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[PMID]: 26130191 [Au] Autor: Carballo-Pacheco M; Ismail AE; Strodel B [Ad] Endereço: †AICES Graduate School and Aachener Verfahrenstechnik: Molecular Simulations and Transformations, RWTH Aachen University, Schinkelstraße 2, 52062 Aachen, Germany. [Ti] Título: Oligomer Formation of Toxic and Functional Amyloid Peptides Studied with Atomistic Simulations. [So] Source: J Phys Chem B;119(30):9696-705, 2015 Jul 30. [Is] ISSN: 1520-5207 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Amyloids are associated with diseases, including Alzheimer's, as well as functional roles such as storage of peptide hormones. It is still unclear what differences exist between aberrant and functional amyloids. However, it is known that soluble oligomers formed during amyloid aggregation are more toxic than the final fibrils. Here, we perform molecular dynamics simulations to study the aggregation of the amyloid-ß peptide Aß25-35, associated with Alzheimer's disease, and two functional amyloid-forming tachykinin peptides: kassinin and neuromedin K. Although the three peptides have similar primary sequences, tachykinin peptides, in contrast to Aß25-35, form nontoxic amyloids. Our simulations reveal that the charge of the C-terminus is essential to controlling the aggregation process. In particular, when the kassinin C-terminus is not amidated, the aggregation kinetics decreases considerably. In addition, we observe that the monomeric peptides in extended conformations aggregate faster than those in collapsed hairpin-like conformations. [Mh] Termos MeSH primário: Peptídeos beta-Amiloides/química Cassinina/química Simulação de Dinâmica Molecular Neurocinina B/química Multimerização Proteica [Mh] Termos MeSH secundário: Sequência de Aminoácidos Dados de Sequência Molecular Estrutura Secundária de Proteína [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Amyloid beta-Peptides); 63968-82-1 (Kassinin); 86933-75-7 (Neurokinin B) [Em] Mês de entrada: 1605 [Cu] Atualização por classe: 150730 [Lr] Data última revisão: 150730 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150702 [St] Status: MEDLINE [do] DOI: 10.1021/acs.jpcb.5b04822

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[PMID]: 22628076 [Au] Autor: Singh PK; Maji SK [Ad] Endereço: Department of Biosciences and Bioengineering and Wadhwani Research Centre for Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India. [Ti] Título: Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid ß-protein aggregation and toxicity. [So] Source: Cell Biochem Biophys;64(1):29-44, 2012 Sep. [Is] ISSN: 1559-0283 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Protein aggregation and amyloid formation are associated with both pathological conditions in humans such as Alzheimer's disease and native functions such as peptide hormone storage in the pituitary secretory granules in mammals. Here, we studied amyloid fibrils formation by three neuropeptides namely physalaemin, kassinin and substance P of tachykinin family using biophysical techniques including circular dichroism, thioflavin T, congo red binding and microscopy. All these neuropeptides under study have significant sequence similarity with Aß(25-35) that is known to form neurotoxic amyloids. We found that all these peptides formed amyloid-like fibrils in vitro in the presence of heparin, and these amyloids were found to be nontoxic in neuronal cells. However, the extent of amyloid formation, structural transition, and morphology were different depending on the primary sequences of peptide. When Aß(25-35) and Aß40 were incubated with each of these neuropeptides in 1:1 ratio, a drastic increase in amyloid growths were observed compared to that of individual peptides suggesting that co-aggregation of Aß and these neuropeptides. The electron micrographs of these co-aggregates were dissimilar when compared with individual peptide fibrils further supporting the possible incorporation of these neuropeptides