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1.
Front Endocrinol (Lausanne) ; 14: 1287212, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-38027158

RESUMO

Context: Surgical treatment is important for male lower urinary tract symptom (LUTS) management, but there are few reviews of the risks of reoperation. Objective: To systematically evaluate the current evidence regarding the reoperation rates of surgical treatment for LUTS in accordance with current recommendations and guidelines. Evidence acquisition: Eligible studies published up to July 2023, were searched for in the PubMed® (National Library of Medicine, Bethesda, MD, USA), Embase® (Elsevier, Amsterdam, the Netherlands), and Web of Science™ (Clarivate™, Philadelphia, PA, USA) databases. STATA® (StataCorp LP, College Station, TX, USA) software was used to conduct the meta-analysis. Random-effects models were used to calculate the pooled incidences (PIs) of reoperation and the 95% confidence intervals (CIs). Evidence synthesis: A total of 119 studies with 130,106 patients were included. The reoperation rate of transurethral resection of the prostate (TURP) at 1, 2, 3, and 5 years was 4.0%, 5.0%, 6.0%, and 7.7%, respectively. The reoperation rate of plasma kinetic loop resection of the prostate (PKRP) at 1, 2, 3, and 5 years was 3.5%, 3.6%, 5.7%, and 6.6%, respectively. The reoperation rate of holmium laser enucleation of the prostate (HoLEP) at 1, 2, 3, and 5 years was 2.4%, 3.3%, 5.4%, and 6.6%, respectively. The reoperation rate of photoselective vaporization of the prostate (PVP) at 1, 2, 3, and 5 years was 3.3%, 4.1%, 6.7%, and 7.1%, respectively. The reoperation rate of surgery with AquaBeam® at 1, 2, 3, and 5 years was 2.6%, 3.1%, 3.0%, and 4.1%, respectively. The reoperation rate of prostatic artery embolization (PAE) at 1, 2, 3, and 5 years was 12.2%, 20.0%, 26.4%, and 23.8%, respectively. The reoperation rate of transurethral microwave thermotherapy (TUMT) at 1, 2, 3, and 5 years was 9.9%, 19.9%, 23.3%, and 31.2%, respectively. The reoperation rate of transurethral incision of the prostate (TUIP) at 5 years was 13.4%. The reoperation rate of open prostatectomy (OP) at 1 and 5 years was 1.3% and 4.4%, respectively. The reoperation rate of thulium laser enucleation of the prostate (ThuLEP) at 1, 2, and 5 years was 3.7%, 7.7%, and 8.4%, respectively. Conclusion: Our results summarized the reoperation rates of 10 surgical procedures over follow-up durations of 1, 2, 3, and 5 years, which could provide reference for urologists and LUTS patients. Systematic review registration: https://www.crd.york.ac.uk/PROSPERO, identifier CRD42023445780.


Assuntos
Embolização Terapêutica , Sintomas do Trato Urinário Inferior , Hiperplasia Prostática , Ressecção Transuretral da Próstata , Estados Unidos , Humanos , Masculino , Hiperplasia Prostática/cirurgia , Ressecção Transuretral da Próstata/métodos , Próstata , Reoperação
2.
Microbiome ; 11(1): 176, 2023 08 07.
Artigo em Inglês | MEDLINE | ID: mdl-37550758

RESUMO

BACKGROUND: The high diversity and complexity of the microbial community make it a formidable challenge to identify and quantify the large number of proteins expressed in the community. Conventional metaproteomics approaches largely rely on accurate identification of the MS/MS spectra to their corresponding short peptides in the digested samples, followed by protein inference and subsequent taxonomic and functional analysis of the detected proteins. These approaches are dependent on the availability of protein sequence databases derived either from sample-specific metagenomic data or from public repositories. Due to the incompleteness and imperfections of these protein sequence databases, and the preponderance of homologous proteins expressed by different bacterial species in the community, this computational process of peptide identification and protein inference is challenging and error-prone, which hinders the comparison of metaproteomes across multiple samples. RESULTS: We developed metaSpectraST, an unsupervised and database-independent metaproteomics workflow, which quantitatively profiles and compares metaproteomics samples by clustering experimentally observed MS/MS spectra based on their spectral similarity. We applied metaSpectraST to fecal samples collected from littermates of two different mother mice right after weaning. Quantitative proteome profiles of the microbial communities of different mice were obtained without any peptide-spectrum identification and used to evaluate the overall similarity between samples and highlight any differentiating markers. Compared to the conventional database-dependent metaproteomics analysis, metaSpectraST is more successful in classifying the samples and detecting the subtle microbiome changes of mouse gut microbiomes post-weaning. metaSpectraST could also be used as a tool to select the suitable biological replicates from samples with wide inter-individual variation. CONCLUSIONS: metaSpectraST enables rapid profiling of metaproteomic samples quantitatively, without the need for constructing the protein sequence database or identification of the MS/MS spectra. It maximally preserves information contained in the experimental MS/MS spectra by clustering all of them first and thus is able to better profile the complex microbial communities and highlight their functional changes, as compared with conventional approaches. tag the videobyte in this section as ESM4 Video Abstract.


