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[PMID]:29352321
[Au] Autor:Jacobi CLJ; Stein C
[Ad] Endereço:Klinik für Anästhesiologie und operative Intensivmedizin, Campus Benjamin Franklin, Charité-Universitätsmedizin Berlin, Berlin, Germany.
[Ti] Título:Inflammatory-linked changes in CpG island methylation of three opioid peptide genes in a rat model for pain.
[So] Source:PLoS One;13(1):e0191698, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Expression of the opioid peptide genes proopiomelanocortin (Pomc), proenkephalin (Penk), and prodynorphin (Pdyn), in immune cells plays a key role in endogenous pain control. In a rat model of painful unilateral paw inflammation, we isolated cells from popliteal lymph nodes and evaluated the role of CpG island C5-methylation on the transcriptional activation of those genes. Using methylated DNA immunoprecipitation, we sorted gDNA into methylated (me) and non-me fractions and then determined the CpG island methylation status of each fraction via quantitative Real Time-PCR (qRT-PCR). In silico analysis by MethPrimer software identified one CpG island in Pdyn and three each in Pomc and Penk. No substantial changes in C5-methylation of any gene were observed. In conclusion, the CpG island methylation status does not seem to be a key regulator of opioid gene activation in immune cells during peripheral tissue inflammation.
[Mh] Termos MeSH primário: Ilhas de CpG
Metilação de DNA
Encefalinas/genética
Inflamação/genética
Dor/genética
Pró-Opiomelanocortina/genética
Precursores de Proteínas/genética
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Regulação da Expressão Gênica
Inflamação/metabolismo
Masculino
Dor/metabolismo
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enkephalins); 0 (Protein Precursors); 0 (proenkephalin); 66796-54-1 (Pro-Opiomelanocortin); 93443-35-7 (preproenkephalin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180121
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191698


  2 / 8739 MEDLINE  
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[PMID]:28859127
[Au] Autor:Zhou J; Gao S; Hsieh CL; Malla M; Shemshedini L
[Ad] Endereço:Department of Biological Sciences, University of Toledo, Toledo, Ohio, United States of America.
[Ti] Título:Peptide B targets soluble guanylyl cyclase α1 and kills prostate cancer cells.
[So] Source:PLoS One;12(8):e0184088, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Among androgen-regulated genes, soluble guanylyl cyclase α1 (sGCα1) is significant in promoting the survival and growth of prostate cancer cells and does so independent of nitric oxide (NO) signaling. Peptides were designed targeting sGCα1 to block its pro-cancer functions and one peptide is discussed here. Peptide B-8R killed both androgen-dependent and androgen-independent prostate cancer cells that expressed sGCα1, but not cells that do not express this gene. Peptide B-8R induced apoptosis of prostate cancer cells. Importantly, Peptide B-8R does not affect nor its cytotoxicity depend on NO signaling, despite the fact that it associates with sGCα1, which dimerizes with sGCß1 to form the sGC enzyme. Just as with a previously studied Peptide A-8R, Peptide B-8R induced elevated levels of reactive oxygen species (ROS) in prostate cancer cells, but using a ROS-sequestering agent showed that ROS was not responsible the cytotoxic activity of Peptide B-8R. Interestingly, Peptide B-8R induced elevated levels of p53 and phosphorylated p38, but neither of these changes is the cause of the peptide's cytotoxicity. Additional drugs were used to alter levels of iron levels in cells and these studies showed that Peptide B-8R activity does not depend on Ferroptosis. Thus, future work will be directed at defining the mechanism of cytotoxic action of Peptide B-8R against prostate cancer cells.