in Aß amyloid fibrils. Further, the fibrils of these neuropeptides can seed the fibrils formation of Aß40 and reduced the toxicity of preformed Aß fibrils. The present study of amyloid formation by tachykinin neuropeptides is not only providing an understanding of the mechanism of amyloid fibril formation in general, but also offering plausible explanation that why these neuropeptide might reduce the cytotoxicity associated with Alzheimer's disease related amyloids. [Mh] Termos MeSH primário: Peptídeos beta-Amiloides/química Amiloide/química Cassinina/química Fragmentos de Peptídeos/química Fisalemina/química [Mh] Termos MeSH secundário: Algoritmos Sequência de Aminoácidos Amiloide/farmacologia Amiloide/ultraestrutura Peptídeos beta-Amiloides/ultraestrutura Linhagem Celular Tumoral Dicroísmo Circular Vermelho Congo/química Heparina/química Seres Humanos Cassinina/farmacologia Microscopia Eletrônica Neurônios/química Neurônios/efeitos dos fármacos Fragmentos de Peptídeos/ultraestrutura Fisalemina/farmacologia Ligação Proteica Estrutura Secundária de Proteína Substância P/química Substância P/farmacologia Tiazóis/química Testes de Toxicidade/métodos [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Amyloid); 0 (Amyloid beta-Peptides); 0 (Peptide Fragments); 0 (Thiazoles); 0 (amyloid beta-protein (25-35)); 2390-54-7 (thioflavin T); 2507-24-6 (Physalaemin); 33507-63-0 (Substance P); 3U05FHG59S (Congo Red); 63968-82-1 (Kassinin); 9005-49-6 (Heparin) [Em] Mês de entrada: 1212 [Cu] Atualização por classe: 131121 [Lr] Data última revisão: 131121 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 120526 [St] Status: MEDLINE [do] DOI: 10.1007/s12013-012-9364-z

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[PMID]: 19298842 [Au] Autor: Wang L; Zhou M; Lynch L; Chen T; Walker B; Shaw C [Ad] Endereço: Molecular Therapeutics Research, School of Pharmacy, Queen's University, Medical Biology Center, Belfast, Northern Ireland, UK. [Ti] Título: Kassina senegalensis skin tachykinins: molecular cloning of kassinin and (Thr2, Ile9)-kassinin biosynthetic precursor cDNAs and comparative bioactivity of mature tachykinins on the smooth muscle of rat urinary bladder. [So] Source: Biochimie;91(5):613-9, 2009 May. [Is] ISSN: 1638-6183 [Cp] País de publicação: France [La] Idioma: eng [Ab] Resumo: Tachykinins are among the most widely-studied families of regulatory peptides characterized by a highly-conserved C-terminal -Phe-X-Gly-Leu-Met.amide motif, which also constitutes the essential bioactive core. The amphibian skin has proved to be a rich source of these peptides with physalaemin from the skin of Physalaemus fuscomaculatus representing the archetypal aromatic tachykinin (X=Tyr or Phe) and kassinin from the skin of Kassina senegalensis representing the archetypal aliphatic tachykinin in which X=Val or Ile. Despite the primary structures of both mature peptides having been known for at least 30 years, neither the structures nor organizations of their biosynthetic precursors have been reported. Here we report the structure and organization of the biosynthetic precursor of kassinin deduced from cDNA cloned from a skin secretion library. In addition, a second precursor cDNA encoding the novel kassinin analog (Thr(2), Ile(9))-kassinin was identified as was the predicted mature peptide in skin secretion. Both transcripts exhibited a high degree of nucleotide sequence similarity and of open-reading frame translated amino acid sequences of putative precursor proteins. The translated preprotachykinins each consisted of 80 amino acid residues encoding single copies of either kassinin or its site-substituted analog. Synthetic replicates of each kassinin were found to be active on rat urinary bladder smooth muscle at nanomolar concentrations. The structural organization of both preprotachykinins differs from that previously reported for those of Odorrana grahami skin indicating a spectrum of diversity akin to that established for amphibian skin