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At least 73 records · Page 4Linked to original sources
PubMed1985

Histamine release by esterase inhibitors. The regulation of histamine release from human leukocytes of allergic and non-allergic individuals by the serine esterase inhibitors diisopropyl fluorophosphate and pinacolyl methylphosphorofluoridate.

The serine esterase inhibitor diisopropyl fluorophosphate (DFP) has been shown to inhibit IgE-dependent histamine release. Recently, it has been demonstrated that lower concentrations of DFP enhanced IgE-dependent histamine release and inhibited desensitization. This manuscript describes the ability of another esterase inhibitor, pinacolyl methylphosphorofluoridate (soman), to directly cause release of histamine from human leukocytes (basophils) by a process that is IgE-independent. This release process requires calcium and is also temperature-dependent but occurs over a longer period of time than IgE-dependent release. These data suggest that there is a serine esterase which controls histamine release, and inhibition of this esterase causes histamine release.

Enzyme Inhibitors↗
PubMed1979

Effect of halogenated benzenes on acetanilide esterase, acetanilide hydroxylase and procaine esterase in rats.

1,2,4-Trichlorobenzene, 1,3,5-trichlorobenzene, hexachlorobenzene, 1,2,4-tribromobenzene, 1,3,5-tribromobenzene and hexabromobenzene were compared for their abilities to induce acetanilide esterase, acentailide hydroxylase and procaine esterase. Except for hexabromobenzene all induced acetanilide esterase whereas the hydroxylation of acetanilide was seen only with the fully halogenated benzenes and with 1,3,5-tribromobenzene. Hepatic procaine esterase activity was increased by the three chlorinated benzenes and 1,2,4-tribromobenzene.

Acetanilides↗
PubMed1983

Arterial neutral cholesteryl esterase. A hormone-sensitive enzyme distinct from lysosomal cholesteryl esterase.

We describe here an activable neutral cholesteryl esterase (EC 3.1.1.13) in arteries similar to the hormone-sensitive lipase of adipose tissue and adrenal cortex. Maximum enzyme activity in rabbit aorta was given by cholesteryl ester substrates dispersed as a mixed micelle with phosphatidylcholine and Na taurocholate (molar ratio 1:4:2). A quantitative assay of enzymic activity was obtained with the following component concentrations: 6.0 microM cholesteryl [1-14C]oleate, 23.7 microM phosphatidylcholine, 12.5 microM Na taurocholate, 0.04% serum albumin, and 85 mM K phosphate buffer, pH 7.0. The enzymic activity in aortic homogenates was stimulated 2-fold by addition of 5 microM glucagon or 100 microM dibutyryl cAMP. This activation was Mg-ATP dependent. Addition of 50 micrograms/ml of exogenous protein kinase could reverse the action of protein kinase inhibitor on dibutyryl cAMP activation of the neutral cholesteryl esterase. In addition to activation by cAMP-dependent protein kinase, the enzyme could be distinguished from the more active arterial lysosomal cholesteryl esterase by its pH 7.0 optimum, relative stability to preincubation at elevated temperatures, and exclusive localization in the cell cytosol. Subcellular fractionation of lipid-laden arterial foam cells revealed a significant portion of the neutral cholesteryl esterase bound to cytoplasmic cholesteryl ester-rich lipid droplets. Our results suggest that the breakdown of cytoplasmic cholesteryl ester droplets in arterial cells may be under hormonal regulation.

Animals↗
PubMed2004

Acquired C1 esterase inhibitor deficiency or serendipity? The chance finding of a paraprotein after an apparently low C1 esterase inhibitor concentration.

Acquired C1 esterase inhibitor deficiency is a rare condition, usually presenting after the 2nd decade of life, and is often related to underlying conditions such as autoimmune and lymphoproliferative disorders. This case report describes a man whose initial clinical presentation with acute angioedema and whose initial estimation of a low C1 esterase inhibitor concentration indicated that he had an acquired angioedema, possibly secondary to a B cell neoplasm. A paraprotein was detected, and although its detection was serendipitous because it hinged on a spurious C1 esterase inhibitor result, this case confirms the role of C4 concentrations in the investigation of C1 esterase inhibitor deficiency. It also confirms the need to obtain repeat confirmatory samples before arriving at a diagnosis, however convincing the clinical signs may be.

Acute Disease↗
PubMed1981

Biochemical genetics of rat esterases: another genetically determined variant, Es-7, is linked to five other esterase loci.

