Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ultrastructural cytochemistry for nonspecific esterase (NSE) was performed on normal and nephritic rabbit kidneys. In normal glomeruli distinct reaction deposits appearing as electron-dense granules were present in visceral epithelial cells (podocytes) and epithelial cells of Bowman's capsule, but only a few small or minute deposits were seen in some endothelial and mesangial cells. In acute proliferative glomerulonephritis (Masugi nephritis), many reaction deposits occurred in mononuclear cells accumulating in glomerular tufts which presented the characteristic features of monocytic cells. Macrophages which had migrated into subendothelial space as well as epithelioid cells and multinucleated giant cells, all of which are known to be derived from monocytes, also exhibited the reaction product. The NSE granules in mesangial and endothelial cells were much smaller and fewer in number than those in monocytic cells. The present method may contribute to the more precise differentiation of monocytic cells from mesangial and endothelial cells in proliferative glomerulonephritis.
Virchows Arch B Cell Pathol Incl Mol Pathol 1984
PMID:Cellular aspects of rabbit Masugi nephritis V. Ultrastructural cytochemistry of monocytic cells. 615 4

Macrophages which are intimately involved in acute and chronic inflammatory reactions are functionally heterogeneous not only with regard to the expression of constitutive functions but also in their response to lymphokine signals. The biological basis of this heterogeneity is poorly understood. Whether we are dealing with true subpopulations or with intermediately stable phenotypes has not been resolved. To study these questions we adopted a bone marrow liquid culture system in which bone marrow cells--in the presence of a colony-stimulating factor--proliferate and differentiate into macrophages. This culture system was taken here as a model to study the expression of various functions by macrophages in the course of maturation. Several tests were performed daily and in parallel from the same batch of cells. It was found that certain functions were expressed early and were also characteristic for mature macrophages such as Fc receptors, phagocytosis of latex beads and unspecific esterase. Other functions appeared and disappeared in an ordered sequence, such as the response to macrophage migration inhibitory factor and chemotactic factor as well as the production of interferon and plasminogen activator. The time course of functional expression was strongly dependent on proliferation of precursor cells as well as on proliferation of differentiated macrophages. It is concluded that the transient phenotypic expression of functions during differentiation is the basis for the functional heterogeneity of macrophages.
Mol Immunol 1982 Oct
PMID:Heterogeneity of macrophages in response to lymphokines and other signals. 618 13

Several mouse monoclonal antibodies to carboxypeptidase A (CPA) were prepared and purified, and their interaction with the enzyme was investigated. CPA is a well-characterized zinc-containing exopeptidase exhibiting peptidase as well as esterase activity. The antibodies obtained could be classified as follows: antibodies inhibiting mainly the peptidase activity of the enzyme, antibodies inhibiting mainly its esterase activity, antibodies affecting both activities, and antibodies which bind to the enzyme but have no marked effect on its catalytic properties. Binding constants of approximately 10(6) M-1 were obtained for most of the antibody-enzyme complexes tested. Additional information on the effect of the monoclonal antibodies on the active site of CPA was obtained by determining the change in the circular dichroism spectra of arsanilazotyrosine-248 carboxypeptidase A occurring as a result of the interaction of the enzyme with the antibodies studied. These findings suggest that CPA possesses at least three different specific antigenic sites, and that the active site of the enzyme for its peptidase activity differs from that for its esterase activity, though both sites seem to overlap to a considerable extent.
Mol Immunol 1984 Jan
PMID:Interaction of carboxypeptidase A with monoclonal antibodies. 620 Jul 67