preprobradykinins. [Mh] Termos MeSH primário: Anuros/metabolismo Cassinina/química Cassinina/farmacologia Músculo Liso/efeitos dos fármacos Pele/metabolismo Taquicininas/farmacologia Bexiga Urinária/efeitos dos fármacos [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Sequência de Bases Clonagem Molecular DNA Complementar/genética Técnicas In Vitro Cassinina/síntese química Cassinina/genética Masculino Dados de Sequência Molecular Ratos Alinhamento de Sequência Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz Taquicininas/síntese química Taquicininas/química Taquicininas/genética [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (DNA, Complementary); 0 (Tachykinins); 63968-82-1 (Kassinin) [Em] Mês de entrada: 0906 [Cu] Atualização por classe: 141120 [Lr] Data última revisão: 141120 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 090321 [St] Status: MEDLINE [do] DOI: 10.1016/j.biochi.2009.03.003

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[PMID]: 15501529 [Au] Autor: Lippe C; Bellantuono V; Ardizzone C; Cassano G [Ad] Endereço: Dipartimento di Fisiologia Generale ed Ambientale, Università di Bari, Via Amendola 165/A, 70126 Bari, Italy. [Ti] Título: Eledoisin and Kassinin, but not Enterokassinin, stimulate ion transport in frog skin. [So] Source: Peptides;25(11):1971-5, 2004 Nov. [Is] ISSN: 0196-9781 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: In frog skin, tachykinins stimulate the ion transport, estimated by measuring the short-circuit current (SCC) value, by interacting with NK1-like receptors. In this paper we show that Kassinin (NK2 preferring in mammals) increases the SCC, while Enterokassinin has no effect. Therefore, either 2 Pro residues or 1 Pro and 1 basic amino acid must be present in the part exceeding the C-terminal pentapeptide. Eledoisin (NK3 preferring in mammals) stimulation of SCC is reduced by CP99994 and SR48968 (NK1 and NK2 antagonists) and not affected by SB222200 (NK3 antagonist). None of the three antagonists affects Kassinin stimulation of SCC. [Mh] Termos MeSH primário: Eledoisina/farmacologia Transporte de Íons/fisiologia Cassinina/farmacologia Rana esculenta/fisiologia Pele/metabolismo Taquicininas/farmacologia [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Benzamidas/farmacologia Eledoisina/metabolismo Cassinina/metabolismo Piperidinas/farmacologia Quinolinas/farmacologia Fenômenos Fisiológicos da Pele/efeitos dos fármacos Estereoisomerismo Taquicininas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Benzamides); 0 (Piperidines); 0 (Quinolines); 0 (SB 222200); 0 (Tachykinins); 136982-36-0 (3-(2-methoxybenzylamino)-2-phenylpiperidine); 63968-82-1 (Kassinin); 69-25-0 (Eledoisin); 720U2QK8I5 (SR 48968) [Em] Mês de entrada: 0504 [Cu] Atualização por classe: 161124 [Lr] Data última revisão: 161124 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 041027 [St] Status: MEDLINE

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[PMID]: 15235762 [Au] Autor: Johansson A; Liu L; Holmgren S; Burcher E [Ad] Endereço: Department of Zoophysiology, University of Göteborg, Box 463, SE-405 30, Sweden. [Ti] Título: Characterization of receptors for two Xenopus gastrointestinal tachykinin peptides in their species of origin. [So] Source: Naunyn Schmiedebergs Arch Pharmacol;370(1):35-45, 2004 Jul. [Is] ISSN: 0028-1298 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: Two tachykinin peptides, bufokinin and Xenopus neurokinin A (X-NKA) were recently isolated from Xenopus laevis. In this study we investigated the tachykinin receptors in the Xenopus gastrointestinal tract. In functional studies using stomach circular muscle strips, all peptides had similar potencies (EC50 values 1-7 nM). The rank order of potency to contract the intestine was physalaemin (EC50 1 nM)> or =bufokinin (EC50 3 nM)>substance P (SP)> or =cod SP>NKA>>X-NKA (EC50 1,900 nM). No maximum response could be obtained for [Sar9,Met(O2)11]SP, eledoisin and kassinin. In stomach strips, the mammalian tachykinin receptor