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[PMID]:29329347
[Au] Autor:Torres SMF; Furrow E; Souza CP; Granick JL; de Jong EP; Griffin TJ; Wang X
[Ad] Endereço:Veterinary Clinical Sciences Department, College of Veterinary Medicine, University of Minnesota, Saint Paul, Minnesota, United States of America.
[Ti] Título:Salivary proteomics of healthy dogs: An in depth catalog.
[So] Source:PLoS One;13(1):e0191307, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To provide an in-depth catalog of the salivary proteome and endogenous peptidome of healthy dogs, evaluate proteins and peptides with antimicrobial properties, and compare the most common salivary proteins and peptides between different breed phylogeny groups. METHODS: 36 healthy dogs without evidence of periodontal disease representing four breed phylogeny groups, based upon single nucleotide polymorphism haplotypes (ancient, herding/sighthound, and two miscellaneous groups). Saliva collected from dogs was pooled by phylogeny group and analyzed using nanoscale liquid chromatography-tandem mass spectrometry. Resulting tandem mass spectra were compared to databases for identification of endogenous peptides and inferred proteins. RESULTS: 2,491 proteins and endogenous peptides were found in the saliva of healthy dogs with no periodontal disease. All dog phylogeny groups' saliva was rich in proteins and peptides with antimicrobial functions. The ancient breeds group was distinct in that it contained unique proteins and was missing many proteins and peptides present in the other groups. CONCLUSIONS AND CLINICAL RELEVANCE: Using a sophisticated nanoscale liquid chromatography-tandem mass spectrometry, we were able to identify 10-fold more salivary proteins than previously reported in dogs. Seven of the top 10 most abundant proteins or peptides serve immune functions and many more with various antimicrobial mechanisms were found. This is the most comprehensive analysis of healthy canine saliva to date, and will provide the groundwork for future studies analyzing salivary proteins and endogenous peptides in disease states.
[Mh] Termos MeSH primário: Saúde
Proteômica
Proteínas e Peptídeos Salivares/metabolismo
[Mh] Termos MeSH secundário: Animais
Cães
Feminino
Masculino
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Salivary Proteins and Peptides)
[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:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191307


  2 / 4214 MEDLINE  
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[PMID]:29283518
[Au] Autor:Ivanova VV; Milto IV; Sukhodolo IV; Serebryakova ON; Buzenkova AV
[Ti] Título:Digestive and Nondigestive Functions of Rodents' Salivary Glands.
[So] Source:Usp Fiziol Nauk;48(1):66-79, 2017 Jan-Mar.
[Is] ISSN:0301-1798
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Major salivary glands play a role not only in digestion, but also in regulation of other functions in rodents. In this review, we analyzed and summarized the data about the rodents' parotid, submandibular and sublingual salivary glands functions, which is not limited to the production of saliva and action of its hydrolytic enzymes on food in the oral cavity. In recent decades significantly expanded understanding of major salivary glands nondigestive functions. They are involved in excretion of metabolic products, maintaining fluid and electrolyte balance. Special attention has been paid to the characteristics of specific (parotin, sialorphin, etc.) and nonspecific (epidermal growth factor, nerve growth factor, kallikrein, etc.) active substances of the major salivary glands and their involvement in wound healing, mineral metabolism, regulation of hematopoiesis and immunity system. Summarized and analyzed major salivary glands endocrine function in the organs and systems. Available literature data suggest: the structure of the major salivary glands, as well as the synthesis and secretion of a number of biologically active substances are controlled by sex hormones. In turn, these biologically active factors of the salivary glands, as epidermal growth factor, and parotin, sialorphin, whose expression is regulated by androgens, have an impact on the morphological and functional state of the gonads. Thus, major salivary glands operate a wide range of functions and involved in the regulation of sexual behavior of reproductive function and maintaining homeostasis in the body.