The distribution and subsequent toxicity of hazardous chemicals can be influenced by their interactions with plasma proteins. In the present study reversible binding of the phosphorothioate insecticides chlorpyrifos and parathion to fatty acid-free bovine serum albumin (BSA) was examined using the technique of equilibrium dialysis. Computer analyses of the binding data revealed that chlorpyrifos and parathion each bound reversibly to a single class of binding sites on BSA, with apparent KD values of 3.4 +/- 0.1 and 11.1 +/- 0.3 microM, respectively. Additionally, the maximal number of binding sites for each insecticide per molecule of BSA was one. Displacement studies using both chlorpyrifos and parathion indicated that each was a competitive inhibitor of the other's binding, suggesting that they were bound to the same site. Incubation of chlorpyrifos oxon or paraoxon with a 1% solution of BSA resulted in limited, EDTA-insensitive formation of 3,5,6-trichloro-2-pyridinol or p-nitrophenol, respectively. Pretreatment of BSA with 5 mM paraoxon, chlorpyrifos oxon, or 1 mM diisopropylfluorophosphate did not alter this activity, suggesting that these reactions resulted from an esterase-like capacity of BSA, and not from phosphorylation of BSA by these oxons.
Mol Pharmacol 1984 Jul
PMID:The interaction of the phosphorothioate insecticides chlorpyrifos and parathion and their oxygen analogues with bovine serum albumin. 620 48

Human pro-coagulant alpha-thrombin may be proteolyzed under controlled conditions to the non-coagulant beta- and gamma-thrombin forms. These derivative forms nonetheless retain esterase and amidase activities with small substrates as well as several other thrombin functions. Structurally, human gamma-thrombin consists of three non-covalently associated fragments which retain structural integrity as measured by several spectroscopic criteria as well as enzymatic function. The protein folding characteristics of three-chain gamma-thrombin indicate that each fragment (domain) contains sufficient information to result in a correct renaturation of protein conformation. Those subtle structural differences which distinguish gamma- from alpha-thrombin are most likely the obstructions to fibrinogen binding which account for the loss of clotting activity.
Mol Cell Biochem 1984
PMID:Structure-function relationships in human alpha- and gamma-thrombins. 632 67

Human myeloid leukemia cell lines ML-1, ML-2, ML-3, promyelocytic leukemia cell line HL-60 and histiocytic lymphoma cell line U-937 were induced to differentiate by 0.5-10 ng/ml (0.8-16 nM) 12-O-tetradecanoylphorbol-13-acetate (TPA). After 48-72 h of induction, changes of the morphology, cytochemistry and of the antigenic phenotype of induced and control cells were studied using a panel of monoclonal antibodies against granulocytic, monocytic, HLA-ABC and HLA-DR antigens in indirect immunofluorescence. Cells of the TPA-treated cultures acquired morphological, cytochemical and antigenic markers of monocytes/macrophages, as surface adherence, alpha-naphthyl acetate esterase (alpha-NE) and acid phosphatase activity and the expression of monocytic antigens detected with monoclonal antibodies 63D3, FMC 17, B 44.1, B 52.1 and anti-Mol. During differentiation in vitro induced by TPA, also loss of HLA-DR antigens and diminution of antigen of cell activation were detected with antibodies L 243 and 4F2. The expression of granulocytic antigens was only slightly diminished and the expression of HLA-ABC antigens was not changed by TPA-treatment. There were differences in the percentage of cells induced to differentiate among the lines of different origin and even among the lines ML-1, ML-2 and ML-3, established from a single patient with acute myeloid leukemia. After treatment of cultures with 5 ng/ml TPA for 72 h DNA synthesis was inhibited to 60-80%.
 ...
PMID:Differentiation of human myeloid leukemia cell lines induced by tumor-promoting phorbol ester (TPA). I. Changes of the morphology, cytochemistry and the surface differentiation antigens analyzed with monoclonal antibodies. 634 16

An arginyl esterase, identified by hydrolysis of tosyl-L-arginine-O-methyl ester (TAME), is present in estrogen-stimulated, immature rat uterine cytosol. The esterase is Ca2+-dependent and appears 3-8 h after injection of 4.5 micrograms of 17 beta-estradiol (E2). The Ca2+-independent TAME hydrolase activity in stimulated uteri decreases as the Ca2+-dependent hydrolase activity increases. The TAME hydrolase activity is not increased by dexamethasone or testosterone, nor is it elevated in liver cytosol of the same E2-treated rats. Rat plasma contains a potent Ca2+-dependent TAME hydrolase activity distinguished from the uterine enzyme by its response to high Ca2+ concentrations and its interaction with goat anti-rat serum immunoglobulin G. The uterine TAME hydrolase is apparently a trypsin-like serine protease, as defined by its pattern of inhibition, e.g. response to diisopropylfluorophosphate. The Ca2+-dependent hydrolase kinetics are complex, with an initial lag phase followed by a dramatic acceleration in the rate of hydrolysis. Both the length of the lag phase and the extent of acceleration vary with the amount of cytosol. The metal requirement is specific for Ca2+. The endogenous substrate of this newly recognized, estrogen-stimulated TAME hydrolase and its role in uterine development remain to be elucidated.
Mol Cell Endocrinol 1983 Oct
PMID:An estrogen-stimulated, calcium-dependent tosylarginine methyl ester (TAME) hydrolase in immature rat uterus. 635 93

