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)

The Charcot-Leyden crystal (CLC) protein, a prominent cell constituent unique to eosinophils and basophils, possesses lysophospholipase activity. This activity and the extracellular deposition and formation of CLC in tissues and body fluids in association with eosinophils suggest an extracellular function for this protein in inflammation. During degranulation, basophils release granule-derived mediators of inflammation. We postulated that CLC protein, localized in part to the basophil granule, might be released along with other mediators during this process. The extracellular release of CLC protein was studied during the degranulation of basophils stimulated by anti-immunoglobulin E (anti-IgE), N-formyl-methionyl-leucyl-phenylalanine (fMLP), phorbol myristate acetate, eosinophil major basic protein (MBP), and calcium ionophore A23187. Histamine release was used as a marker of basophil degranulation; its release was measured utilizing the fluorometric technique. CLC protein was not released into the supernatant during this process as determined by radioimmunoassay. CLC protein in the extracellular space, either as intact crystals or aggregates, was undetectable by indirect immunofluorescent staining of basophils activated with either anti-IgE or fMLP. However, upon activation, the immunofluorescent cytoplasmic and nuclear staining pattern for CLC protein was significantly altered. Decreased cytoplasmic staining and persistent or increased nuclear staining for CLC protein were observed after activation, with recovery of the preactivation, unstimulated cellular staining pattern at 30 and 45 min after stimulation with fMLP and anti-IgE, respectively. These findings suggest that CLC protein functions intracellularly in basophils during the process of activation, degranulation, and recovery. The potential nuclear function(s) of this lysophospholipase in the basophil requires further investigation.
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PMID:Charcot-Leyden crystal protein in the degranulation and recovery of activated basophils. 137 30

Venom from the endoparasitic wasp Pimpla turionellae L. (Hymenoptera: Ichneumonidae) was found to contain a complex mixture of biogenic amines, noradrenalin, phospholipase B, and several proteins and peptides. The amount of noradrenalin and serotonin was found to be highest in venom from newly emerged wasps and decreased with age. Histamine was detected in minute amounts in comparison to the other venom components, and declined with increasing age of the parasitoids. Total peptides and proteins detected by reversed-phase HPLC increased with host age. Old-aged (30-33 days after emergence) wasps contained 2-fold more phospholipase B than young (<10 days [d] old) or medium-aged (10-22-d-old) females. Increases in phospholipase B alone, however, did not account for all changes in total venom protein because by 40 days after emergence, the levels of this enzyme began to decline while the amount of total protein was higher than in younger wasps. For all venom components detected, the amount present in the venom sharply decreased following host exposure. This was presumed to be the result of venom depletion associated with envenomation. Consistent with this view were the modest increases in venom components in wasps displaying a decreased rate of parasitization. When adult females were offered honey alone or in combination with feeding on hosts, no significant changes in venom composition were observed, with the exception of noradrenalin, which was found to be 5 times higher in concentration in wasps fed honey only. These results suggest that wasp age and incidence of parasitism are more important features influencing the composition of venom than the diet of adult females.
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PMID:Age and diet influence the composition of venom from the endoparasitic wasp Pimpla turionellae L. (Hymenoptera: Ichneumonidae). 1710 1