[Mh] Termos MeSH primário: Encefalinas/administração & dosagem
Neoplasias da Próstata/tratamento farmacológico
Neoplasias da Próstata/genética
Precursores de Proteínas/administração & dosagem
Guanilil Ciclase Solúvel/genética
[Mh] Termos MeSH secundário: Androgênios/genética
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Encefalinas/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Masculino
Óxido Nítrico/metabolismo
Proteína Oncogênica pp60(v-src)/genética
Fragmentos de Peptídeos/genética
Neoplasias da Próstata/patologia
Precursores de Proteínas/genética
Espécies Reativas de Oxigênio/metabolismo
Guanilil Ciclase Solúvel/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Androgens); 0 (Enkephalins); 0 (Peptide Fragments); 0 (Protein Precursors); 0 (Reactive Oxygen Species); 0 (peptide A); 0 (peptide B); 31C4KY9ESH (Nitric Oxide); EC 2.7.10.2 (Oncogene Protein pp60(v-src)); EC 4.6.1.2 (Soluble Guanylyl Cyclase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184088


  3 / 8739 MEDLINE  
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[PMID]:28691876
[Au] Autor:Jakab L
[Ad] Endereço:III. Belgyógyászati Klinika, Semmelweis Egyetem, Általános Orvostudományi Kar Budapest, Kútvölgyi út 4., 1125.
[Ti] Título:[Physiological, pathophysiological and clinical significance of chromogranins/secretogranins].
[Ti] Título:A kromograninok, szekretograninok élettani, kórélettani és klinikai szerepérol..
[So] Source:Orv Hetil;158(28):1092-1099, 2017 Jul.
[Is] ISSN:0030-6002
[Cp] País de publicação:Hungary
[La] Idioma:hun
[Ab] Resumo:This paper investigates the fundamental knowledge, build-up, as well as essential structural and important features of the big family of chromogranins/secretogranins. Previously the different properties and the slightly diverging funcional relations of the two family members were in focus. Later on, it has been discovered that they are essentially two similar compounds with identical structures and functions, and they are chemically, biochemically related. From details discovered so far we can tell that they are long polypeptid chains formed from amino acids. Based on insights gained until now we can also state that these compounds are formed in Ca containing environments with acidic pH. Among the compounds there are several molecules which have characteristic oligosacharid groups. This is especially interesting because oligosacharid chains with sialic acid in terminal position play an important role in the recognising and connectional processes. The chromogranins/secretogranins are mostly formed in neuroendocrine cells, but are also capable of building up in any cell type in the organism during pathological processes. Intracellular biogenesis takes place in the dense endoplasmatic reticulum across the mitochondrium, developing biogenetic granulums, followed by the stimulus-motivated secretum (exocytosis). The next stage of the molecular development is the specific break-up of the long polypeptid chains into shorter fragments. These fragments have individual effects. Some important clinical (diagnostic, prognostic) significance and connections are also touched upon in this paper, however, the cardiovascular, immunological systems and the tumors are mostly in focus. There are more immunological, cardiovascular and tumoral data. It is stated that as these molecules are in close connection with all of the organisms and systems of the body, a new chief organisator system has been identified. This chief organisator is closely connected with the central nervous system. Orv Hetil. 2017; 158(28): 1092-1099.
[Mh] Termos MeSH primário: Cromograninas/metabolismo
Encefalinas/metabolismo
Precursores de Proteínas/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromograninas/genética
Encefalinas/genética
Seres Humanos
Precursores de Proteínas/genética
Processamento de Proteína Pós-Traducional
Proteínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromogranins); 0 (Enkephalins); 0 (Protein Precursors); 0 (Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1556/650.2017.30774


  4 / 8739 MEDLINE  
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[PMID]:28635314
[Au] Autor:Stefanucci A; Lei W; Hruby VJ; Macedonio G; Luisi G; Carradori S; Streicher JM; Mollica A
[Ad] Endereço:Dipartimento di Farmacia, Università di Chieti-Pescara "G. d'Annunzio", Via dei Vestini 31, 66100 Chieti, Italy.
[Ti] Título:Fluorescent-labeled bioconjugates of the opioid peptides biphalin and DPDPE incorporating fluorescein-maleimide linkers.
[So] Source:Future Med Chem;9(9):859-869, 2017 Jun.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: The conjugation of fluorescent labels to opioid peptides is an extremely challenging task, which needs to be overcome to create new classes of probes for biological assays. MATERIALS & METHODS: Three opioid peptide analogs of biphalin and [D-Pen2,5]-Enkephalin (DPDPE) containing a fluorescein-maleimide motif were synthesized. RESULTS & DISCUSSION: The biphalin analog 17 binds to opioid receptors with K = 530 ± 90 nM and K = 69.8 ± 16.4 nM. We then tested the ability of the compounds to stimulate G-protein-coupling, 17 activated µ-receptor expressing cells (EC = 16.7 ± 6.7 nM, E = 76 ± 4%) as well as δ-receptor expressing cells (EC = 42 ± 10 nM, E = 34 ± 8%). However, 17 was not able to fluorescently label receptor in live or fixed cells. CONCLUSION: Our data suggest that the biphalin scaffold could be employed to develop fluorescent ligands with the appropriate fluorescent motif, and suggest a means for further probe development.