[Mh] Termos MeSH primário: Glândula Parótida/fisiologia
Roedores/fisiologia
Proteínas e Peptídeos Salivares/metabolismo
Glândula Sublingual/fisiologia
Glândula Submandibular/fisiologia
[Mh] Termos MeSH secundário: Animais
Fator de Crescimento Epidérmico/genética
Fator de Crescimento Epidérmico/metabolismo
Regulação da Expressão Gênica
Hormônios Esteroides Gonadais/genética
Hormônios Esteroides Gonadais/metabolismo
Hematopoese/fisiologia
Imunidade Inata/efeitos dos fármacos
Calicreínas/genética
Calicreínas/metabolismo
Fator de Crescimento Neural/genética
Fator de Crescimento Neural/metabolismo
Saliva/química
Saliva/fisiologia
Proteínas e Peptídeos Salivares/genética
Proteínas e Peptídeos Salivares/farmacologia
Equilíbrio Hidroeletrolítico/fisiologia
Cicatrização/efeitos dos fármacos
Cicatrização/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Gonadal Steroid Hormones); 0 (Salivary Proteins and Peptides); 62229-50-9 (Epidermal Growth Factor); 9061-61-4 (Nerve Growth Factor); EC 3.4.21.- (Kallikreins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171229
[St] Status:MEDLINE


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[PMID]:29023574
[Au] Autor:Kammoun-Rebai W; Bahi-Jaber N; Naouar I; Toumi A; Ben Salah A; Louzir H; Meddeb-Garnaoui A
[Ad] Endereço:Laboratory of Medical Parasitology, Biotechnologies and Biomolecules, Institut Pasteur de Tunis, Tunis, Tunisia.
[Ti] Título:Human cellular and humoral immune responses to Phlebotomus papatasi salivary gland antigens in endemic areas differing in prevalence of Leishmania major infection.
[So] Source:PLoS Negl Trop Dis;11(10):e0005905, 2017 Oct.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Sand fly saliva compounds are able to elicit specific immune responses that have a significant role in Leishmania parasite establishment and disease outcome. Characterizing anti-saliva immune responses in individuals living in well defined leishmaniasis endemic areas would provide valuable insights regarding their effect on parasite transmission and establishment in humans. METHODOLOGY/PRINCIPAL FINDINGS: We explored the cellular and humoral immune responses to Phlebotomus (P.) papatasi salivary gland extracts (SGE) in individuals living in cutaneous leishmaniasis (CL) old or emerging foci (OF, EF). OF was characterized by a higher infection prevalence as assessed by higher proportions of leishmanin skin test (LST) positive individuals compared to EF. Subjects were further subdivided into healed, asymptomatic or naïve groups. We showed anti-SGE proliferation in less than 30% of the individuals, regardless of the immune status, in both foci. IFN-γ production was higher in OF and only observed in immune individuals from OF and naïve subjects from EF. Although IL-10 was not detected, addition of anti-human IL-10 antibodies revealed an increase in proliferation and IFN-γ production only in individuals from OF. The percentage of seropositive individuals was similar in immune and naïves groups but was significantly higher in OF. No correlation was observed between anti-saliva immune responses and LST response. High anti-SGE-IgG responses were associated with an increased risk of developing ZCL. No differences were observed for anti-SGE humoral or cellular responses among naïve individuals who converted or not their LST response or developed or not ZCL after the transmission season. CONCLUSIONS/SIGNIFICANCE: These data suggest that individuals living in an old focus characterized by a frequent exposure to sand fly bites and a high prevalence of infection, develop higher anti-saliva IgG responses and IFN-γ levels and a skew towards a Th2-type cellular response, probably in favor of parasite establishment, compared to those living in an emerging focus.
[Mh] Termos MeSH primário: Antígenos/imunologia
Imunidade Celular
Imunidade Humoral
Proteínas de Insetos/imunologia
Leishmaniose Cutânea/epidemiologia
Phlebotomus/imunologia
Proteínas e Peptídeos Salivares/imunologia
[Mh] Termos MeSH secundário: Adolescente
Animais
Infecções Assintomáticas/epidemiologia
Criança
Doenças Endêmicas
Feminino
Seres Humanos
Imunoglobulina G/sangue
Mordeduras e Picadas de Insetos
Interferon gama/imunologia
Interleucina-10/biossíntese
Interleucina-10/imunologia
Leishmania major/imunologia
Leishmaniose Cutânea/imunologia
Leishmaniose Cutânea/parasitologia
Leishmaniose Cutânea/transmissão
Masculino
Prevalência
Saliva/química
Saliva/imunologia
Proteínas e Peptídeos Salivares/química
Células Th2
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens); 0 (IL10 protein, human); 0 (Immunoglobulin G); 0 (Insect Proteins); 0 (Salivary Proteins and Peptides); 130068-27-8 (Interleukin-10); 82115-62-6 (Interferon-gamma)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171105
[Lr] Data última revisão:
171105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005905


  4 / 4214 MEDLINE  
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[PMID]:28914590
[Au] Autor:Gomi H; Osawa H; Uno R; Yasui T; Hosaka M; Torii S; Tsukise A
[Ad] Endereço:Department of Veterinary Anatomy, College of Bioresource Sciences, Nihon University, Fujisawa, Japan.
