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1.
Photodiagnosis Photodyn Ther ; 35: 102349, 2021 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-34033939

RESUMO

BACKGROUND: Indocyanine green-mediated photodynamic therapy is effective against chronic periodontitis. Here, we evaluated the efficiency of indocyanine green-based adjunctive antimicrobial photodynamic therapy in non-surgical treatment of chronic periodontitis patients. METHODS: Fifty-six periodontally involved teeth of 20 patients were treated with "scaling and root planing" (control group) or "scaling and root planing with indocyanine green-based (perio-green, 0.1 mg/ml) antimicrobial photodynamic therapy" (test group) using a split-mouth design. We performed clinical assessment of probing depth, gingival recession, clinical attachment loss, and other indices, while plaque samples were collected for microbiome analysis. RESULTS: At baseline, periodontal depth and clinical attachment loss were significantly higher in the test group (p < 0.05), and at 1-month post-treatment, we observed a significant favorable reduction of both periodontal depth and clinical attachment loss in test and control sites, with lower means maintained at 3 months (p = 0.01 and p = 0.000, respectively). Additionally, analysis of variance showed significant improvements in periodontal depth and clinical attachment loss in the indocyanine green-antimicrobial photodynamic therapy group (p = 0.001), although not for clinical attachment loss in controls (p = 0.102). Moreover, a significant reduction was observed in test sites for bleeding on probing and residual pocket post-therapy (p = 0.04 and p = 0.0001 respectively). Furthermore, microbiome analysis identified Porphyromonons gingivalis, Treponema, and Tannerella in all samples with favorable changes in test sites (p = 0.07). CONCLUSION: We observed a significant reduction in periodontal clinical parameters (periodontal depth and clinical attachment loss) in chronic periodontitis patients treated with antimicrobial photodynamic therapy as an adjunctive procedure to conventional scaling and root planing. This improvement was associated with periodontal pathogen reduction and increase in the healthy subgingival microbiome.


Assuntos
Anti-Infecciosos , Periodontite Crônica , Fotoquimioterapia , Anti-Infecciosos/uso terapêutico , Periodontite Crônica/tratamento farmacológico , Raspagem Dentária , Humanos , Verde de Indocianina/uso terapêutico , Fotoquimioterapia/métodos , Fármacos Fotossensibilizantes/uso terapêutico , Aplainamento Radicular , Método Simples-Cego
2.
Int J Mol Sci ; 20(9)2019 May 09.
Artigo em Inglês | MEDLINE | ID: mdl-31075852

RESUMO

Lin-28 is an RNA-binding protein that is known for its role in promoting the pluripotency of stem cells. In the present study, Arabian camel Lin-28 (cLin-28) cDNA was identified and analyzed. Full length cLin-28 mRNA was obtained using the reverse transcription polymerase chain reaction (RT-PCR). It was shown to be 715 bp in length, and the open reading frame (ORF) encoded 205 amino acids. The molecular weight and theoretical isoelectric point (pI) of the cLin-28 protein were predicted to be 22.389 kDa and 8.50, respectively. Results from the bioinformatics analysis revealed that cLin-28 has two main domains: an N-terminal cold-shock domain (CSD) and a C-terminal pair of retroviral-type Cysteine3Histidine (CCHC) zinc fingers. Sequence similarity and phylogenetic analysis showed that the cLin-28 protein is grouped together Camelus bactrianus and Bos taurus. Quantitative real-time PCR (qPCR) analysis showed that cLin-28 mRNA is highly expressed in the lung, heart, liver, and esophageal tissues. Peptide mass fingerprint-mass spectrometry (PMF-MS) analysis of the purified cLin-28 protein confirmed the identity of this protein. Comparing the modeled 3D structure of cLin-28 protein with the available protein 3D structure of the human Lin-28 protein confirmed the presence of CSD and retroviral-type CCHC zinc fingers, and high similarities were noted between the two structures by using super secondary structure prediction.


Assuntos
Camelus/genética , Biologia Computacional/métodos , Perfilação da Expressão Gênica , Proteínas de Ligação a RNA/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Regulação da Expressão Gênica , Modelos Moleculares , Peptídeos/química , Filogenia , Estrutura Secundária de Proteína , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Proteínas de Ligação a RNA/química , Proteínas de Ligação a RNA/metabolismo
3.
Int J Mol Sci ; 18(4)2017 Mar 28.
Artigo em Inglês | MEDLINE | ID: mdl-28350354

RESUMO

Camel milk is consumed in the Middle East because of its high nutritional value. Traditional heating methods and the duration of heating affect the protein content and nutritional quality of the milk. We examined the denaturation of whey proteins in camel milk by assessing the effects of temperature on the whey protein profile at room temperature (RT), moderate heating at 63 °C, and at 98 °C, for 1 h. The qualitative and quantitative variations in the whey proteins before and after heat treatments were determined using quantitative 2D-difference in gel electrophoresis (DIGE)-mass spectrometry. Qualitative gel image analysis revealed a similar spot distribution between samples at RT and those heated at 63 °C, while the spot distribution between RT and samples heated at 98 °C differed. One hundred sixteen protein spots were determined to be significantly different (p < 0.05 and a fold change of ≥1.2) between the non-heated and heated milk samples. Eighty protein spots were decreased in common in both the heat-treated samples and an additional 25 spots were further decreased in the 98 °C sample. The proteins with decreased abundance included serum albumin, lactadherin, fibrinogen ß and γ chain, lactotransferrin, active receptor type-2A, arginase-1, glutathione peroxidase-1 and, thiopurine S, etc. Eight protein spots were increased in common to both the samples when compared to RT and included α-lactalbumin, a glycosylation-dependent cell adhesion molecule. Whey proteins present in camel milk were less affected by heating at 63 °C than at 98 °C. This experimental study showed that denaturation increased significantly as the temperature increased from 63 to 98 °C.


Assuntos
Leite/metabolismo , Proteômica/métodos , Proteínas do Soro do Leite/metabolismo , Animais , Camelus , Regulação da Expressão Gênica , Temperatura Alta , Espectrometria de Massas , Desnaturação Proteica , Proteínas do Soro do Leite/química
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