alpha-mannosidase inhibitors, swainsonine and mannostatin A. We show that three pyrrolidine-based compounds designed for selective inhibition of Golgi alpha-mannosidase II (GMII) exhibited varying degrees of inhibition for hLM and hEpman.
Innate immune response triggers lupus-like autoimmune disease.
Paulson, Los Angeles, United States. In Cell, 2007
Reporting in Immunity, Green et al. (2007) now show that mice lacking alpha-mannosidase II develop an autoimmune disease similar to lupus.
Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation.
Harvey et al., Oxford, United Kingdom. In Febs Lett, 2007
The disruption of Golgi alpha-mannosidase II activity by swainsonine in human embryonic kidney cells is capable of inducing a novel class of hybrid-type glycosylation containing a partially processed mannose moiety.
In vivo role of alpha-mannosidase IIx: ineffective spermatogenesis resulting from targeted disruption of the Man2a2 in the mouse.
Akama et al., Los Angeles, United States. In Biochim Biophys Acta, 2003
Alpha-mannosidase IIx (MX) is an enzyme closely related to the Golgi N-glycan processing enzyme alpha-mannosidase II (MII).
Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals.
Moremen, Athens, United States. In Biochim Biophys Acta, 2003
The maturation of N-glycans to complex type structures on cellular and secreted proteins is essential for the roles that these structures play in cell adhesion and recognition events in metazoan organisms.
The role of N-glycans in spermatogenesis.
Akama et al., Los Angeles, United States. In Cytogenet Genome Res, 2002
Alpha-mannosidase IIx (MX) was identified as the gene product of processing alpha-mannosidase II (MII)-related gene.
MS screening strategies: investigating the glycomes of knockout and myodystrophic mice and leukodystrophic human brains.
Dell et al., London, United Kingdom. In Biochem Soc Symp, 2001
Thus novel glycosylation pathways have been uncovered in two such knockouts, namely alpha-mannosidase II null mice and UDP-N-acetylglucosamine: alpha 6-D-mannoside beta 1,2-N-acetylglucosaminyltransferase II null mice.
Genetic remodeling of protein glycosylation in vivo induces autoimmune disease.
Marth et al., San Diego, United States. In Proc Natl Acad Sci U S A, 2001
This article discribes experiments in which the MAN2A1 homologue in mouse was deleted, resulting in a systemic autoimmune disease in the mice which is similar to human systemic lupus erythematosus.
Importance of glycosidases in mammalian glycoprotein biosynthesis.
Herscovics, Montréal, Canada. In Biochim Biophys Acta, 2000
Removal of mannose residues continues in the Golgi with the action of alpha1, 2-mannosidases IA and IB that can form Man(5)GlcNAc(2) and of alpha-mannosidase II that removes the alpha1,3- and alpha1,6-linked mannose from GlcNAcMan(5)GlcNAc(2) to form GlcNAcMan(3)GlcNAc(2).
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