[Ti] Título:Canine Salivary Glands: Analysis of Rab and SNARE Protein Expression and SNARE Complex Formation With Diverse Tissue Properties.
[So] Source:J Histochem Cytochem;65(11):637-653, 2017 Nov.
[Is] ISSN:1551-5044
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The comparative structure and expression of salivary components and vesicular transport proteins in the canine major salivary glands were investigated. Histochemical analysis revealed that the morphology of the five major salivary glands-parotid, submandibular, polystomatic sublingual, monostomatic sublingual, and zygomatic glands-was greatly diverse. Immunoblot analysis revealed that expression levels of α-amylase and antimicrobial proteins, such as lysozyme, lactoperoxidase, and lactoferrin, differed among the different glands. Similarly, Rab proteins (Rab3d, Rab11a, Rab11b, Rab27a, and Rab27b) and soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) proteins VAMP4, VAMP8, syntaxin-2, syntaxin-3, syntaxin-4, and syntaxin-6 were expressed at various levels in individual glands. mmunohistochemistry of Rab3d, Rab11b, Rab27b, VAMP4, VAMP8, syntaxin-4, and syntaxin-6 revealed their predominant expression in serous acinar cells, demilunes, and ductal cells. The VAMP4/syntaxin-6 SNARE complex, which is thought to be involved in the maturation of secretory granules in the Golgi field, was found more predominantly in the monostomatic sublingual gland than in the parotid gland. These results suggest that protein expression profiles in canine salivary glands differ among individual glands and reflect the properties of their specialized functions.
[Mh] Termos MeSH primário: Proteínas de Ligação a RNA/metabolismo
Proteínas SNARE/metabolismo
Glândulas Salivares/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Cães
Imuno-Histoquímica
Imunoprecipitação
Masculino
Ligação Proteica
Proteínas e Peptídeos Salivares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA-Binding Proteins); 0 (SNARE Proteins); 0 (Salivary Proteins and Peptides)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1369/0022155417732527


  5 / 4214 MEDLINE  
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[PMID]:28837608
[Au] Autor:Mutahar M; O'Toole S; Carpenter G; Bartlett D; Andiappan M; Moazzez R
[Ad] Endereço:Mucosal and Salivary Biology, King's College London Dental Institute, London, United Kingdom.
[Ti] Título:Reduced statherin in acquired enamel pellicle on eroded teeth compared to healthy teeth in the same subjects: An in-vivo study.
[So] Source:PLoS One;12(8):e0183660, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aim of this in-vivo study was to compare total protein and four key salivary proteins present in the acquired enamel pellicle (AEP) on eroded and non-eroded surfaces in participants with erosive tooth wear. Participants with erosive tooth wear of dietary non-intrinsic origin, present on the occlusal surfaces of the lower first molars and an unaffected posterior occlusal surface in the same quadrant were recruited from restorative dental clinics at King's College London Dental Institute (n = 29, REC ref 14/EM/1171). Following removal of the salivary film, AEP samples were collected from the eroded occlusal surfaces (EP, n = 29) and the non-eroded occlusal surfaces (NP, n = 29) using 0.5% sodium dodecyl sulfate (SDS) soaked filter papers. Total protein concentration was analysed using bicinchoninic acid assay (BCA). Protein fractions were separated using SDS-PAGE and immunoblotted against: mucin5b, albumin, carbonic anhydrase VI (CA VI) and statherin antibodies. Amounts were quantified using ImageLab software against purified protein standards of known concentration. ANOVA followed by paired t-test and Wilcoxon's matched-pair signed-rank test were used to test statistical significance. The difference was considered to be significant at a P value < 0.05. The total protein on eroded surfaces was significantly lower compared to the total protein on non-eroded surfaces [0.41mg/mL (0.04) and 0.61 mg/mL (0.11)] respectively (p< 0.05). The median (min, max) amount of statherin was also significantly lower on eroded occlusal surfaces [84.1 (20.0, 221.8) ng] compared to AEP from non-eroded teeth in the same subjects [97.1(30.0, 755.6) ng] (p = 0.002). No statistical differences were observed for mucin 5b, albumin or CA VI. The total protein and statherin in the in-vivo AEP were different between eroded and non-eroded tooth surfaces of the same patient.
