ArticleThe Journal of biological chemistry2013
Identification of ectonucleotide pyrophosphatase/phosphodiesterase 3 (ENPP3) as a regulator of N-acetylglucosaminyltransferase GnT-IX (GnT-Vb).
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 40 citations in OpenAlex.
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- Identification of the extracellular membrane protein ENPP3 as a major cGAMP hydrolase and innate immune checkpoint.Cell reports · 2024Article
- Antibody-Drug Conjugates for the Treatment of Renal Cancer: A Scoping Review on Current Evidence and Clinical Perspectives.Journal of personalized medicine · 2023Review
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- β-Lactoglobulin affects the oxidative status and viability of equine endometrial progenitor cells via lncRNA-mRNA-miRNA regulatory associations.Journal of cellular and molecular medicine · 2023Article
- Structure-based design of UDP-GlcNAc analogs as candidate GnT-V inhibitors.Biochimica et biophysica acta. General subjects · 2022Article
- Genome-Wide Selective Analysis of Boer Goat to Investigate the Dynamic Heredity Evolution under Different Stages.Animals : an open access journal from MDPI · 2022Article
- A Proteome Approach Reveals Differences between Fertile Women and Patients with Repeated Implantation Failure on Endometrial Level⁻Does hCG Render the Endometrium of RIF Patients?International journal of molecular sciences · 2019Article
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- Crystallization of ectonucleotide phosphodiesterase/pyrophosphatase-3 and orientation of the SMB domains in the full-length ectodomain.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Crystal structure and substrate binding mode of ectonucleotide phosphodiesterase/pyrophosphatase-3 (NPP3).Scientific reports · 2018Article
- Compartmentalized gene expression profiling of receptive endometrium reveals progesterone regulated ENPP3 is differentially expressed and secreted in glycosylated form.Scientific reports · 2016Article
- Regulation of allergic inflammation by the ectoenzyme E-NPP3 (CD203c) on basophils and mast cells.Seminars in immunopathology · 2016Review
- Enzymes for N-Glycan Branching and Their Genetic and Nongenetic Regulation in Cancer.Biomolecules · 2016Review
- Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase.Scientific reports · 2016Article
- Counter-regulatory phosphatases TNAP and NPP1 temporally regulate tooth root cementogenesis.International journal of oral science · 2015Article
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Our previous studies on a β1,6-N-acetylglucosaminyltransferase, GnT-IX (GnT-Vb), a homolog of GnT-V, indicated that the enzyme has a broad GlcNAc transfer activity toward N-linked and O-mannosyl glycan core structures and that its brain-specific gene expression is regulated by epigenetic histone modifications. In this study, we demonstrate the existence of an endogenous inhibitory factor for GnT-IX that functions as a key regulator for GnT-IX enzymatic activity in Neuro2a (N2a) cells. We purified this factor from N2a cells and found that it is identical to ectonucleotide pyrophosphatase/phosphodiesterase 3 (ENPP3), as evidenced by mass spectrometry and by the knockdown and overexpression of ENPP3 in cultured cells. Kinetic analyses revealed that the mechanism responsible for the inhibition of GnT-IX caused by ENPP3 is the ENPP3-mediated hydrolysis of the nucleotide sugar donor substrate, UDP-GlcNAc, with the resulting generation of UMP, a potent and competitive inhibitor of GnT-IX. Indeed, ENPP3 knockdown cells had significantly increased levels of intracellular nucleotide sugars and displayed changes in the total cellular glycosylation profile. In addition to chaperones or other known regulators of glycosyltransferases, the ENPP3-mediated hydrolysis of nucleotide sugars would have widespread and significant impacts on glycosyltransferase activities and would be responsible for altering the total cellular glycosylation profile and modulating cellular functions.
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