Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recently the pH gradient evoked by a K+ diffusion potential was shown to translocate a synthetic monobasic amphipathic hexapeptide across the bilayer of lipid vesicles (De Kroon, A.I.P.M., Vogt, B., Van 't Hof, R., De Kruijff, B. and De Gier, J. (1991) Biophys. J. 60, in press). Here this observation is extended by studying the effect of a membrane potential on a set of bioactive peptides. The panel of peptides comprises the toxin mastoparan X, a tryptophan-containing analogue of the presequence of the mitochondrial protein cytochrome oxidase subunit IV (preCoxIV(1-25)W18), and the regulatory peptides ACTH(1-24), alpha-MSH, ACTH(1-10), dynorphin A, bombesin, and LHRH. The interaction of these peptides with phospholipid vesicles has been measured using the intrinsic tryptophan residue as fluorescent probe. In the absence of a K+ diffusion potential only mastoparan X and the presequence show considerable binding to vesicles consisting of phosphatidylcholine (PC). In contrast, under these conditions all peptides display affinity for vesicles consisting of the acidic phospholipid cardiolipin (CL), the extent of which depends on the net positive charge of the peptide. Application of a K+ diffusion potential to large unilamellar vesicles (LUV) consisting of PC results in a time dependent tryptophan fluorescence increase for mastoparan X, which is accelerated upon incorporating increasing amounts of CL into the LUV. A similar fluorescence increase in response to a K+ diffusion potential was observed for the above model peptide. Yet the mechanism resulting in the fluorescence increase of mastoparan X is completely different from that of the hexapeptide. Binding experiments indicate that a membrane potential-induced enhanced binding of the peptide to the outer surface of the vesicles contributes to the fluorescence increase. PreCoxIV(1-25)W18, dynorphin A, and ACTH(1-24) show fluorescence responses upon applying a membrane potential that are consistent with that of mastoparan X, whereas the other peptides tested do not respond up to a LUV CL content of 50%. The results tentatively suggest that the membrane potential only affects a peptide when it has the ability to adopt a stable membrane bound conformation.
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PMID:The effect of a membrane potential on the interaction of mastoparan X, a mitochondrial presequence, and several regulatory peptides with phospholipid vesicles. 168 Mar 97

The measurement of the density of the reaction product produced by the histochemical demonstration of cytochrome oxidase activity provides a method for the visual identification of physiologically active enteric neurons. The current study utilized the cytochrome oxidase technique in order to evaluate the metabolic history of neurons in different regions of the bowel and in chemically identified types of neuron. In addition, the effect of drugs or neurotoxins commonly used in the immunocytochemical identification of enteric neuronal phenotypes was also analyzed. Cytochrome oxidase activity was visualized with a blue-black reaction product resulting from the cobalt-intensified oxidation of 3,3'-diaminobenzidine. Peptides or 5-hydroxytryptamine (5-HT) were localized with biotinylated secondary antibodies and alkaline phosphatase-labeled avidin. Bound avidin or endogenous alkaline phosphatase was visualized with a red reaction product in the presence or absence, respectively, of levamisole. Use of measured without interference from a simultaneously demonstrated histo- or immunochemical marker. A multi-peptidergic class of cholinergic submucosal secretomotor neuron containing neuropeptide Y (NPY) and calcitonin gene related peptide (CGRP) immunoreactivities was found to be less metabolically active than the average of all submucosal neurons. In contrast, a non-cholinergic submucosal secretomotor neuron containing dynorphin (which is also known to contain vasoactive intestinal peptide) immunoreactivity was more metabolically active than submucosal neurons that do not contain this peptide. On average, submucosal neurons were more metabolically active than those of the myenteric plexus, and levels of metabolic activity in the myenteric plexus were found to be higher in the duodenum and the cecum than in the jejunum-ileum or colon. Myenteric neurons characterized by CGRP or NPY immunoreactivities or by endogenous alkaline phosphatase activity, were all less metabolically active than the average of all neurons in myenteric ganglia. Colchicine, which stimulates intestinal motility, was observed to increase cytochrome oxidase activity in enteric neurons, suggesting that an effect on the enteric nervous system contributes to its action on the bowel. The neurotoxins, 6-hydroxydopamine and 5,7-dihydroxytryptamine (5,7-DHT) were each found to stimulate neuronal metabolic activity. 5,7-DHT appeared to activate excitatory subtypes of 5-HT receptor since its effects were blocked or mimicked by compounds that act as antagonists or agonists, respectively, at these receptors.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Evaluation of the activity of chemically identified enteric neurons through the histochemical demonstration of cytochrome oxidase. 170 53