[Mh] Termos MeSH primário: Película Dentária/metabolismo
Proteínas e Peptídeos Salivares/metabolismo
[Mh] Termos MeSH secundário: Western Blotting
Eletroforese em Gel de Poliacrilamida
Seres Humanos
Erosão Dentária
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (STATH protein, human); 0 (Salivary Proteins and Peptides)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170825
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183660


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[PMID]:28822204
[Au] Autor:Monteon V; May-Gil I; Acosta-Viana K; Ramos-Logonio A; Hernandez O; Lopez R
[Ad] Endereço:Centro Investigaciones Biomedicas, Universidad Autonoma Campeche, Patricio Trueba s/n, Campeche 24090, Mexico
[Ti] Título:Comparative 2-D electrophoresis of salivary proteins in Triatoma dimidiata and Rhodnius prolixus (Hemiptera: Reduviidae) and major cross-reactive antigens
[So] Source:Ann Parasitol;63(2):121-125, 2017.
[Is] ISSN:2299-0631
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:An immune response to triatomine's saliva is an immunological marker of exposure to triatomine bites. However, considerable variability in salivary protein profiles did exist among species. In the present work, we compare salivary proteins from Mexican Triatoma dimidiata and Rhodnius prolixus using 2-D electrophoresis. A clear differential saliva profile was found to exist between these two triatomine species. Fewer protein spots were detected in R. prolixus than in T. dimidiata. More than half of the proteins had an isoelectric point between 5 and 7 and a molecular weight between 10 and 30 kDa in T. dimidiata. Mice exposed to T. dimidiata saliva mount an immune response to three major cross-reacting antigens in R. prolixius saliva with weights of 10 kDa and 55 kDa. Our findings may alert for the presence of cross-reacting antigens between triatomine species in regions where two or more species are overlapping in the same geographical area.
[Mh] Termos MeSH primário: Antígenos/metabolismo
Proteínas de Insetos/metabolismo
Rhodnius/metabolismo
Proteínas e Peptídeos Salivares/metabolismo
Triatoma/metabolismo
[Mh] Termos MeSH secundário: Animais
Eletroforese em Gel Bidimensional
Proteínas de Insetos/genética
Proteínas e Peptídeos Salivares/genética
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens); 0 (Insect Proteins); 0 (Salivary Proteins and Peptides)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.17420/ap6302.95


  7 / 4214 MEDLINE  
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[PMID]:28809925
[Au] Autor:Tian C; Sun X; Liu X; Huang X; Chen F; Zheng S
[Ad] Endereço:Department of Preventive Dentistry, Peking University School and Hospital of Stomatology, National Engineering Laboratory for Digital and Material Technology of Stomatology, Beijing Key Laboratory of Digital Stomatology, Beijing, PR China.
[Ti] Título:Salivary peptidome profiling analysis for occurrence of new carious lesions in patients with severe early childhood caries.
