Publication for CELA3A and CELA3B

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression
CoexViewer
hsa CELA3A chymotrypsin like elastase 3A 10136 [link]
hsa CELA3B chymotrypsin like elastase 3B 23436

Pubmed ID Priority Text
27999401 0.98 CELA3A and CELA3B and the gene conversion in CELA3B alter elastase secretion and activity, we transfected human embryonic kidney (HEK) 293T cells with expression plasmids and measured proelastase levels in the conditioned medium by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and elastase activity by enzymatic assays.
0.98 CELA3A and CELA3B are also shown.
0.98 CELA3A and CELA3B.
0.98 CELA3A and CELA3B variants in the conditioned medium of transfected HEK 293T cells.
0.97 CELA3B between c.736 and c.742 was converted with the corresponding CELA3A sequence.
0.97 CELA3B variant, we found no other association of CELA3A and CELA3B variants with CP or disease subgroups ACP and ICP.
0.96 CELA3A p.G241A variant was increased by 1.8-fold, whereas activity of the CELA3B p.A241G variant was decreased by 2.2-fold relative to their respective wild-type controls.
0.95 CELA3A and p.A241G in CELA3B had opposite effects on elastase activity.
0.95 CELA3A and CELA3B are polymorphic in the population.
0.94 CELA3A and p.A241G in CELA3B between subjects with CP and controls without pancreatic disease.
0.94 CELA3A p.G241A variant and/or enrichment of the CELA3B p.A241G variant in a cohort of CP patients versus population controls.
0.93 CELA3A and CELA3B.
0.92 CELA3A nor p.A241G in CELA3B was significantly enriched in patients or controls.
0.92 CELA3A and CELA3B genes and replication of the observed association(s) in an independent cohort.
0.90 CELA3A is 92% identical with CELA3B in its primary structure, it does not form tight complexes with proCPA1 or proCPA2.
0.90 CELA3A and CELA3B variants.
0.89 CELA3A and c.722C>G (p.A241G) in CELA3B in subjects with CP and controls without pancreatic disease.
0.88 CELA3A and CELA3B in a cohort of 225 subjects with chronic pancreatitis (120 alcoholic and 105 non-alcoholic) and 300 controls of Hungarian origin.
0.86 CELA3B forms stable complexes with procarboxypeptidases A1 and A2 whereas CELA3A binds poorly due to the evolutionary substitution of Ala241 with Gly in exon 7.
0.83 CELA3A p.G241A and 1.5% for CELA3B p.A241G in controls, and no significant difference was observed in patients.
0.78 CELA3A and CELA3B are not associated with chronic pancreatitis, indicating that changes in complex formation between proelastases and procarboxypeptidases do not alter pancreatitis risk.
0.77 CELA3A (p.G241A) and CELA3B (p.A241G), genetic analysis can directly assess whether individual variability in complex formation might alter risk for chronic pancreatitis.
0.73 CELA3A and CELA3B in 225 patients and 300 controls from the registry of the Hungarian Pancreatic Study Group.
0.70 CELA3A and CELA3B in CP patients and controls of Hungarian origin.
0.60 CELA3A increases whereas mutation p.A241G in CELA3B reduces binding to proCPA1.
0.58 CELA3A and CELA3B was detected in a CP patient, however, this is likely an accidental finding as we found no functional defect with respect to secretion or activity of the converted CELA3B that might suggest a pathogenic role in CP.
0.53 CELA3A and CELA3B) to Assess the Role of Complex Formation between Proelastases and Procarboxypeptidases in Chronic Pancreatitis
21631589 0.98 ELA3A, ELA3B) are inactive or markedly less effective at promoting procarboxypeptidase activation.
0.95 ELA3A, ELA3B) do not digest the trypsinogen activation peptide.
