Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The peptides H-Phe-Gly-Gly-Arg-Ile-Asp-Arg-Ile-NH2 (rANF8-15-NH2), Ac-Phe-Gly-Gly-Arg-Ile-Asp-Arg-Ile-NH2 (Ac-rANF8-15-NH2), and their corresponding retro-inverso-isomeric peptides H-D-Ile-D-Arg-D-Asp-D-Ile-D-Arg-Gly-Gly-D-Phe-NH2 (D-rANF15-8-NH2), Ac-D-Ile-D-Arg-D-Asp-D-Ile-D-Arg-Gly-Gly-D-Phe-NH2 (Ac-D-rANF15-8-NH2), were evaluated for their ability to compete for the binding of 125I-rANF5-28 to cultured spontaneously hypertensive rat (SHR) aortic smooth muscle cell membranes. Their stability toward hydrolysis by the neutral endopeptidase thermolysin was also studied. The octapeptides rANF8-15-NH2 and Ac-rANF8-15-NH2 bound with IC50's of 367 pM and 1900 pM, respectively, but were rapidly hydrolyzed by thermolysin. Retro-inverso-isomers were prepared to provide molecules with an improved enzymatic stability. The retro-inverso-isomers were completely stable to thermolysin but were virtually inactive in the binding assay (IC50 greater than 1 microM).
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PMID:Receptor binding affinity and thermolysin degradation of truncated and retro-inverso-isomeric ANF analogs. 254 Dec 91

Taking advantage of the recently demonstrated identity of common acute lymphoblastic leukemia antigen (CALLA) and neutral endopeptidase EC.24.11 (NEP) the presence of this ectoenzyme on lymphoid cells has been reassessed using highly sensitive assays (cleavage of [3H]-D-Ala2-leucine-enkephalin and binding of the inhibitor [3H]HACBO-Gly. NEP activity was found not only on already classified CALLA + ve cells but also on numerous cells (including mature B and polyclonal T cells) previously considered as CALLA-ve. This suggests that CALLA/NEP is expressed all along the differentiation pathway in B and T cell lineage. Moreover substantial ACE-like activity was also detected in three tested cells, all of the pre-B phenotype. The availability of specific inhibitors for these enzymes should help clarify their role in cell-differentiation.
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PMID:Neutral endopeptidase 24.11 and angiotensin converting enzyme like activity in CALLA positive and CALLA negative lymphoid cells. 254 97

The distributions of the neutral endopeptidase 24.11 (NEP; enkephalinase) and of mu and delta opioid receptors have been studied by autoradiography in the human spinal cord during ontogenesis, mu and delta sites were assessed by using [3H]DAGO and [3H]DTLET respectively and NEP was labelled by [3H]HACBO-Gly, a NEP inhibitor. Labelling by the three markers was found at an early stage of development of the central nervous system (14 weeks) and was mainly localized in the gray matter, with highest densities in the superficial layers of the dorsal horn. Moreover [3H]DAGO also diffusely labelled the ventral motor areas. NEP and delta binding sites were localized transiently in the fasciculus gracilis at the cervical level at a fetal age of 24 weeks, an area where no enkephalin-like immunoreactivity (ELI) has been found. Conversely no opioid binding sites or NEP were observed at a fetal age of 18 weeks in the intermediolateral region where ELI fibres and cells were detected transiently. In general, a better correlation between the distribution of NEP and that of delta opioid sites was observed. Meninges contained a very high density of [3H]HACBO-Gly sites. This labelling appeared almost simultaneously with that in the spinal cord tissue and increased with maturation. An increase in labelling by the three markers appeared slightly earlier than the clustering of ELI fibres in the substantia gelatinosa. Our data show that in the human spinal cord, structural and biochemical elements involved in enkephalinergic transmission appear almost simultaneously and early in ontogeny.
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PMID:Ontogeny of mu and delta opioid receptors and of neutral endopeptidase in human spinal cord: an autoradiographic study. 255 52