[So] Source:PLoS One;12(8):e0182712, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study aimed to identify differences of peptide profiles in stimulated whole saliva among children with and without occurrence of new carious lesions, and to provide a simple way for early diagnosis and prevention of the relapse of severe early childhood caries (s-ECC). Overall, 26 children aged 3-4 years were selected out from all the children in the kindergarten to be involved in the present study, among them 13 were diagnosed as s-ECC and underwent dental treatment, whilst the other 13 were matched by age and sex as control. Stimulated whole saliva samples were collected before treatment, and at 10 days and 4 months after treatment. During follow-up, 7 of the 13 children with s-ECC showed a relapse, and the new carious lesions were then treated. Salivary peptides were detected using the technique of magnetic beads combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Fifteen peptides showed significant differences in the group without occurrence of new carious lesions (CH group). On comparing the CH group and the other group with occurrence of new carious lesions (CR group), no significant differences were observed before treatment, whereas certain peptides showed significant differences at both 10 days and 4 months after treatment. Two peptides (experimental m/z values: 3162.0 Da and 3290.4 Da) exhibited a consistent tendency in cross-sectional and longitudinal comparisons among these groups; these may be associated with recurrence of s-ECC. Based on our findings, it is concluded that different saliva peptide peaks can be detected in s-ECC using MALDI-TOF MS combined with magnetic beads. Moreover, 2 specific peptides with m/z values 3162.0 Da and 3290.4 Da could be promising salivary protein biomarkers for diagnosis of recurrence of s-ECC.
[Mh] Termos MeSH primário: Biomarcadores/análise
Cárie Dentária/diagnóstico
Peptídeos/análise
Saliva/química
Proteínas e Peptídeos Salivares/análise
[Mh] Termos MeSH secundário: Pré-Escolar
Estudos Transversais
Cárie Dentária/metabolismo
Feminino
Seres Humanos
Estudos Longitudinais
Masculino
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Peptides); 0 (Salivary Proteins and Peptides)
[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:170816
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182712


  8 / 4214 MEDLINE  
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[PMID]:28734839
[Au] Autor:De Paula VS; Silva FHS; Francischetti IMB; Monteiro RQ; Valente AP
[Ad] Endereço:Campus Xerém, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 25245-390, Brazil; Centro de Biologia Estrutural e Bioimagem, Rio de Janeiro, 21941-920, Brazil.
[Ti] Título:Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
[So] Source:Protein Expr Purif;139:49-56, 2017 Nov.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ixolaris is an anticoagulant protein identified in the tick saliva of Ixodes scapularis. Ixolaris contains 2 Kunitz like domains and binds to Factor Xa or Factor X as a scaffold for inhibition of the Tissue Factor (TF)/Factor VIIa (FVIIa). In contrast to tissue factor pathway inhibitor (TFPI), however, Ixolaris does not bind to the active site cleft of FXa. Instead, complex formation is mediated by the FXa heparin-binding exosite. Due to its potent and long-lasting antithrombotic activity, Ixolaris is a promising agent for anticoagulant therapy. Although numerous functional studies of Ixolaris exist, three-dimensional structure of Ixolaris has not been obtained at atomic resolution. Using the pET32 vector, we successfully expressed a TRX-His -Ixolaris fusion protein. By combining Ni-NTA chromatography, enterokinase protease cleavage, and reverse phase HPLC (RP-HPLC), we purified isotopically labeled Ixolaris for NMR studies. 1D H and 2D N- H NMR analysis yielded high quality 2D N- H HSQC spectra revealing that the recombinant protein is folded. These studies represent the first steps in obtaining high-resolution structural information by NMR for Ixolaris enabling the investigation of the molecular basis for Ixolaris-coagulation factors interactions.
[Mh] Termos MeSH primário: Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Glândulas Salivares/química
Proteínas e Peptídeos Salivares/química
Proteínas e Peptídeos Salivares/genética
[Mh] Termos MeSH secundário: Anticoagulantes/química
Anticoagulantes/metabolismo
Clonagem Molecular
Escherichia coli/genética
Histidina/genética
Ressonância Magnética Nuclear Biomolecular
Oligopeptídeos/genética
Proteínas Recombinantes de Fusão/metabolismo
Proteínas e Peptídeos Salivares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticoagulants); 0 (His-His-His-His-His-His); 0 (Ixolaris protein, Ixodes scapularis); 0 (Oligopeptides); 0 (Recombinant Fusion Proteins); 0 (Salivary Proteins and Peptides); 4QD397987E (Histidine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170724
[St] Status:MEDLINE


  9 / 4214 MEDLINE  
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[PMID]:28704370
[Au] Autor:Lestinova T; Rohousova I; Sima M; de Oliveira CI; Volf P
[Ad] Endereço:Department of Parasitology, Faculty of Science, Charles University, Prague, Czech Republic.