antagonists RP 67580 (NK1) and MEN 10376 (NK2) had agonistic effects but did not antagonize bufokinin or X-NKA. In intestinal strips, RP 67580 (1 microM) reduced the maximal response to X-NKA but not bufokinin, while MEN 10376 was ineffective. [125I]BH-bufokinin bound with high affinity to a single class of sites, of KD 213+/-35 (stomach) and 172+/-9.3 pM (intestine). Specific binding of [125I]BH-bufokinin was displaced by bufokinin> or =SP>NKA> or =eledoisin approximately kassinin>X-NKA, indicating binding to a tachykinin NK1-like receptor. Selective tachykinin receptor antagonists were weak or ineffective. Other iodinated tachykinins ([125I]NKA and [125I]BH-eledoisin) displayed biphasic competition profiles, with the majority of sites preferring bufokinin rather than X-NKA. In conclusion, there is evidence for two different tachykinin receptors in Xenopus gastrointestinal tract. Both receptors may exist in stomach, whereas the bufokinin-preferring NK1-like receptor predominates in longitudinal muscle of the small intestine. Antagonists appear to interact differently with amphibian receptors, compared with mammalian receptors. [Mh] Termos MeSH primário: Neurocinina A/análogos & derivados Fisalemina/análogos & derivados Receptores de Taquicininas/química Receptores de Taquicininas/efeitos dos fármacos Especificidade da Espécie Substância P/análogos & derivados Xenopus/metabolismo [Mh] Termos MeSH secundário: Animais Sítios de Ligação/efeitos dos fármacos Cárdia/citologia Cárdia/efeitos dos fármacos Cárdia/metabolismo Relação Dose-Resposta a Droga Eledoisina/farmacologia Feminino Indóis/farmacologia Peptídeos e Proteínas de Sinalização Intercelular/química Peptídeos e Proteínas de Sinalização Intercelular/farmacologia Intestino Delgado/citologia Intestino Delgado/efeitos dos fármacos Intestino Delgado/metabolismo Radioisótopos do Iodo Isoindóis Cassinina/farmacologia Masculino Contração Muscular/efeitos dos fármacos Contração Muscular/fisiologia Músculo Liso/efeitos dos fármacos Músculo Liso/fisiologia Neurocinina A/antagonistas & inibidores Neurocinina A/química Neurocinina A/farmacologia Fragmentos de Peptídeos/farmacologia Fisalemina/farmacologia Receptores de Taquicininas/fisiologia Substância P/farmacologia [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Indoles); 0 (Intercellular Signaling Peptides and Proteins); 0 (Iodine Radioisotopes); 0 (Isoindoles); 0 (Peptide Fragments); 0 (Receptors, Tachykinin); 0 (bufokinin); 110880-55-2 (substance P, Sar(9)-Met(O2)(11)-); 129623-01-4 (GR 82334); 135306-85-3 (neurokinin A(4-10), Tyr(5)-Trp(6,8,9)-Lys(10)-); 135911-02-3 (7,7-diphenyl-2-(1-imino-2-(2-methoxyphenyl)ethyl)perhydroisoindol-4-one); 2507-24-6 (Physalaemin); 33507-63-0 (Substance P); 63968-82-1 (Kassinin); 69-25-0 (Eledoisin); 86933-74-6 (Neurokinin A) [Em] Mês de entrada: 0506 [Cu] Atualização por classe: 170920 [Lr] Data última revisão: 170920 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 040706 [St] Status: MEDLINE

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[PMID]: 11679016 [Au] Autor: Tucci P; Bolle P; Severini C [Ad] Endereço: Dipartimento di Farmacologia delle Sostanze Naturali e Fisiologia Generale, University of Rome 'La Sapienza', Ple Aldo Moro 5, 00185 Rome, Italy. [Ti] Título: Effects of natural tachykinins on ovine lower urinary tract smooth muscle. [So] Source: J Auton Pharmacol;21(2):79-84, 2001 Apr. [Is] ISSN: 0144-1795 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: 1. Numerous studies have demonstrated that the urinary bladder is particularly sensitive to tachykinins; rat, rabbit and guinea pig bladders, besides human detrusor, have been the most extensively studied, whereas very little is known about most large animal detrusors. The aim of this work was to study natural tachykinin activity on the lower urinary tract of ovine to make a comparison with data obtained in laboratory animals. 2. As in other animal species, tachykinins are also able to contract ovine bladder smooth muscle. 