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Basophil CD203c surface expression reliably discriminated cystic fibrosis (show S100A8 Proteins) with allergic bronchopulmonary aspergillosis from cystic fibrosis (show S100A8 Proteins) with Aspergillus colonization and cystic fibrosis (show S100A8 Proteins) over time.
Both NPP1 (show ENPP1 Proteins) and NPP3 ectoenzymes are expressed in N2a cells, their levels dramatically changing when cells differentiate into a neuronal-like phenotype
Expression of CD203c on basophils as a marker of immunoglobulin E-mediated (L)-asparaginase (show ASRGL1 Proteins) allergy.
Anaphylactic transfusion reaction in homozygous haptoglobin (show HP Proteins) deficiency detected by CD203c expression on basophils.
ENPP3 is a regulator of N-acetylglucosaminyltransferase (show GCNT2 Proteins) GnT-IX (GnT-Vb (show MGAT5B Proteins))
The early signaling requirements for the CD11b (show ITGAM Proteins)/CD203c compartment expression and CD63 (show CD63 Proteins) degranulation provide support for the hypothesis that CD11b (show ITGAM Proteins) and CD203c reside in a similar compartment.
Subjects with nut allergy show an increase of basophil CD203c levels at baseline and following rapid ex vivo stimulation with nut allergen
Asthma exacerbation was accompanied by increased expression of CD203c on basophils that decreased significantly during remission
Influence of hyperosmotic conditions on basophil CD203c upregulation in patients with food-dependent exercise-induced anaphylaxis.
Data show that low and high dilutions of histamine inhibit CD203c up-regulation in anti-IgE stimulated basophils.
In Enpp3-/- mice, ATP concentrations were increased in the intestinal lumen. Plasmacytoid dendritic cell (pDC (show PDC Proteins)) numbers were remarkably decreased in the small intestinal lamina propria and Peyer's patches. Intestinal pDCs of Enpp3-/- mice showed enhanced cell death.
E-NPP3 decreases ATP concentration and suppresses basophil and mast cell activity.
The protein encoded by this gene belongs to a series of ectoenzymes that are involved in hydrolysis of extracellular nucleotides. These ectoenzymes possess ATPase and ATP pyrophosphatase activities and are type II transmembrane proteins. Expression of the related rat mRNA has been found in a subset of immature glial cells and in the alimentary tract. The corresponding rat protein has been detected in the pancreas, small intestine, colon, and liver. The human mRNA is expressed in glioma cells, prostate, and uterus. Expression of the human protein has been detected in uterus, basophils, and mast cells.
, dJ1005H11.3 (phosphodiesterase I/nucleotide pyrophosphatase 3)
, dJ914N13.3 (phosphodiesterase I/nucleotide pyrophosphatase 3)
, ectonucleotide pyrophosphatase/phosphodiesterase family member 3
, phosphodiesterase I beta
, phosphodiesterase I/nucleotide pyrophosphatase 3
, phosphodiesterase-I beta
, RB13-6 antigen
, alkaline phosphodiesterase
, ectonucleotide pyrophosphatase/phosphodiesterase 3
, ectonucleotide pyrophosphatase/phosphodiesterase family member 3-like
, ectonucleotidase enpp3