Disease relevance of Es2

• High glucose suppressed the enzyme activity of the E1 component of the BCKDH complex, as well as the total activity of the BCKDH complex, to usually negligible levels in islets and decreased by an average of 90% the mRNA which encodes E1 alpha, the catalytic subunit of the E1 component of BCKDH, in islets and rat insulinoma cells [1].
• Parkinson's disease is also characterized by decreases in midbrain levels of total glutathione which could impact on E1 enzyme activity via oxidation of the active site sulfhydryl [2].
• BFA (2.5 micrograms/ml) inhibited not only the secretion of plasma proteins into the medium, but also the assembly of both G protein of VSV and E1 and E2 proteins (envelope proteins) of sindbis virus into respective virions [3].
• The data indicate that glycosylation of cellular proteins is differently affected by the expression of specific regions of the adenovirus genome, and the combined action of E1 and E4 gene products is important for the expression of the GlcNAc beta 1----6Man group associated with tumorigenicity of the cells [4].
• Dietary protein deficiency decreased the amount of E1 alpha protein to a greater extent than E2 protein [5].

High impact information on Es2

• Glucose regulates leucine-induced insulin release and the expression of the branched chain ketoacid dehydrogenase E1 alpha subunit gene in pancreatic islets [1].
• When the endoplasmic reticulum was completely stained for microsomal carboxyesterase E1, the enzyme was not found to be labeled in the developed envelopes forming autophagic vacuoles [6].
• Cell lines (5WY cells) established from Ad5 wild type-induced foci contained the E1 gene of wild type (E1a and b) [7].
• Cell lines (313Y cells) established from dl313-induced foci contained the E1 gene of the dl313 genome (E1a only) [7].
• This is a reversible process as E1 activity increases upon glutathione restoration [2].

Chemical compound and disease context of Es2

• Retransformation of a revertant cell line with the adenovirus E1 oncogenes and vanadate [8].

Biological context of Es2

• Molecular cloning and nucleotide sequence of cDNA of microsomal carboxyesterase E1 of rat liver [9].
• 7. These data show that E1 causes desensitization and down-regulation of the rat mu-opioid receptor expressed in CHO cells [10].
• 5 These data show that E-1/E-2 bind with high affinity and selectivity to mu-opioid receptors and modulate signal transduction pathways typical of opioids [11].
• E-1/E-2 bound weakly to CHOdelta and CHOkappa membranes, with IC50 values of greater than 10 microM [11].
• To determine whether the reversion mutation was acting in cis or trans the G5 cells were co-transfected with an E1 gene bearing expression plasmid and a neomycin phosphotransferase bearing plasmid [8].

Anatomical context of Es2

• A tetrapeptide (KDEL) which was shown to keep a few microsomal proteins in the lumen of the endoplasmic reticulum was not found in the primary structure of carboxyesterase E1, which suggested the existence of another mechanism for retention of proteins in the lumen of endoplasmic reticulum [9].
• Two key regulatory enzymes involved in citrate synthesis by prostate epithelial cells are mitochondrial aspartate aminotransferase (mAAT) which provides oxalacetate, and PDH E1 alpha (pyruvate dehydrogenase) which provides acetyl CoA for citrate synthesis [12].
• 2 E-1 displaced [3H]-diprenorphine ([3H]-DPN) binding in CHO micro and SH-SY5Y membranes with pKi values of 8.02+/-0.09 and 8.54+/-0.13 respectively [11].
• Carboxyesterase E1 was solubilized from microsomes by treatment with low concentrations of detergents [13].
• In vitro translation of rat liver RNA by reticulocyte lysate showed that carboxyesterase E1 was synthesized preferentially on the bound ribosomes, as a precursor peptide larger than the peptide of the mature enzyme [13].

Associations of Es2 with chemical compounds

• cDNA clones of the mRNA for rat liver carboxyesterase E1, one of the carboxyesterases exclusively located on the luminal side of microsomal vesicles, were isolated [9].
• Sequence analysis of 2 kbp long cDNA revealed the primary structure of carboxyesterase E1, which consisted of 549 amino acids (Mr 60, 171.71) and contained an extra peptide of 18 amino acids at the NH2-terminus of the mature enzyme [9].
• 3 In CHOmu cells, E-1/E-2 inhibited forskolin (1 microM) stimulated cyclic AMP formation with pIC50 values of 8.03+/-0.16 (Imax = 53.0+/-9. 3%) and 8.15+/-0.24 (Imax = 56.3+/-3.8%) respectively [11].
• 1 Endomorphin-1 and -2 (E-1/E-2) have been proposed as endogenous ligands for the mu-opioid receptor [11].
• At this time, we propose that the effects of prolactin and testosterone involve increased expression of the E1 alpha gene of LP and VP epithelial cells, respectively [12].

Other interactions of Es2

• Carboxyesterase E1 showed significant homology with the COOH-terminal portion of thyroglobulin [9].
• In rats fed the low fat diet, but not in those fed the high fat diet, clofibrate raised the activity of serum esterase-1, which (unlike esterase-2) does not hydrolyze clofibrate [14].

Analytical, diagnostic and therapeutic context of Es2

• The intramuscular injection of these plasmids generated a significant level of antibody titers to the E1 and E2 proteins, which maximally reached 850 and 25,000 respectively [15].

References