Assuntos
Microbiota , Espectrometria de Massas em Tandem , Animais , Camundongos , Fluxo de Trabalho , Proteômica , Microbiota/genética , Peptídeos
3.
Nanoscale ; 15(15): 7068-7076, 2023 Apr 13.
Artigo em Inglês | MEDLINE | ID: mdl-36974995

RESUMO

Amorphous Ga2O3 (a-Ga2O3) films have attracted considerable attention in the field of photodetectors due to their excellent optical absorption response and photoelectric properties. However, there are few studies that have utilized the piezo-phototronic effect to regulate the broadband photoresponse of Ga2O3-based photodetectors. Here, a flexible a-Ga2O3/ZnO heterojunction was constructed, which demonstrated a broadband response range from deep ultraviolet (265 nm) to the near-infrared (1060 nm) and realized a bidirectional adjustable photocurrent response via the piezo-phototronic effect. Under 265 nm illumination and 0.5 V bias, the responsivity and detectivity of the a-Ga2O3/ZnO heterojunction reached up to 12.19 A W-1 and 4.71 × 1011 Jones under 0.164% compressive strain, corresponding to enhancements of 67.7% and 66.8% compared to those under a strain-free state, respectively. Moreover, the broadband photoresponse of the a-Ga2O3/ZnO heterojunction beyond the bandgap limit was tunable under bidirectional strain. The working mechanism of photoresponse performance for the a-Ga2O3/ZnO heterojunction at different wavelengths was elucidated in detail. Oxygen vacancy-assisted carrier generation was found to be influenced by the wavelength of incident light, which mainly determined the broadband photoresponse of the heterojunction. The modulation of the a-Ga2O3/ZnO heterojunction photodetector was interpreted in light of the strain-induced regulation of the barrier height. This work represents an important step toward the development of adjustable broadband photodetectors based on a-Ga2O3 films.

4.
J Proteome Res ; 20(1): 212-221, 2021 01 01.
Artigo em Inglês | MEDLINE | ID: mdl-33253578

RESUMO

Selenocysteine is cotranslationally inserted into polypeptide chains by recoding the stop codon UGA. However, selenocysteine has also been found to be misincorporated into a small number of proteins displacing cysteines in previous studies, but such misincorporation has not yet been examined at the proteome level thoroughly. We performed label-free quantitative proteomics analysis on Escherichia coli grown in a high-selenium medium to obtain a fuller picture of selenocysteine misincorporation in its proteome. We found 139 misincorporation sites, including 54 recurred in all biological replicates, suggesting that some cysteine sites are more prone to be misincorporated than others. However, sequence and evolutionary conservation analysis showed no clear pattern among these misincorporation sites. We hypothesize that misincorporations occur randomly throughout the proteome, but the degradation rate of such misincorporated proteins varies depending on the impact of the misincorporation on protein function and stability, leading to the differential detectability of misincorporated sites by proteomics. Our hypothesis is further supported by two observations: (1) cells cultured with severely limited sulfur still retained a substantial proportion of normal cysteine counterparts of all of the found misincorporated proteins and (2) proteins involved in protein folding and proteolysis were highly upregulated in high-selenium culture.


Assuntos
Proteoma , Selenocisteína , Cisteína/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Biossíntese de Proteínas , Proteoma/genética , Proteoma/metabolismo , Proteômica , Selenocisteína/genética
5.
J Proteomics ; 210: 103541, 2020 01 06.
Artigo em Inglês | MEDLINE | ID: mdl-31614210

RESUMO

Recently it was discovered that thioproline, an unnatural analog of proline, can arise in vivo from the reaction of cysteine and formaldehyde in cells under oxidative stress. Sequence-specific bioincorporation of thioproline into proteins was studied via shotgun proteomics of Escherichia coli (E. coli) cells. In a strain auxotrophic for proline, thioproline was found widely incorporated in lieu of proline when the cells were incubated with thioproline. In total 1428 proteins and 235 distinct thioproline-containing peptides were identified. Label-free relative quantitation revealed 102 differentially expressed proteins (82 up-regulated and 20 down-regulated) in the thioproline-treated group (with thioproline in the medium) relative to the control group (with proline in the culture medium). Pathway enrichment analysis of the differentially expressed proteins showed that amino acid biosynthesis and protein synthesis has been most affected by thioproline exposure, as expected. Phenotypically, the thioproline-treated group was found to exhibit slower cell growth and stronger antioxidant capacity relative to the control. SIGNIFICANCE: Thioproline is a secondary metabolite of formaldehyde and a structural analog of proline. It is also known to exhibit a wide variety of pharmaceutical properties, but its exact biochemical role in the cell has not been elucidated. In this paper, we studied thioproline misincorporation (in lieu of proline) events during protein synthesis in E. coli. Global proteome profiling revealed that thioproline is extensively misincorporated throughout the proteome in E. coli cells exposed to thioproline, and pathways related to amino acid and protein biosynthesis are up-regulated. In addition, we demonstrated that pretreatment with thioproline appeared to increase E. coli cells' capacity to tolerate oxidative stress. Our findings suggest a novel explanation of thioproline's known antioxidative properties. This is, to our knowledge, the first ever study of thioproline misincorporation at the proteome level in any organism.