26171222 0.97 elastase 1 (ELA1), ELA2, ELA2A, ELA2B, ELA3A, and ELA3B) are known.
0.96 ELA3B exhibited moderate specific activity, and ELA3A showed weak specific activity.
0.96 ELA3A, and ELA3B) were cloned, expressed in human cells, purified from the conditioned medium, and activated with trypsin.
0.90 ELA3A and ELA3B are known to have a slight elastolytic activity but do have protease activity with preferential cleavage after alanine (Bode et al.).
0.88 ELA3B, and 5 for ELA3A, ELA3B, and CTSA), and the average of technical duplicates from a representative single experiment is shown with error bars representing the higher value.
24997602 0.97 CELA3A and CELA3B (Fig. 3c).
0.92 CELA3A and CELA3B (which were not among the 94 enzymes screened initially).
0.85 CELA3A and CELA3B are expressed only in the pancreas , it seems unlikely that their inhibition contributes to telaprevir-associated rash.
22111014 0.97 FE1 has been investigated in subjects with both diabetes mellitus and hypovitaminosis D, fecal pancreas elastase 1 in subjects with obesity syndrome and vitamin D deficiency has not been demonstrated.
0.74 elastase 1 in feces (FE1) has previously been regarded to be revealed sensitivities of 14%, 87%, and 95% for the Cambridge grades I, II, and III, and correlated significantly with this classification of severity of chronic pancreatitis.
27459204 0.97 CELA3A, CELA3B) are encoded in the human genome.
30085215 0.97 CELA3B:CELA3A were similarly reported as being significantly up/down regulated in these studies, whereas MS4A10 was not reported in them.
27620696 0.96 CELA3A, CELA3B, CTRC, CPA1, CPA2, and PNLIP (Figure 6) in acinar tissue compared to islets is in agreement with data from HPA and with previous studies on protein and gene expression levels.
29886024 0.94 elastase-1 values; six of these nine children had fecal elastase-1 >200 mug/g at week 24, a value consistent with normal pancreatic function.
30774274 0.94 fecal elastase 1 > 200 mug/g), mildly reduced (100-200 mug/g) and severely reduced (fecal elastase 1 < 100 mug/g).
31619925 0.94 fecal elastase-1 shows close correlation with the pancreatic output of pancreatic enzymes including elastase-1, amylase, lipase, and trypsin.
23035638 0.91 ELA3A, ELA3B) do not catalyze this reaction.
0.89 ELA3A, ELA3B) did not catalyze cleavage of this peptide bond to a detectable extent (Fig 2).
0.70 ELA3A) and proelastase 3B (ELA3B).
17389914 0.91 ELA3A, ELA3B), carboxypeptidase A (CPA2), pancreatic lipase (PNLIP), and trypsin (PRSS2) were enriched in this cluster (Figures 1, "Acinar" cluster).
23601753 0.86 ELA3A, ELA3B) do not catalyze this reaction (Figure 4C).
30100563 0.82 CELA3A protein was grouped with the highly homologous CELA3B, and the two are both known as pancreatic elastase 1.
26929737 0.73 pancreatic elastase 1 and pancreatic elastase 3 (ELA1 and ELA3A and ELA3B).
24328148 0.66 elastase 3b (formerly designated elastase 1) in pancreatic cancer tissue samples have been observed by several groups.
30633213 0.66 CELA3A and CELA3B are downregulated in prostate cancer, which is consistent with our results.
25910082 0.63 CELA3B, CPA2, CTRL, GP2, CPB1, CTRC, RBPJL, KLK1, PLA2G1B, CELA2A, CEL, GNMT, CELA3A, CPA1, PRSS3P2, PRSS3, CLPS, PNLIP, SLC39A5, SPINK1, CTRB1, TMED11P, PRSS1, GATM), encoding pancreatic acinar cell secretory- and related proteins (Table 2).
32099594 0.61 Elastase 3A, CystD, and CELA3B expression in GC progression They believed that three-biomarker panel of CystD+PepA-Ela3A could be sufficient for GC diagnosis with 95.7% sensitivity.



The preparation time of this page was 0.0 [sec].