Disease relevance of Es1

• None of the lymphomas stained with T-cell antibodies or the esterase; 15 did not stain for immunoglobulin, but 13 of these 15 did express Ia antigen [1].
• These results favor the hypothesis that esterase inhibition leads to an agonist-induced myopathy, which is mediated by Ca++ and requires an intact AChR [2].
• In mice whose oxidative metabolism had been increased with beta-ionone or in which esterase metabolism had been inhibited by diazinon, the severity of the toxicity was increased but the intraacinar origin of the lesion did not change [3].
• Both compounds inhibited the growth of preestablished 4T1 tumors when given i.p. However, when given by oral gavage, only the esterase-resistant Valpha-TEA was able to suppress primary tumor growth and reduce lung metastasis [4].
• In the accompanying paper (Shi, W.-X., Chammas, R., and Varki, A. (1996) J. Biol. Chem. 261, 31517-31525), we report that the extent of 9-O-acetylation of cell surface sialic acids on murine erythroleukemia (MEL) cells can be modified by various manipulations, including differentiation, nocodazole treatment, and 9-O-acetyl esterase treatment [5].

Psychiatry related information on Es1

• This metabolic pathway is normally a minor one in humans, but takes on significance when metabolism of cocaine by the P-450 system is increased, as may occur with excessive alcohol consumption (enzyme induction) or after exposure to organophosphate pesticides (esterase inhibition) [6].

High impact information on Es1

• A similar construct driven by the phenylethanolamine-N-methyltransferase promoter did not cause this block, but gave transgenic mice with selective expression of esterase in the retina and the adrenal gland [7].
• We have selectively destroyed these O-acetyl groups during murine embryogenesis by expressing the 9-O-acetyl-sialic acid-specific esterase of influenza C [7].
• Organophosphorous compounds, which are potent inhibitors of egasyn-esterase activity, caused a rapid dissociation of the high molecular weight egasyn-microsomal beta-glucuronidase complex when administered in vivo or when added in vitro to microsomal suspensions [8].
• The dissociation was relatively specific to phosphodiester inhibitors of the esterase active site [8].
• Involvement of the esterase active site of egasyn in compartmentalization of beta-glucuronidase within the endoplasmic reticulum [8].

Chemical compound and disease context of Es1

• Since a Ca++-activated protease which specifically removes Z-disks is known to exist in mammalian skeletal muscle, we tested the possibility that the myopathy after esterase inactivation is due to the prolongation of acetylcholine lifetime and thus of Ca++ influx [2].
• The myopathy was later mimicked by bath application of carbamylcholine without esterase inhibitors [2].
• Acetyl groups substituted on sialic acid were removed either by alkali treatment or by incubation with influenza virus C, which contains receptor-destroying enzyme (a neuraminidate 9-O-acetyl esterase) [9].
• Specific esterase activity induced in mouse Friend erythroleukemia cells by dimethylsulfoxide [10].
• Between 10 and 15 days after injecting mice intravenously with 89Sr at 2 microCi per gm. of body weight, monocytes were only rarely detectable in the peripheral blood as determined by morphology, stains for nonspecific esterase and peroxidase, and by latex phagocytosis [11].

Biological context of Es1

• Genetic mapping confirmed the location of an egasyn cDNA fragment in cluster 1 of the esterase region on chromosome 8 [12].
• Transfection of COS cells with the 2022-bp cDNA resulted in the expression of esterase activity, which comigrated on native gels with liver esterase-22 [12].
• A further polymorphic rat esterase with broad tissue expression and restricted substrate specificity is described and tentatively called Es-6 [13].
• The genetics of esterase-28, the major esterase of cauda epididymidis of the house mouse, has been studied after separation by polyacrylamide gel electrophoresis and isoelectric focusing [14].
• ES-23 is controlled by a structural locus situated within the esterase gene cluster 2 on chromosome 8 [15].