The possible changes in neutral endopeptidase EC 3.4.24.11 ("enkephalinase", NEP), mu and delta opioid binding sites, were investigated using in vitro quantitative radioautography in various regions of the central nervous system of the Freund's adjuvant-induced arthritic rat, a model of chronic pain. Enkephalinase was labeled by a specific tritiated inhibitor, [3H]N-[(2RS)-3-hydroxyaminocarbonyl-2-benzyl-1-oxopropyl]glycine ([3H]HACBO-Gly), while mu and delta opioid binding sites were selectively labelled with [3H]Tyr-D-Ala-Gly-(Me)Phe-Gly-ol ([3H]DAGO) and [3H]Tyr-D-Thr-Gly-Phe-Leu-Thr ([3H]DTLFT), respectively. As compared to controls, no significant modifications were found in NEP, mu or delta binding sites at both supraspinal and spinal levels of arthritic rats. These results suggest that the enhanced efficiency of exogenous opioids or endogenous enkephalins, reported to occur in this model of chronic inflammatory pain, are not directly related to changes in mu and delta opioid binding sites or steady state levels of NEP.
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PMID:Lack of significant changes in mu, delta opioid binding sites and neutral endopeptidase EC 3.4.24.11 in the brain and spinal cord of arthritic rats. 255 47

An endopeptidase that converts the opioid peptide dynorphin B (Tyr-Gly-Gly-Phe-Leu-Arg-aRg-Gln-Phe-Lys-Val-Val-Thr) to its bioactive fragment Leu-enkephalin-Arg6 was isolated from bovine spinal cord. The enzyme was purified about 230-fold from a concentrated spinal cord extract. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it stained as a protein of Mr 55,000. The purified enzyme is optimally active at around pH7 and has essential thiol groups. It appears to be highly specific for dynorphin B (Km = 11 microM) but not for alpha-neoendorphin or dynorphin A, two other opioids included in the prodynorphin precursor. From its specificity, molecular size, and inhibitory spectrum, this enzyme is different from other known dynorphin-converting or -degrading enzymes and appears to be a unique and novel endoprotease.
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PMID:A novel bovine spinal cord endoprotease with high specificity for dynorphin B. 256 32

The participation of a serine endopeptidase, previously shown to be involved in endogenous cholecystokinin inactivation [Rose, Camus and Schwartz (1989) Neuroscience 29, 583-594], in the hydrolysis of various exogenous cholecystokinin peptides was studied with slices from rat cerebral cortex. In order to protect intermediate fragments from further degradation and mimick experimental conditions in this previous study, most experiments were performed in the presence of Thiorphan, an enkephalinase inhibitor, and bestatin, an aminopeptidase inhibitor, which did not significantly affect the rate of cholecystokinin-8 hydrolysis. All peptide fragments formed after incubation of cholecystokinin-8, non-sulphated cholecystokinin-8, cholecystokinin-6, cholecystokinin-5, cholecystokinin-4 or Asp-Tyr-Met-Gly-Trp were identified by isocratic high-performance liquid chromatography in several systems, fluorescence spectra and/or amino acid analysis. When identified, the appearing fragments were quantified by u.v. spectrophotometry and found to fully account for the substrate disappearance. The hydrolysis rate was higher for short cholecystokinin peptides than for the octapeptide and was, in all cases, diminished by 30-50% in the presence of diisopropyl fluorophosphate, a serine peptidase inhibitor. One of the main hydrolysis products of cholecystokinin-8, or its non-sulphated analogue, was cholecystokinin-5, whose formation was impaired in the presence of diisopropyl fluorophosphate. Cholecystokinin-5 itself was apparently a substrate for a serine peptidase leading to the formation of the tripeptide Gly-Trp-Met, later cleaved into Trp-Met and Trp. Hence a serine endopeptidase(s) appears to be responsible for cleavage of the two peptides bonds of the cholecystokinin-8 molecule where the carboxyl group is donated by a methionine residue.2+n addition,
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PMID:Role of a serine endopeptidase in the hydrolysis of exogenous cholecystokinin by brain slices. 266 53