[Mh] Termos MeSH primário: D-Penicilina (2,5)-Encefalina/química
Encefalinas/química
Fluoresceína/química
Fluorescência
Corantes Fluorescentes/química
Maleimidas/química
[Mh] Termos MeSH secundário: Corantes Fluorescentes/síntese química
Seres Humanos
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enkephalins); 0 (Fluorescent Dyes); 0 (Maleimides); 2519R1UGP8 (maleimide); 83916-01-2 (biphalin); 88373-73-3 (Enkephalin, D-Penicillamine (2,5)-); TPY09G7XIR (Fluorescein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2016-0232


  5 / 8739 MEDLINE  
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[PMID]:28424060
[Au] Autor:Ahn S; Song TJ; Park SU; Jeon S; Kim J; Oh JY; Jang J; Hong S; Song MA; Shin HS; Jung YR; Park HJ
[Ad] Endereço:Integrative Parkinson's Disease Research Group, Acupuncture & Meridian Science Research Center, Kyung Hee University, 26 Kyungheedae-ro, Dongdaemoon-gu, Seoul, 02447, Republic of Korea.
[Ti] Título:Effects of a combination treatment of KD5040 and -dopa in a mouse model of Parkinson's disease.
[So] Source:BMC Complement Altern Med;17(1):220, 2017 Apr 19.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Although the dopamine precursor L-3, 4-dihydroxyphenylalanine ( -dopa) remains the gold standard pharmacological therapy for patients with Parkinson's disease (PD), long-term treatment with this drug has been known to result in several adverse effects, including -dopa-induced dyskinesia (LID). Recently, our group reported that KD5040, a modified herbal remedy, had neuroprotective effects in both in vitro and in vivo models of PD. Thus, the present study investigated whether KD5040 would have synergistic effects with -dopa and antidyskinetic effects caused by -dopa as well. METHODS: The effects of KD5040 and -dopa on motor function, expression levels of substance P (SP) and enkephalin (ENK) in the basal ganglia, and glutamate content in the motor cortex were assessed using behavioral assays, immunohistochemistry, Western blot analyses, and liquid chromatography tandem mass spectrometry in a mouse model of PD induced by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). In addition, the antidyskinetic effects of KD5040 on pathological movements triggered by -dopa were investigated by testing abnormal involuntary movements (AIMs) and measuring the activations of FosB, cAMP-dependent phosphor protein of 32 kDa (DARPP-32), extracellular signal-regulated kinases (ERK), and cAMP response element-binding (CREB) protein in the striatum. RESULTS: KD5040 synergistically improved the motor function when low-dose -dopa (LL) was co-administered. In addition, it significantly reversed MPTP-induced lowering of SP, improved ENK levels in the basal ganglia, and ameliorated abnormal reduction in glutamate content in the motor cortex. Furthermore, KD5040 significantly lowered AIMs and controlled abnormal levels of striatal FosB, pDARPP-32, pERK, and pCREB induced by high-dose -dopa. CONCLUSIONS: KD5040 lowered the effective dose of -dopa and alleviated LID. These findings suggest that KD5040 may be used as an adjunct therapy to enhance the efficacy of -dopa and alleviate its adverse effects in patients with PD.