[Ti] Título:Insights into the sand fly saliva: Blood-feeding and immune interactions between sand flies, hosts, and Leishmania.
[So] Source:PLoS Negl Trop Dis;11(7):e0005600, 2017 Jul.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Leishmaniases are parasitic diseases present worldwide that are transmitted to the vertebrate host by the bite of an infected sand fly during a blood feeding. Phlebotomine sand flies inoculate into the mammalian host Leishmania parasites embedded in promastigote secretory gel (PSG) with saliva, which is composed of a diverse group of molecules with pharmacological and immunomodulatory properties. METHODS AND FINDINGS: In this review, we focus on 3 main aspects of sand fly salivary molecules: (1) structure and composition of salivary glands, including the properties of salivary molecules related to hemostasis and blood feeding, (2) immunomodulatory properties of salivary molecules and the diverse impacts of these molecules on leishmaniasis, ranging from disease exacerbation to vaccine development, and (3) use of salivary molecules for field applications, including monitoring host exposure to sand flies and the risk of Leishmania transmission. Studies showed interesting differences between salivary proteins of Phlebotomus and Lutzomyia species, however, no data were ever published on salivary proteins of Sergentomyia species. CONCLUSIONS: In the last 15 years, numerous studies have characterized sand fly salivary proteins and, in parallel, have addressed the impact of such molecules on the biology of the host-sand fly-parasite interaction. The results obtained shall pave the way for the development of field-application tools that could contribute to the management of leishmaniasis in endemic areas.
[Mh] Termos MeSH primário: Comportamento Alimentar
Leishmania/imunologia
Psychodidae/fisiologia
Psychodidae/parasitologia
Saliva/imunologia
Saliva/parasitologia
Proteínas e Peptídeos Salivares/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas e Peptídeos Salivares/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Salivary Proteins and Peptides)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005600


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[PMID]:28699734
[Au] Autor:Harmouche N; Aisenbrey C; Porcelli F; Xia Y; Nelson SED; Chen X; Raya J; Vermeer L; Aparicio C; Veglia G; Gorr SU; Bechinger B
[Ad] Endereço:Université de Strasbourg/CNRS , UMR7177, Institut de Chimie, 1, rue Blaise Pascal, 67070 Strasbourg, France.
[Ti] Título:Solution and Solid-State Nuclear Magnetic Resonance Structural Investigations of the Antimicrobial Designer Peptide GL13K in Membranes.
[So] Source:Biochemistry;56(32):4269-4278, 2017 Aug 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The antimicrobial peptide GL13K encompasses 13 amino acid residues and has been designed and optimized from the salivary protein BPIFA2 to exhibit potent bacteriocidal and anti-biofilm activity against Gram-negative and Gram-positive bacteria as well as anti-lipopolysaccharide activity in vitro and in vivo. Here, the peptide was analyzed in a variety of membrane environments by circular dichroism spectroscopy and by high-resolution multidimensional solution nuclear magnetic resonance (NMR) spectroscopy. Whereas in the absence of membranes a random coil conformation predominates, the peptide adopts a helical structure from residue 5 to 11 in the presence of dodecylphosphocholine micelles. In contrast, a predominantly ß-sheet structure was observed in the presence of lipid bilayers carrying negatively charged phospholipids. Whereas N solid-state NMR spectra are indicative of a partial alignment of the peptide N- H vector along the membrane surface, H and P solid-state NMR spectra indicate that in this configuration the peptide exhibits pronounced disordering activities on the phospholipid membrane, which is possibly related to antimicrobial action. GL13K, thus, undergoes a number of conformational transitions, including a random coil state in solution, a helical structure upon dilution at the surface of zwitterionic membranes, and ß-sheet conformations at high peptide:lipid ratios.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/química
Ressonância Magnética Nuclear Biomolecular
Proteínas e Peptídeos Salivares/química
[Mh] Termos MeSH secundário: Seres Humanos
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (BPIFA2 protein, human); 0 (Salivary Proteins and Peptides)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00526



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