A new esterase variant has been isolated by electrophoresis of homogenized testis, heart, and lung tissues. This esterase variant is genetically determined. The carrier strain was crossed with another in which the enzyme was not originally present; the presence of the enzyme was investigated in successive generations and in backcrosses to the carrier strain. Linkage was found with other esterases linkage group V, while there was independent segregation from the immunogenetic markers Ly-1, Ly-2, LH-1 and Rt-la.

Alleles↗
PubMed1981

Esterase-16 (es-16): characterization, polymorphism, and linkage to chromosome 3 of a kidney esterase locus of the house mouse.

A polymorphism for an isozyme of a presumed arylesterase, esterase-16 (EC 3.1.1.2), has been detected in kidney, heart, and spleen of the house mouse, Mus musculus, by means of isoelectric focusing and by disc electrophoresis. Three phenotypes can be distinquished: the ES-16A phenotype (IEP 5.9) was found in C57BL/10Sn and many other laboratory inbred strains; the ES-16B phenotype (IEP 6.1) was found in M. m. molossinus; and the ES-16C phenotype (IEP 5.9; very weak activity) was found in Peru-Coppock. Esterase-16 is strongly inhibited by 10(-3) M p-chloromercuribenzoate, but not by 2. 10(-4) M bis-p-nitrophenyl phosphate or by 10(-3) M Diamox. It stains well with indoxyl acetate and other indigogenic substrates but only weakly with alpha-naphthyl acetate. Esterase-16 is completely insoluble in water. It is apparently governed by a structural gene locus, Es-16, with three alleles, Es-16a, Es-16b, and ES-16c, respectively. Es-16 is closely linked to Car-1 and Car-2 on chromosome 3 Typing of 94 animals of the backcross (C57BL/10Sn x M. m. mol.) F1 x M. m. mol. revealed a recombination frequency of 8.51 /+- 2.9%.

Animals↗
PubMed1975

Esterase. XXI. Es-9, a possibly new polymorphic esterase in Mus musculus genetically linked to es-2.

A so far undescribed gene controlling zone III esterases has been detected by means of disc gel electrophoresis of kidney homogenates from the two inbred mice strains NMRI and SK/Cam. The gene is tentatively designated Es-9, and the two codominant alleles are designated Es-9a and Es-9b. Es-9 esterases are present in many tissues, but, unlike the other zone III esterase (controlled by Es-5), are not found in the serum. Close linkage with the Es-2 gene leads us to map the Es-9 gene on chromosome 8.

Alleles↗
PubMed1976

Esterases in the mosquito Culex pipiens pipiens L: formal genetics and polymorphism of adult esterases.

The genetics of two esterase loci active in autogenous adults of the mosquito Culex pipiens pipiens L. has been studied by means of starch gel electrophoresis. Three alleles at the Est-1 locus and eight at the Est-2 locus are described. Both loci have a null allele. Active alleles are codominant and there is no hybrid enzyme in heterozygotes. The Est-1 locus codes esterases preferentially hydrolyzing alpha-naphthylacetate and the Est-2 locus esterases preferentially hydrolyzing beta-naphthylacetate. Strains homozygous for both loci were selected. Linkage studies of the two loci have shown that they are not sex linked but are linked to each other, the crossover frequency being 8.6%. The polymorphism of two laboratory and two natural populations is described for both loci. Phenotypic distributions are in good agreement with Hardy-Weinberg expectations.

Alleles↗
PubMed1994

A cluster of at least three esterase genes in Lucilia cuprina includes malathion carboxylesterase and two other esterases implicated in resistance to organophosphates.

Three distinct malathion carboxylesterase (MCE) phenotypes have been identified among strains of Lucilia cuprina. The high-activity phenotype shows 1.6- and 33-fold more MCE specific activity than the intermediate- and low-activity phenotypes, respectively. Flies with high MCE activity are 1000-fold more resistant to malathion than flies with either low or intermediate MCE phenotypes, which are equally susceptible. High and low MCE specific activity are allelic and encoded by the Rmal gene on chromosome 4. Rmal is clustered within one map unit of two other esterase genes, Rop1 and E9, which are implicated in resistance to other organophosphate insecticides. Intermediate MCE specific activity is also inherited within the cluster, although its allelism to Rmal, Rop1, or E9 is unclear. The cluster does not contain the gene for the hemolymph esterase E4, which maps 6.1 map units from Rop1, on the other side of the bubbled wing marker. The cluster appears to be homologous to part of a tandem array of 11 esterase genes on chromosome 3R of Drosophila melanogaster.

Animals↗
PubMed2000

Quantitative deficiency of monocyte-specific esterase (MSE) mRNA in monocyte esterase deficiency (MED).