[Mh] Termos MeSH primário: Encéfalo/efeitos dos fármacos
Discinesia Induzida por Medicamentos/prevenção & controle
Levodopa/uso terapêutico
Magnoliopsida
Doença de Parkinson/tratamento farmacológico
Fitoterapia
Extratos Vegetais/uso terapêutico
[Mh] Termos MeSH secundário: 1-Metil-4-Fenil-1,2,3,6-Tetra-Hidropiridina
Animais
Encéfalo/metabolismo
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
Modelos Animais de Doenças
Fosfoproteína 32 Regulada por cAMP e Dopamina/metabolismo
Discinesia Induzida por Medicamentos/etiologia
Encefalinas/metabolismo
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Levodopa/administração & dosagem
Levodopa/efeitos adversos
Levodopa/farmacologia
Masculino
Camundongos Endogâmicos C57BL
Movimento
Doença de Parkinson/metabolismo
Extratos Vegetais/farmacologia
Proteínas Proto-Oncogênicas c-fos/metabolismo
Substância P/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclic AMP Response Element-Binding Protein); 0 (Dopamine and cAMP-Regulated Phosphoprotein 32); 0 (Enkephalins); 0 (Fosb protein, mouse); 0 (Plant Extracts); 0 (Proto-Oncogene Proteins c-fos); 33507-63-0 (Substance P); 46627O600J (Levodopa); 9P21XSP91P (1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-1731-2


  6 / 8739 MEDLINE  
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[PMID]:28423013
[Au] Autor:Frederick A; Goldsmith J; de Zavalia N; Amir S
[Ad] Endereço:Centre for Studies in Behavioural Neurobiology, Concordia University, Montreal, Quebec, Canada.
[Ti] Título:Mapping the co-localization of the circadian proteins PER2 and BMAL1 with enkephalin and substance P throughout the rodent forebrain.
[So] Source:PLoS One;12(4):e0176279, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite rhythmic expression of clock genes being found throughout the central nervous system, very little is known about their function outside of the suprachiasmatic nucleus. Determining the pattern of clock gene expression across neuronal subpopulations is a key step in understanding their regulation and how they may influence the functions of various brain structures. Using immunofluorescence and confocal microscopy, we quantified the co-expression of the clock proteins BMAL1 and PER2 with two neuropeptides, Substance P (SubP) and Enkephalin (Enk), expressed in distinct neuronal populations throughout the forebrain. Regions examined included the limbic forebrain (dorsal striatum, nucleus accumbens, amygdala, stria terminalis), thalamus medial habenula of the thalamus, paraventricular nucleus and arcuate nucleus of the hypothalamus and the olfactory bulb. In most regions examined, BMAL1 was homogeneously expressed in nearly all neurons (~90%), and PER2 was expressed in a slightly lower proportion of cells. There was no specific correlation to SubP- or Enk- expressing subpopulations. The olfactory bulb was unique in that PER2 and BMAL1 were expressed in a much smaller percentage of cells, and Enk was rarely found in the same cells that expressed the clock proteins (SubP was undetectable). These results indicate that clock genes are not unique to specific cell types, and further studies will be required to determine the factors that contribute to the regulation of clock gene expression throughout the brain.
[Mh] Termos MeSH primário: Fatores de Transcrição ARNTL/genética
Relógios Circadianos/genética
Encefalinas/genética
Proteínas Circadianas Period/genética
Substância P/genética
[Mh] Termos MeSH secundário: Fatores de Transcrição ARNTL/metabolismo
Tonsila do Cerebelo/anatomia & histologia
Tonsila do Cerebelo/metabolismo
Animais
Núcleo Arqueado do Hipotálamo/anatomia & histologia
Núcleo Arqueado do Hipotálamo/metabolismo
Mapeamento Encefálico
Corpo Estriado/anatomia & histologia
Corpo Estriado/metabolismo
Encefalinas/metabolismo
Expressão Gênica
Habênula/anatomia & histologia
Habênula/metabolismo
Imuno-Histoquímica
Masculino
Núcleo Accumbens/anatomia & histologia
Núcleo Accumbens/metabolismo
Bulbo Olfatório/anatomia & histologia
Bulbo Olfatório/metabolismo
Núcleo Hipotalâmico Paraventricular/anatomia & histologia
Núcleo Hipotalâmico Paraventricular/metabolismo
Proteínas Circadianas Period/metabolismo
Ratos
Ratos Wistar
Núcleos Septais/anatomia & histologia
Núcleos Septais/metabolismo
Substância P/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARNTL Transcription Factors); 0 (Bmal1 protein, rat); 0 (Enkephalins); 0 (Per2 protein, rat); 0 (Period Circadian Proteins); 33507-63-0 (Substance P)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176279


  7 / 8739 MEDLINE  
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[PMID]:28381725
[Au] Autor:Konishi S
[Ad] Endereço:Department of Pharmacology, Kagawa School of Pharmaceutical Sciences, Tokushima Bunri University.