Anatomical context of Es1

• This protein, like mouse egasyn, has esterase catalytic activity and is concentrated in microsomes [16].
• Since killer-specific esterases and channel-forming proteins can be demonstrated in in vitro cell lines, it is important to ascertain that the described esterase and channel-forming proteins are also present in killer cells from in vivo sources [17].
• Most of the colonies consisted exclusively of large, dispersed macrophages that were intensely stained for nonspecific esterase [18].
• The expressed protein showed a granular pattern in intracellular distribution, was fractionated at the density of lysosomes, and had serine esterase activities; acid carboxypeptidase at pH 5.6, esterase at pH 7.0, and carboxyl-terminal deamidase at pH 7 [19].
• A significant portion of murine hepatocyte beta-glucuronidase is maintained within the endoplasmic reticulum (ER) by complex formation with the esterase active site of the protein egasyn [20].

Associations of Es1 with chemical compounds

• Kidney expression of the electrophoretic esterase band controlled by the Es-6 locus is sex influenced, with increased activity apparently induced by testosterone [21].
• With three of the substrates (alpha-naphthyl acetate and esters 2 and 3), esterase activity was the same in both groups; however, with the others (rho-nitrophenyl acetate and esters 1 and 4), there was a small increase in activity in ovariectomized females, compared with intact females [22].
• These results indicate that clofibrate causes significant alterations in the regulation of esterase activity, whereas sex hormones only cause small changes [22].
• Esterase 1 (Es-1) is a sexually dimorphic 65-kDa glycoprotein present in plasma and other murine tissues able to hydrolyze a variety of esters including fatty acid esters of estradiol [23].
• Assay of different cytotoxic effector cells reveals the presence of N alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester serine esterase in clones with T killer and NK activity, but enzyme levels do not correlate with cytolytic activity nor does inhibition of esterase activity interfere with granule-mediated cell lysis [17].

Regulatory relationships of Es1

• BSF-1 plus PMA stimulated a significant increase in the intracellular content of N-benzyloxycarbonyl-L-lysine thiobenzylester esterase, a granule-associated biochemical marker, whereas IL-2 plus PMA was only marginally effective [24].
• Inhibition of amyloid formation was dependent on the molar ratio AChE:mAb 25B1, and at least 50% of the inhibition of the AChE promoting effect occurs at a molar ratio similar to that required for inhibition of the esterase activity [25].
• The esterase was found to increase markedly the mEGF-induced incorporation of glucosamine into extracellular hyaluronic acid, while the addition of ascorbic acid did not significantly alter glucosamine incorporation [26].
• Although originally described as mouse B lymphocytes, the IIA1.6 cells proved positive for non-specific esterase activity and expressed the CD5 antigen [27].

Other interactions of Es1

• The acd mutant gene has been mapped just proximal to oligosyndactyly (Os) and esterase-1 (Es-1) in the central region of chromosome 8 [28].
• Allelic differences at an esterase locus designated Es-6 exist between mouse strain C57 BL/6J and a laboratory stock of M.m. molossinus [21].
• Esterase. XXI. Es-9, a possibly new polymorphic esterase in Mus musculus genetically linked to es-2 [29].
• Polymorphism of esterase 11 in Mus musculus, a further esterase locus on chromosome 8 [30].
• We have examined the linkage relationships between Aprt and the markers of chromosome 8 including esterase-1 and the centromere [31].

Analytical, diagnostic and therapeutic context of Es1

• Esterase 1F was isolated from mouse serum and purified by ion-exchange chromatography, isoelectrofocusing, and molecular sieve chromatography [32].
• Similarly, immunoblotting after sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an affinity-purified rabbit antibody to Es-1 showed no cross-reacting proteins in the plasma until after birth [23].
• Northern blot analysis of total RNA from a variety of adult mouse tissues showed the presence of substantial levels of Es-1 mRNA only in liver with lower levels in kidney, testes, and ovaries [23].
• The enzyme was identified after disc electrophoresis and subsequent staining for esterase using alpha-naphthyl acetate as the substrate [33].
• Molecular cloning, characterization, and differential expression pattern of mouse lung surfactant convertase [34].

References