Cytochemical staining of monocyte-specific esterase (MSE) is widely used for identification of the monocytic lineage in leukaemias. Deficiency of this enzymatic activity occurs as a familial trait and the deficiency has been shown to occur with greater frequency in patients with lymphoproliferative or gastrointestinal malignant neoplastic diseases than in normal blood donors. Reverse transcriptase polymerase chain reaction (RT-PCR), sequencing and quantification by Northern blot analysis was conducted on the MSE mRNA of 12 subjects with monocyte esterase deficiency (MED) and seven MSE-positive subjects to examine whether mutations were present or whether the defect was quantitative. Mutations were not found in the mRNA sequences. However, MED subjects had significantly less MSE mRNA than MSE-positive subjects (P = 0.001). These findings show that deficiency of monocyte esterase activity in MED is not as a result of the presence of inactive isoenzymes and may be owing to an abnormality in the regulation of mRNA production.

Anemia, Hemolytic, Autoimmune↗
PubMedDate not supplied

[Puffing in the regions of the esterase and ecdysterone genes in Drosophila lummei strains differing in beta-esterase expression].

Correlation between the activity of esterase and ecdysterone puffs was observed by comparison of puff expression in the areas of alpha- and beta-esterase genes localization and exogenous ecdysterone-sensitive areas (2-G-1-2-G-5). 2-G-5 puff expression and beta-esterase activation correlated with decrease of ecdysterone puffs activity. Constant puffing in 2-G-1 and 2-G-4 matched with constant activity of alpha-specific isoenzymes. The F1 larvae from cross between lines with normal and null-allele beta Est2 gene carried heteromorph puff and its expression depended upon cross direction.

Alleles↗
PubMed1978

Esterase XXVII. Purification and characterization of esterase-9A of mouse kidney.

Esterase-9A, which appears electrophoretically as a triplet of the bands III-50, III-40 and III-30, was isolated from the kidneys of male NMRI-mice by isoelectrofocusing and refocusing followed by repeated molecular sieve chromography. The overall purification was approx. 250 fold and each of the three bands was isolated separately. The band of the triplet nearest to the cathode, III-50, changed in vitro into the satellite bands III-40 and III-30 and, further, into the band III-22 not observed before in the homogenate. It is assumed that the band III-50 represents the original gene product. The molecular weight (45 000) of the band III-50 is identical with those of III-40 and III-30, as measured by analytical electrophoresis, whereas the molecular weight obtained by thin-layer chromatography was 51 000. There were no obvious signs that esterase-9 was composed of subunits. The Km constant for 4-nitrophenyl proprionate was identical for each of three bands. The esterase-9A is the first testosterone-dependent isozyme of the mouse carboxylesterase (carboxylicester hydrolase, EC 3.1.1.1) system which has been isolated.

Animals↗
PubMed1988

Lymph esterases of the house mouse (Mus musculus)--I. Identification and possible origins of abdominal lymph esterases.

1. Abdominal lymph was obtained from Mus musculus by cannulation of the thoracic duct: lymph esterases were identified by polyacrylamide gel electrophoresis. Seven known esterases (ES-1, ES-2, ES-5, ES-27, SE-I, SE-II and SE-III) and a newly described activity (SE-IV) were demonstrated, all of which were also present in serum. 2. Electrophoretic staining intensities indicated that the lymph esterases were less concentrated than the corresponding activities in serum, with the single exception of ES-2. This finding was supported by quantitative immunoelectrophoresis of ES-1 and ES-2 (two allozymes each). 3. The jejunum appeared to be the origin of lymph ES-2 by a comparison of organ distribution of the allozymes ES-2B and ES-2D and by monitoring the re-appearance of ES-2 in several organs, serum and lymph after total inhibition in vivo by bis-p-nitrophenyl phosphate.

Abdomen↗
PubMed2004

The feruloyl esterase system of Talaromyces stipitatus: production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity.

Several extracellular feruloyl esterases were produced by the mesophilic fungus Talaromyces stipitatus when grown on selective carbon sources in liquid media. Type-A and Type-B feruloyl esterases, as defined by their substrate specificity against methyl hydroxycinnamates, were produced during growth on wheat bran and sugar beet pulp, respectively. In addition, Tal. stipitatus produced a new type of esterase (TsFaeC) during growth on sugar beet pulp with a broader spectrum of activity (Type-C) against the (hydroxy)cinnamate esters than those previously described. All three enzymes were purified and N-terminal amino acid sequences and internal peptide sequences determined. The TsFaeC sequences were used to amplify a gene fragment from Tal. stipitatus genomic DNA. The flanking sequences were identified with the aid of RACE-RTPCR, and a full-length clone constructed. The faeC gene is present as a single copy and contains a single intron. The complete cDNA fragment contains an ORF of 1590bp, faeC, which is predicted to encode a 530 amino acid pre-protein, including a 25-residue signal peptide, and to produce a mature protein of M(R) 55 340Da. There was no evidence for a carbohydrate-binding domain in TsFaeC.