An ultrastructural, histochemical, and biochemical study of the electric organ of the South American Torpedinid ray, Discopyge tschudii, was carried out. Fine structural cytochemical localization of acetylcholinesterase (AChE) indicated that most of the esterase was associated with the basal lamina. Electron microscopy indicated no marked differences in the electrocyte ultrastructure between Discopyge and Torpedo californica. Discopyge electric organ possessed three molecular forms, two asymmetric forms (16 S and 13 S) and one globular hydrophobic form (6.5 S). The asymmetric 16 S AChE form was solubilized by heparin, a sulfated glycosaminoglycan, suggesting that heparin-like macromolecules are involved in the binding of the enzyme to the basal lamina. Our results show that cell-free translated AChE peptides, synthesized using Discopyge electric organ poly(A+) RNA, correspond to a main band of 62,000 daltons which probably represents the catalytic subunit of the asymmetric AChE.
Cell Mol Neurobiol 1984 Jun
PMID:The electric organ of Discopyge tschudii: its innervated face and the biology of acetylcholinesterase. 648 42

We modified a binding assay using polyethylene glycol (PEG) to precipitate bound hormone. Optimum precipitation occurred when reaction mixtures were incubated with 10-40% PEG and 1.25-2.5 mg/ml gamma-globulins for 2-90 min at 4 or 23 degrees C. Results from this assay and from the dextran-coated charcoal assay were similar. Addition of phenylmethylsulfonyl fluoride eliminated nonspecific esterase activity in extracts. JH III-binding macromolecules were identified in hemolymph and ovaries of Leucophaea maderae. These molecules were pronase- and heat-sensitive and saturable. Using Scatchard analysis an average KD of 2.04 (+/- 0.32) X 10(-8) M and 1.91 (+/- 0.80) X 10(-8) M was calculated for hemolymph and ovarian binding proteins. JH III had the highest affinity for binding sites, followed by JH I and JH 0. Various extraction procedures caused changes in JH affinity for both binding proteins. At high concentrations the (+) isomer and mixed isomer preparations of methoprene and hydroprene competed for binding sites. Binding proteins had no affinity for the (-) isomer or for the JH III acid.
Mol Cell Endocrinol 1983 Aug
PMID:Assay and identification of juvenile hormone binding proteins in Leucophaea maderae. 662 33

Binding of 3H-labeled juvenile hormone (JH) to cytosol components of fat body from adult female Locusta migratoria, a tissue in which JH stimulates vitellogenin synthesis, has been characterized. Protein-bound JH is separated from unbound hormone with hydroxyapatite, which is found to provide a more sensitive and less variable assay than use of dextran-coated charcoal. By chromatography on DEAE-cellulose, three JH-binding components have been separated from cytosol. BP-I exhibited relatively stable binding with little degradation of the hormone, gave a Kd for JH-I by Scatchard analysis of 1.69 X 10(-8) M, and binding of JH-I was competed by JH-I and several synthetic JH analogs in an order corresponding to their JH activities. These characteristics suggest that BP-I may be a cytoplasmic JH receptor. BP-II, a minor component, also bound JH-I stably, but competition by analogs was not correlated with their hormone activity. BP-III caused rapid degradation of JH to JH acid and may be an esterase.
Mol Cell Endocrinol 1983 Jul
PMID:Juvenile hormone binding by components of fat body cytosol from vitellogenic locusts. 688 75


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