Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.5 (neuropathy target esterase)
 1,070 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Membrane-bound neuropathy target esterase (NTE) and associated phenyl valerate carboxylesterases were solubilized from chicken embryo brain by phospholipase A2. Phospholipase A2 from bee or cobra (Naja) venoms were the most effective preparations in solubilizing brain NTE and other phenyl valerate carboxylesterases. Phospholipase C and several proteinases (endoproteinase, pronase E, proteinase K, thermolysin, trypsin) did not solubilize brain membrane-bound carboxylesterases but reduced their activity. NTE solubilization by phospholipase A2 did not affect its apparent Km and Vmax for the substrate phenyl valerate or the susceptibility of phenyl valerate carboxylesterases to inhibition by paraoxon and mipafox. NTE thermal stability diminished after the treatment of brain membrane fragments with phospholipase A2.
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PMID:Solubilization of neuropathy target esterase and other phenyl valerate carboxylesterases from chicken embryonic brain by phospholipase A2. 788 4

NEST is a hydrophobic recombinant polypeptide comprising the catalytic domain (residues 727-1216) of neuropathy target esterase. NEST in bacterial lysates has potent esterase activity, which is lost after its solubilization and purification in detergent-containing solutions. Activity in purified NEST preparations was restored by the addition of phospholipids before the removal of detergent by dialysis. The pattern of digestion by proteinase K of NEST-phospholipid complexes suggested that NEST might incorporate in a topologically random fashion into nascent liposomes and that the bulk of each NEST molecule might be exposed either to the liposome lumen or the external medium. Significant quantities of NEST were liberated from NEST-phospholipid complexes by treatment with dilute acid or alkali, suggesting that charge interactions might contribute to the association; however, NEST was irreversibly denatured at these pH values. Treatment of NEST-phospholipid complexes with glutaraldehyde afforded some protection against the inactivation of esterase activity by detergent but the pattern of cross-linked forms of NEST generated did not indicate pre-existing oligomers. Similarly, the inactivation of esterase activity in NEST-phospholipid complexes by radiation indicated that NEST monomers are catalytically active. The foregoing observations are not compatible with structural algorithms predicting that the catalytic serine residue lies at the centre of one of three transmembrane helices in NEST.
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PMID:Monomers of the catalytic domain of human neuropathy target esterase are active in the presence of phospholipid. 1174 36

Adipocytes and perivascular adipose tissue are emerging as regulators of vascular function. The effects of adipocytes and perivascular adipose tissue on human smooth muscle cell (SMC) proliferation were investigated. Conditioned medium was prepared from cultured premature and differentiated 3T3-L1 adipocytes and from periaortic adipose tissue from young (3 mo) and old (24 mo) Wistar-Kyoto (WKY) rats, lean and obese Zucker rats (3 mo), and WKY rats fed normal chow or a high-fat diet for 3 mo. Conditioned medium from differentiated (but not premature) adipocytes stimulated SMC proliferation, which was abolished by charcoal and proteinase K treatment but was resistant to heat, trypsin, or phospholipase B (to hydrolyze lysophosphatidic acid). Further experiments demonstrated that the growth factor(s) are hydrosoluble and present in the fraction of molecular mass >100 kDa. Moreover, conditioned medium from periaortic adipose tissue stimulated SMC proliferation, which was significantly enhanced in aged rats and in rats fed a high-fat diet but not in obese Zucker rats deficient in functional leptin receptors. In conclusion, mature adipocytes release hydrosoluble protein growth factor(s) with a molecular mass >100 kDa for SMCs. Perivascular adipose tissue stimulates SMC proliferation, which is enhanced in aged WKY and in high-fat, diet-induced obesity but not in leptin receptor-deficient obese Zucker rats. These adipocyte-derived growth factor(s) and the effect of perivascular adipose tissue may be involved in vascular disease associated with aging and obesity.
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PMID:Mature adipocytes and perivascular adipose tissue stimulate vascular smooth muscle cell proliferation: effects of aging and obesity. 1621 8