An endopeptidase specific to the Plasmodium falciparum erythrocytic schizont stage and to free merozoites was detected using the fluorogenic GlcA-Val-Leu-Gly-Lys(or Arg)-AEC substrate. The enzyme was purified by high performance liquid chromatography (HPLC); its optimal activity was around pH 7.5 and its isoelectric point was 4.4. The molecular weight of the enzyme was about 68,000, as demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. The endopeptidase was strongly inhibited by thiol proteinase inhibitors, leupeptin, and antipain. The possible involvement of this neutral endopeptidase in the reinvasion process is discussed.
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PMID:Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites. 266 80

A protease of molecular weight 29,000 was isolated and purified using ammonium sulphate precipitation, lentil lectin-Sepharose affinity chromatography and DEAE-5PW ion-exchange chromatography. The protease had an unusual amino acid composition including 5% serine, 6% proline and 20% tyrosine. It was a glycoprotein containing 12-15% carbohydrate by weight. Activity was optimal at 40-45 degrees C using [3H]-acetyl casein substrate and at 40-55 degrees C using [3H]-acetyl enamel protein substrate. It was irreversibly denatured at 80 degrees C and above. With [3H]-acetyl casein the pH optimum was 8.0-8.5 and with [3H]-acetyl enamel protein it was 6.0-8.0. There was no activity below pH 5.0, and irreversible denaturation occurred at pH 4.0 and below. No autodegradation occurred with storage at 4 degrees C for 30 days at pH 7.0. Phenylmethylsulphonyl fluoride, mercuric chloride, and p-aminobenzoic acid completely inactivated the protease. The enzyme had no requirement for calcium. The sites of cleavage of the oxidized B-chain of insulin were the Cys-Gly and Arg-Gly bonds. The enzyme was therefore an endopeptidase. Cleavage of Na-benzoyl-L-arginine ethyl ester, but not Na-benzoyl-L-tyrosine ethyl ester, suggests that the protease is of the trypsin family. On the basis of its physical and enzymic properties the protease is a serine proteinase and, consistent with existing terminology, has been named proteinase pemB.
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PMID:Purification and properties of a protease from developing porcine dental enamel. 268 9

The structure of Eubacterium nodatum cell wall peptidoglycan was investigated. The peptide subunit of E. nodatum peptidoglycan has the following structure: L-Ala-D-Glu (Gly)-L-Orn-D-Ala. The carboxyl group of alanine occupying position 4 is attached to the delta-amino group of ornithine of an other subunit by the cross-linking bridge L-Ala-L-Ala-L-Orn. All glycine molecules are connected with the alpha-carboxyl group of glutamic acid with the ratio being 0.5-1. The hydrolysis of E. nodatum peptidoglycan by the S. albus G enzyme proceeds primarily due to the activity of alanyl-alanine endopeptidase, ornithyl-ornithine endopeptidase, ornithyl-alanine endopeptidase, N-acetyl-muramyl-alanine amidase, N-acetylmuramidase and N-acetylglucosaminidase.
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PMID:Chemical composition of Eubacterium nodatum cell wall peptidoglycan. 274 51

The tripeptide Tyr-Gly-Gly (YGG), representing the product of enkephalin hydrolysis by enkephalinase (EC 3.4.24.11), was characterized and its levels measured in spinal cord perfusates of halothane-anaesthetized rats. During noxious pinching of the muzzle, which is known to trigger enkephalin release, YGG levels were enhanced more markedly and for longer than were those of [Met5]enkephalin (YGGFM), in the same samples. By contrast, neither YGG nor YGGFM levels were affected by pinching the tail. Treatment with carbaphethiol, a parenterally-active aminopeptidase inhibitor, markedly increased YGG levels and lengthened the duration of the increase produced by pinching the muzzle. Treatment with acetorphan, a parenterally-active enkephalinase inhibitor, given alone or in combination with carbaphethiol, completely prevented the rise in YGG triggered by noxious stimulation. By contrast, [Met5]enkephalin levels in the perfusates were increased by the combined administration of the two peptidase inhibitors but these levels were not further enhanced by noxious stimulation. Thus, spinal cord YGG appears to be formed under the influence of enkephalinase and to constitute a sensitive index of enkephalin release.
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PMID:Changes in levels of the tripeptide Tyr-Gly-Gly as an index of enkephalin release in the spinal cord: effects of noxious stimuli and parenterally-active peptidase inhibitors. 278 Apr 19


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