3. The results reported in this study indicate that in ovine bladder, neurokinin 2 (NK2) receptors are expressed most. In fact, on lamb and sheep bladder neurokinin A (NKA), a NK2- almost selective peptide, was shown to be > 100% more active than the natural tachykinins kassinin (KASS) and eledoisin (ELED). Eledoisin was shown to be 50% less active than KASS, which is typical behaviour for an almost exclusively NK2 receptor population. Moreover, NK1- preferential peptides, namely substance P (SP) and physalaemin (PHYS), showed a lack of activity even when applied at high concentrations. 4. The results reported in this study show that lamb and sheep detrusor represent a good alternative model for the characterization of NK2-selective tachykinins. [Mh] Termos MeSH primário: Músculo Liso/efeitos dos fármacos Taquicininas/metabolismo Sistema Urinário/efeitos dos fármacos [Mh] Termos MeSH secundário: Animais Eledoisina/farmacologia Feminino Cobaias Técnicas In Vitro Cassinina/farmacologia Masculino Neurocinina A/farmacologia Peptídeos Cíclicos/farmacologia Receptores da Neurocinina-2/efeitos dos fármacos Ovinos Substância P/farmacologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Peptides, Cyclic); 0 (Receptors, Neurokinin-2); 0 (Tachykinins); 157351-81-0 (MEN 10627); 33507-63-0 (Substance P); 63968-82-1 (Kassinin); 69-25-0 (Eledoisin); 86933-74-6 (Neurokinin A) [Em] Mês de entrada: 0201 [Cu] Atualização por classe: 141120 [Lr] Data última revisão: 141120 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 011027 [St] Status: MEDLINE

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[PMID]: 11575875 [Au] Autor: Higa K; Gao C; Motokawa W; Abe K [Ad] Endereço: Department of Pediatric Dentistry, Fukuoka Dental College, Japan. [Ti] Título: The roles of the N-terminal portions of various tachykinins in promoting salivation. [So] Source: Oral Dis;7(4):238-45, 2001 Jul. [Is] ISSN: 1354-523X [Cp] País de publicação: Denmark [La] Idioma: eng [Ab] Resumo: OBJECTIVES: In order to determine the active sites for salivation of various tachykinins, the regulatory roles of the N-terminal portion of various newly-synthesized tachykinins were studied after i.p. injection of rats using the submandibular glands as model organs. METHODS: N-shortened oligopeptides from kassinin, eledoisin, neurokinins A (NKA) and NKB were synthesized by the multipin peptide synthesis method. Amino acids were eliminated one by one to form octa- to undeca-peptides adjoining the inactive or less active heptapeptides and various heptapeptides, in which an amino acid in position 8 (Xaa8), numbering as in an undecapeptide, was replaced with Tyr, Phe, Ile or Val. RESULTS: The N-terminal amino acids in positions 1 to 4 could be activators or inhibitors, depending on whether the C-terminal heptapeptide was inactive or less active. The Xaa8 residue, in combination with amino acids in positions 5 and 6, seemed to be very important in determining the sialogogic activity of a heptapeptide. The discrimination between NKA and NKB appeared due to the N-terminal amino acid sequence in positions I to 4 including Phe or Ser in position 6. CONCLUSIONS: It is concluded that the N-terminal amino acids in positions I to 4 serve as either activators or inhibitors depending upon the sialogogic activity of the C-terminal heptapeptide, in which particular amino acids in positions 5, 6 and 8 regulate its activity. [Mh] Termos MeSH primário: Salivação/efeitos dos fármacos Glândula Submandibular/efeitos dos fármacos Taquicininas/farmacologia [Mh] Termos MeSH secundário: Análise de Variância Animais Eledoisina/farmacologia Injeções Intraperitoneais Isoleucina/farmacologia Cassinina/farmacologia Masculino Modelos Animais Neurocinina A/farmacologia Neurocinina B/farmacologia Fenilalanina/farmacologia Ratos Ratos Sprague-Dawley Serina/farmacologia Estatística como Assunto Glândula Submandibular/secreção Taquicininas/administração & dosagem Tirosina/farmacologia Valina/farmacologia [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Tachykinins); 04Y7590D77 (Isoleucine); 42HK56048U (Tyrosine); 452VLY9402 (Serine); 47E5O17Y3R (Phenylalanine); 63968-82-1 (Kassinin); 69-25-0 (Eledoisin); 86933-74-6 (Neurokinin A); 86933-75-7 (Neurokinin B); HG18B9YRS7 (Valine) [Em] Mês de entrada: 0111 [Cu] Atualização por classe: 131121 [Lr] Data última revisão: 131121 [Sb] Subgrupo de revista: D [Da] Data de entrada para processamento: 010929 [St] Status: MEDLINE