[Ti] Título:Pursuit of Neurotransmitter Functions: Being Attracted with Fascination of the Synapse.
[So] Source:Yakugaku Zasshi;137(4):459-475, 2017.
[Is] ISSN:1347-5231
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:In the beginning of the 1970s, only two chemical substances, acetylcholine and γ-aminobutyric acid (GABA), had been definitely established as neurotransmitters. Under such circumstances, I started my scientific career in Professor Masanori Otsuka's lab searching for the transmitter of primary sensory neurons. Until 1976, lines of evidence had accumulated indicating that the undecapeptide substance P could be released as a transmitter from primary afferent fibers into spinal synapses, although the substance P-mediated synaptic response had yet to be identified. Peripheral synapses could serve as a good model and thus, it was demonstrated in the prevertebral sympathetic ganglia by1985 that substance P released from axon collaterals of primary sensory neurons acts as the transmitter mediating non-cholinergic slow excitatory postsynaptic potential (EPSP). At that time, we also found that autonomic synapses were useful to uncover the transmitter role of the opioid peptide enkephalins, whose functions had been unknown since their discovery in 1975. Accordingly, enkephalins were found to serve a transmitter role in mediating presynaptic inhibition of cholinergic fast and non-cholinergic slow transmission in the prevertebral sympathetic ganglia. In 1990s, we attempted to devise a combined technique of brain slices and patch-clamp recordings. We applied it to study the regulatory mechanisms that operate around cerebellar GABAergic inhibitory synapses, because most of the studies then had centered on excitatory synapses and because inhibitory synapses are crucially involved in brain functions and disorders. Consequently, we discovered novel forms of heterosynaptic interactions, dual actions of a single transmitter, and receptor crosstalk, the details of which are described in this review.
[Mh] Termos MeSH primário: Neurotransmissores/fisiologia
Células Receptoras Sensoriais/fisiologia
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Axônios/metabolismo
Encefalinas/fisiologia
Potenciais Pós-Sinápticos Excitadores/fisiologia
Gânglios Simpáticos/fisiologia
Seres Humanos
Neurônios Aferentes/metabolismo
Neurônios Aferentes/fisiologia
Técnicas de Patch-Clamp
Receptor Cross-Talk/fisiologia
Medula Espinal/citologia
Substância P/metabolismo
Substância P/fisiologia
Sinapses/metabolismo
Ácido gama-Aminobutírico/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Enkephalins); 0 (Neurotransmitter Agents); 33507-63-0 (Substance P); 56-12-2 (gamma-Aminobutyric Acid)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1248/yakushi.16-00258


  8 / 8739 MEDLINE  
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[PMID]:28295336
[Au] Autor:Parker LM; Le S; Wearne TA; Hardwick K; Kumar NN; Robinson KJ; McMullan S; Goodchild AK
[Ad] Endereço:Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, NSW, 2109, Australia.
[Ti] Título:Neurochemistry of neurons in the ventrolateral medulla activated by hypotension: Are the same neurons activated by glucoprivation?
[So] Source:J Comp Neurol;525(9):2249-2264, 2017 Jun 15.
[Is] ISSN:1096-9861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Previous studies have demonstrated that a range of stimuli activate neurons, including catecholaminergic neurons, in the ventrolateral medulla. Not all catecholaminergic neurons are activated and other neurochemical content is largely unknown hence whether stimulus specific populations exist is unclear. Here we determine the neurochemistry (using in situ hybridization) of catecholaminergic and noncatecholaminergic neurons which express c-Fos immunoreactivity throughout the rostrocaudal extent of the ventrolateral medulla, in Sprague Dawley rats treated with hydralazine or saline. Distinct neuronal populations containing PPCART, PPPACAP, and PPNPY mRNAs, which were largely catecholaminergic, were activated by hydralazine but not saline. Both catecholaminergic and noncatecholaminergic neurons containing preprotachykinin and prepro-enkephalin (PPE) mRNAs were also activated, with the noncatecholaminergic population located in the rostral C1 region. Few GlyT2 neurons were activated. A subset of these data was then used to compare the neuronal populations activated by 2-deoxyglucose evoked glucoprivation (Brain Structure and Function (2015) 220:117). Hydralazine activated more neurons than 2-deoxyglucose but similar numbers of catecholaminergic neurons. Commonly activated populations expressing PPNPY and PPE mRNAs were defined. These likely include PPNPY expressing catecholaminergic neurons projecting to vasopressinergic and corticotrophin releasing factor neurons in the paraventricular nucleus, which when activated result in elevated plasma vasopressin and corticosterone. Stimulus specific neurons included noncatecholaminergic neurons and a few PPE positive catecholaminergic neuron but neurochemical codes were largely unidentified. Reasons for the lack of identification of stimulus specific neurons, readily detectable using electrophysiology in anaesthetized preparations and for which neural circuits can be defined, are discussed.