Amino Acid Sequence↗
PubMed1994

Synthesis and characterization of a biotinylated organophosphorus ester for detection and affinity purification of a brain serine esterase: neuropathy target esterase.

We have synthesized a novel stable precursor, saligenin phosphorotrichloridate, which, on reaction with N-monobiotinyldiamines, generates a series of biotinylated covalent inhibitors of serine esterases. A homologue designated S9B [1-(saligenin cyclic phospho)-9-biotinyldiaminononane] was selected to allow detection and rapid isolation of neuropathy target esterase (NTE). This enzyme is the primary target site for those organophosphorus esters (OPs) which cause delayed neuropathy. NTE comprises about 0.03% of the total protein in brain microsomal fractions and has resisted purification attempts over many years. S9B is a potent progressive inhibitor of NTE esteratic activity (second-order rate constant 1.4 x 10(7) M-1.min-1). Incubation of S9B with brain microsomes led to specific covalent labelling of NTE as determined by detection of a biotinylated 155 kDa polypeptide on Western blots. Specificity of S9B labelling was further demonstrated by inhibition with the neuropathic OP mipafox. Biotinyl-NTE in SDS-solubilized S9B-labelled microsomes was adsorbed on to avidin-Sepharose and subsequently eluted, yielding a fraction enriched approx. 1000-fold in NTE by a single step with recoveries of 30%. Essentially pure NTE was obtained after separation from two endogenous biotinylated polypeptides (120 and 70 kDa) in avidin-Sepharose eluates by preparative SDS/PAGE. Other biotinylated saligenin phosphoramidates derived from the same precursor may be useful for detection and isolation of other serine esterases and proteinases.

Animals↗
PubMed1997

Divergent and conserved features in the spatial expression of the Drosophila pseudoobscura esterase-5B gene and the esterase-6 gene of Drosophila melanogaster.

The regulatory regions of homologous genes encoding esterase 6 (Est-6) of Drosophila melanogaster and esterase 5B (Est-5B) of Drosophila pseudoobscura show very little similarity. We have undertaken a comparative study of the pattern of expression directed by the Est-5B and Est-6 5'-flanking DNA to attempt to reveal conserved elements regulating tissue-specific expression in adults. Esterase regulatory sequences were linked to a lacZ reporter gene and transformed into D. melanogaster embryos. Est-5B, 5' upstream elements, give rise to a beta-galactosidase expression pattern that coincides with the wild-type expression of Est-5B in D. pseudoobscura. The expression patterns of the Est-5B/lacZ construct are different from those of a fusion gene containing the upstream region of Est-6. Common sites of expression for both kinds of constructs are the third segment of antenna, the maxillary palps, and salivary glands. In vitro deletion mutagenesis has shown that the two genes have a different organization of regulatory elements controlling expression in both the third segment of antenna and maxillary palps. The results suggest that the conservation of the expression pattern in genes that evolved from a common ancestor may not be accompanied by preservation of the corresponding cis-regulatory elements.

Animals↗
PubMed2000

The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity.

The Bacillus pumilus gene encoding acetyl xylan esterase (axe) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) purified from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar size and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.

Acetylesterase↗
PubMed1990

Genetic identification of non-specific esterases of the mouse cauda epididymidis and description of esterase-28, a new carboxylesterase isoenzyme (EC 3.1.1.1).

Twenty-five (25) electrophoretic bands with esterase activity were distinguished in supernatants of cauda epididymidis of DBA/2J mice. Twenty (20) of these were assigned to 10 genetically defined esterases (ES-1, ES-2, ES-3, ES-6, ES-7, ES-11, ES-14, ES-17, ES-19, ES-22) which were already known from investigations of other mouse tissues. Furthermore, ES-10 was identified in cauda supernatants after isoelectric focussing. A hitherto genetically undefined esterase was assigned to locus Es-28 which was expressed solely in the epididymis. Three phenotypes were distinguished: ES-28A was present in the majority of the inbred strains examined. ES-28B was observed in AKR/Han mice and ES-28C was found in SEG/1 mice.

Alleles↗