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[PMID]: 11245256 [Au] Autor: Grace RC; Lynn AM; Cowsik SM [Ad] Endereço: Department of Physics, Indian Institute of Science, Bangalore. [Ti] Título: Lipid induced conformation of the tachykinin peptide Kassinin. [So] Source: J Biomol Struct Dyn;18(4):611-21, 623-5, 2001 Feb. [Is] ISSN: 0739-1102 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Both the aqueous and lipid-induced structure of Kassinin, a dodecapeptide of amphibian origin, has been studied by two-dimensional proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy and distance geometry calculations. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The distance constraints obtained from the NMR data have been utilized in a distance geometry algorithm to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that, while in water Kassinin prefers to be in an extended chain conformation, in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system, helical conformation is induced in the central core and C-terminal region (K4-M12) of the peptide. N-terminus though less defined also displays some degree of order and a possible turn structure. The conformation adopted by Kassinin in the presence of DPC micelles is consistent with the structural motif typical of neurokinin-1 selective agonists and with that reported for Eledoisin in hydrophobic environment. [Mh] Termos MeSH primário: Cassinina/química Modelos Moleculares Fosforilcolina/análogos & derivados Fosforilcolina/química [Mh] Termos MeSH secundário: Dicroísmo Circular Cassinina/metabolismo Espectroscopia de Ressonância Magnética Fosforilcolina/metabolismo Conformação Proteica Água [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 059QF0KO0R (Water); 107-73-3 (Phosphorylcholine); 53949-18-1 (dodecylphosphocholine); 63968-82-1 (Kassinin) [Em] Mês de entrada: 0106 [Cu] Atualização por classe: 131121 [Lr] Data última revisão: 131121 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 010314 [St] Status: MEDLINE

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[PMID]: 10502070 [Au] Autor: Jenkinson KM; Morgan JM; Furness JB; Southwell BR [Ad] Endereço: Department of Anatomy and Cell Biology, University of Melbourne, Parkville, Victoria 3052, Australia, k.Jenkinson@anatomy.unimelb.edu.au [Ti] Título: Neurons bearing NK(3) tachykinin receptors in the guinea-pig ileum revealed by specific binding of fluorescently labelled agonists. [So] Source: Histochem Cell Biol;112(3):233-46, 1999 Sep. [Is] ISSN: 0948-6143 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: The localisation of NK(3) tachykinin receptors in guinea-pig ileum was studied using the fluorescently labelled agonists, Cy3. 5-neurokinin A and Cy3.5-kassinin. Binding to nerve cell bodies in the myenteric and submucosal plexuses was visualised using confocal microscopy. Binding to NK(1) receptors was blocked by the NK(1) receptor antagonist, CP-99994. NK(3) receptors, demonstrated by binding in the presence of CP-99994, occurred in 72% of myenteric and 38% of submucosal neurons. Colocalisation with other markers was examined to deduce the classes of neurons with NK(3) receptors. In myenteric ganglia, NK(3) receptors were present on the following: 73% of calbindin-immunoreactive (IR) intrinsic primary afferent neurons, 63% of calretinin-IR excitatory motor neurons and ascending interneurons, 63% of nitric oxide synthase-IR inhibitory motor neurons and descending interneurons, 79% of strongly neuropeptide Y (NPY)-IR secretomotor neurons, 67% of weakly NPY-IR descending