[Mh] Termos MeSH primário: Bulbo/citologia
Neuroquímica
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
[Mh] Termos MeSH secundário: Animais
Anti-Hipertensivos/farmacologia
Catecolaminas/metabolismo
Desoxiglucose/farmacologia
Encefalinas/genética
Encefalinas/metabolismo
Regulação da Expressão Gênica/efeitos dos fármacos
Proteínas da Membrana Plasmática de Transporte de Glicina/genética
Proteínas da Membrana Plasmática de Transporte de Glicina/metabolismo
Hidralazina/farmacologia
Hipotensão/metabolismo
Hipotensão/patologia
Masculino
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Neuropeptídeo Y/genética
Neuropeptídeo Y/metabolismo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Precursores de Proteínas/genética
Precursores de Proteínas/metabolismo
Proteínas Proto-Oncogênicas c-fos/genética
Proteínas Proto-Oncogênicas c-fos/metabolismo
Ratos
Ratos Sprague-Dawley
Taquicininas/genética
Taquicininas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adcyap1 protein, rat); 0 (Antihypertensive Agents); 0 (Catecholamines); 0 (Enkephalins); 0 (Glycine Plasma Membrane Transport Proteins); 0 (Nerve Tissue Proteins); 0 (Neuropeptide Y); 0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (Protein Precursors); 0 (Proto-Oncogene Proteins c-fos); 0 (Slc6a5 protein, rat); 0 (Tachykinins); 0 (cocaine- and amphetamine-regulated transcript protein); 0 (preprotachykinin); 26NAK24LS8 (Hydralazine); 93443-35-7 (preproenkephalin); 9G2MP84A8W (Deoxyglucose)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/cne.24203


  9 / 8739 MEDLINE  
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[PMID]:28284867
[Au] Autor:Rosa M; Gonzalez-Nunez V; Barreto-Valer K; Marcelo F; Sánchez-Sánchez J; Calle LP; Arévalo JC; Rodríguez RE; Jiménez-Barbero J; Arsequell G; Valencia G
[Ad] Endereço:Instituto de Química Avanzada de Cataluña (IQAC-CSIC), E-08034 Barcelona, Spain.
[Ti] Título:Role of the sugar moiety on the opioid receptor binding and conformation of a series of enkephalin neoglycopeptides.
[So] Source:Bioorg Med Chem;25(7):2260-2265, 2017 Apr 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycosylation by simple sugars is a drug discovery alternative that has been explored with varying success for enhancing the potency and bioavailability of opioid peptides. Long ago we described two O-glycosides having either ß-Glucose and ß-Galactose of (d-Met , Pro )-enkephalinamide showing one of the highest antinociceptive activities known. Here, we report the resynthesis of these two analogs and the preparation of three novel neoglycopeptide derivatives (α-Mannose, ß-Lactose and ß-Cellobiose). Binding studies to cloned zebrafish opioid receptors showed very small differences of affinity between the parent compound and the five glycopeptides thus suggesting that the nature of the carbohydrate moiety plays a minor role in determining the binding mode. Indeed, NMR conformational studies, combined with molecular mechanics calculations, indicated that all glycopeptides present the same major conformation either in solution or membrane-like environment. The evidences provided here highlight the relevance for in vivo activity of the conjugating bond between the peptide and sugar moieties in opioid glycopeptides.
[Mh] Termos MeSH primário: Carboidratos/química
Encefalinas/química
Glicopeptídeos/metabolismo
Receptores Opioides/metabolismo
[Mh] Termos MeSH secundário: Animais
Glicopeptídeos/química
Glicosilação
Espectroscopia de Ressonância Magnética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Conformação Proteica
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbohydrates); 0 (Enkephalins); 0 (Glycopeptides); 0 (Receptors, Opioid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170313
[St] Status:MEDLINE


  10 / 8739 MEDLINE  
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[PMID]:28254587
[Au] Autor:Silva RN; Oliveira LCG; Parise CB; Oliveira JR; Severino B; Corvino A; di Vaio P; Temussi PA; Caliendo G; Santagada V; Juliano L; Juliano MA
[Ad] Endereço:Department of Biophysics, Escola Paulista de Medicina, Universidade Federal de São Paulo, Brazil.
[Ti] Título:Activity of human kallikrein-related peptidase 6 (KLK6) on substrates containing sequences of basic amino acids. Is it a processing protease?
[So] Source:Biochim Biophys Acta;1865(5):558-564, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Human kallikrein 6 (KLK6) is highly expressed in the central nervous system and with elevated level in demyelinating disease. KLK6 has a very restricted specificity for arginine (R) and hydrolyses myelin basic protein, protein activator receptors and human ionotropic glutamate receptor subunits. Here we report a previously unreported activity of KLK6 on peptides containing clusters of basic amino acids, as in synthetic fluorogenic peptidyl-Arg-7-amino-4-carbamoylmethylcoumarin (peptidyl-ACC) peptides and FRET peptides in the format of Abz-peptidyl-Q-EDDnp (where Abz=ortho-aminobenzoic acid and Q-EDDnp=glutaminyl-N-(2,4-dinitrophenyl) ethylenediamine), in which pairs or sequences of basic amino acids (R or K) were introduced. Surprisingly, KLK6 hydrolyzed the fluorogenic peptides Bz-A-R R-ACC and Z-R R-MCA between the two R groups, resulting in non-fluorescent products. FRET peptides containing furin processing sequences of human MMP-14, nerve growth factor (NGF), Neurotrophin-3 (NT-3) and Neurotrophin-4 (NT-4) were cleaved by KLK6 at the same position expected by furin. Finally, KLK6 cleaved FRET peptides derived from human proenkephalin after the KR, the more frequent basic residues flanking enkephalins in human proenkephalin sequence. This result suggests the ability of KLK6 to release enkephalin from proenkephalin precursors and resembles furin a canonical processing proteolytic enzyme. Molecular models of peptides were built into the KLK6 structure and the marked preference of the cut between the two R of the examined peptides was related to the extended conformation of the substrates.
[Mh] Termos MeSH primário: Calicreínas/metabolismo
Cinética
Peptídeo Hidrolases/metabolismo
Peptídeos/química
[Mh] Termos MeSH secundário: Aminoácidos Básicos/química
Aminoácidos Básicos/genética
Encefalinas/química
Encefalinas/metabolismo
Transferência Ressonante de Energia de Fluorescência
Furina/química
Furina/metabolismo
Seres Humanos
Hidrólise
Calicreínas/química
Calicreínas/genética
Metaloproteinase 14 da Matriz/química
Metaloproteinase 14 da Matriz/metabolismo
Modelos Moleculares
Fator de Crescimento Neural/química
Fator de Crescimento Neural/metabolismo
Fatores de Crescimento Neural/química
Fatores de Crescimento Neural/metabolismo
Peptídeo Hidrolases/química
Peptídeo Hidrolases/genética
Peptídeos/metabolismo
Conformação Proteica
Precursores de Proteínas/química
Precursores de Proteínas/metabolismo
Proteólise
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids, Basic); 0 (Enkephalins); 0 (Nerve Growth Factors); 0 (Peptides); 0 (Protein Precursors); 0 (neurotrophin-3, human); 0 (proenkephalin); 9061-61-4 (Nerve Growth Factor); EC 3.4.- (Peptide Hydrolases); EC 3.4.21.- (KLK6 protein, human); EC 3.4.21.- (Kallikreins); EC 3.4.21.75 (Furin); EC 3.4.24.80 (Matrix Metalloproteinase 14); P658DCA9XD (neurotrophin 4)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171008
[Lr] Data última revisão:
171008
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE



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