interneurons and motor neurons, and 46% of NK(1) receptor-IR neurons. In submucosal ganglia, NK(3) receptors were on 65% of calretinin-IR secretomotor/vasodilator neurons, 81% of NPY-IR cholinergic secretomotor neurons, 2% of vasoactive intestinal peptide-IR non-cholinergic secretomotor neurons and were completely absent from substance P-IR intrinsic primary afferent neurons. The results support physiological studies suggesting that NK(3) receptors mediate tachykinin transmission between myenteric sensory neurons and to interneurons and/or motor neurons in descending inhibitory and ascending excitatory pathways. [Mh] Termos MeSH primário: Íleo/metabolismo Cassinina/metabolismo Neurocinina A/metabolismo Neurônios/metabolismo Receptores da Neurocinina-3/metabolismo [Mh] Termos MeSH secundário: Animais Carbocianinas/química Contagem de Células Feminino Corantes Fluorescentes/química Cobaias Técnicas In Vitro Cassinina/química Masculino Microscopia Confocal Plexo Mientérico/citologia Plexo Mientérico/metabolismo Neurocinina A/química Neurônios/citologia Piperidinas/farmacologia Receptores da Neurocinina-3/antagonistas & inibidores Plexo Submucoso/citologia Plexo Submucoso/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Carbocyanines); 0 (Fluorescent Dyes); 0 (Piperidines); 0 (Receptors, Neurokinin-3); 0 (SR 142801); 0 (cyanine dye 3); 136982-36-0 (3-(2-methoxybenzylamino)-2-phenylpiperidine); 63968-82-1 (Kassinin); 86933-74-6 (Neurokinin A) [Em] Mês de entrada: 9911 [Cu] Atualização por classe: 141120 [Lr] Data última revisão: 141120 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 990929 [St] Status: MEDLINE

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MEDLINE

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[PMID]: 9694566 [Au] Autor: Malendowicz LK [Ad] Endereço: Department of Histology and Embryology, School of Medicine, Poznan, Poland. [Ti] Título: Role of neuromedins in the regulation of adrenocortical function. [So] Source: Horm Metab Res;30(6-7):374-83, 1998 Jun-Jul. [Is] ISSN: 0018-5043 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: Neuromedins, smooth-muscle-stimulating peptides, are commonly divided into four groups: bombesin-like, kassinin-like, neurotensin-like and neuromedins U. In the present review, current data on the synthesis and mechanism of action of neuromedins on hypothalamo-pituitary-adrenal (HPA) axis will be presented. These neuropeptides and their receptors are localized to all components of the HPA axis, the only exemption seems to be neurokinin B, which is not detected in the adenohypophysis. Neuromedins exert a manifold effect on HPA axis, and their action on the adrenal suggests their involvement in the regulation of growth, structure and function of the adrenal cortex. Neuromedins may exert both direct and indirect effects on the adrenal cortex. Direct effect is proven by the stimulation of mineralo- and glucocorticoid output by isolated or cultured adrenocortical cells and by mobilisation of intracellular [Ca2+]i. Indirect effects, on the other hand, may be mediated by ACTH, arginine-vasopressin, angiotensin II, catecholamines or by other regulatory substances of medullary origin. [Mh] Termos MeSH primário: Córtex Suprarrenal/fisiologia Neuropeptídeos/farmacologia [Mh] Termos MeSH secundário: Córtex Suprarrenal/efeitos dos fármacos Sequência de Aminoácidos Animais Bombesina/genética Bombesina/farmacologia Seres Humanos Cassinina/genética Cassinina/farmacologia Dados de Sequência Molecular Neuropeptídeos/genética Neurotensina/genética Neurotensina/farmacologia [Pt] Tipo de publicação: JOURNAL ARTICLE; REVIEW [Nm] Nome de substância: 0 (Neuropeptides); 117505-80-3 (neuromedin U); 39379-15-2 (Neurotensin); 63968-82-1 (Kassinin); PX9AZU7QPK (Bombesin) [Em] Mês de entrada: 9810 [Cu] Atualização por classe: 131121 [Lr] Data última revisão: 131121 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 980807 [St] Status: MEDLINE

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