Assuntos
Antioxidantes/metabolismo , Proteínas de Escherichia coli/metabolismo , Escherichia coli/metabolismo , Estresse Oxidativo , Proteoma/metabolismo , Proteômica/métodos , Tiazolidinas/metabolismo , Aminoácidos/metabolismo , Escherichia coli/crescimento & desenvolvimento , Proteoma/análise , Tiazolidinas/química
6.
Sci Rep ; 9(1): 14337, 2019 10 04.
Artigo em Inglês | MEDLINE | ID: mdl-31586081

RESUMO

To identify clinical characteristics and mutation spectra in Chinese patients with renal angiomyolipoma (AML) associated with the tuberous sclerosis complex (TSC, TSC-AML), examined the efficacy and safety of short-term everolimus therapy (12 weeks). We analyzed the frequency distribution of each TSC-related clinical feature and investigated gene mutations by genetic testing. Some subjects received everolimus for 12 weeks at a dose of 10 mg/day, and the efficacy and safety of short-term everolimus therapy were examined. Finally, 82 TSC-AML patients were enrolled for analysis in this study. Of the 47 patients who underwent genetic testing, 22 patients (46.81%) had at least one detectable mutation in the TSC1 or TSC2 gene: 7 were TSC1 gene mutations, 13 were TSC2 gene mutations, and 2 were found in both TSC1 and TSC2. Everolimus treatment had a statistically significant effect on the renal AML volume reduction during follow-up (P < 0.05), and the mean reduction rate of volume for all cases was 56.47 ± 23.32% over 12 weeks. However, 7 patients (7/25; 28.00%) experienced an increase in renal AML tumor volume within 12 weeks after discontinuation of the everolimus treatment. Although most patients (27/30, 90.00%) experienced some adverse events during the treatment period, all such events were mild, and no patients discontinued or needed dose reduction because of adverse events. Overall, in this study, the mutation rate of TSC-AML patients is much lower than other reports. Short-term everolimus treatment for TSC-AML is effective and safe, but the stability is much lower than long-term therapy.


Assuntos
Angiomiolipoma/genética , Antineoplásicos/administração & dosagem , Everolimo/administração & dosagem , Neoplasias Renais/genética , Esclerose Tuberosa/complicações , Adolescente , Adulto , Idoso , Angiomiolipoma/tratamento farmacológico , Antineoplásicos/efeitos adversos , China , Análise Mutacional de DNA , Relação Dose-Resposta a Droga , Esquema de Medicação , Everolimo/efeitos adversos , Feminino , Humanos , Neoplasias Renais/tratamento farmacológico , Masculino , Pessoa de Meia-Idade , Taxa de Mutação , Resultado do Tratamento , Esclerose Tuberosa/genética , Carga Tumoral/efeitos dos fármacos , Adulto Jovem
7.
J Proteome Res ; 17(11): 3984-3996, 2018 11 02.
Artigo em Inglês | MEDLINE | ID: mdl-30336045

RESUMO

Bacterial persisters, a dormant and multidrug tolerant subpopulation that are able to resuscitate after antibiotic treatment, have recently received considerable attention as a major cause of relapse of various infectious diseases in the clinic. However, because of their low abundance and inherent transience, it is extremely difficult to study them by proteomics. Here we developed a magnetic-beads-based separation approach to enrich Escherichia coli persisters and then subjected them to shotgun proteomics. Rifampin pretreatment was employed to increase persister formation, and the resulting cells were exposed to a high concentration of ampicillin (10× MIC) to remove nonpersisters. The survivors were analyzed by spectral counting-based quantitative proteomics. On average, 710 proteins were identified at a false discovery rate of 0.01 for enriched E. coli persisters. By spectral counting-based quantification, 105 proteins (70 down-regulated, 35 up-regulated) were shown to be differentially expressed compared with normal cells. A comparison of the differentially expressed proteins between the magnetic beads-enriched persisters and nonenriched persisters (a mixture of persisters and intact dead cells) shows only around half (∼58%) overlap and different protein-protein interaction networks. This suggest that persister enrichment is important to eliminate the cumulative effect of dead cells that will obscure the proteome of persisters. As expected, proteins involved in carbohydrate metabolism, fatty acid and amino acid biosynthesis, and bacterial chemotaxis were found to be down-regulated in the persisters. Interestingly, membrane proteins including some transport proteins were up-regulated, indicating that they might be important for the drug tolerance of persisters. Knockout of the pal gene expressing peptidoglycan-associated lipoprotein, one of the most up-regulated proteins detected in persisters, led to 10-fold reduced persister formation under ampicillin treatment.


Assuntos
Antibacterianos/farmacologia , Farmacorresistência Bacteriana/genética , Proteínas de Escherichia coli/genética , Escherichia coli/efeitos dos fármacos , Regulação Bacteriana da Expressão Gênica , Rifampina/farmacologia , Aminoácidos/biossíntese , Ampicilina/farmacologia , Proteínas da Membrana Bacteriana Externa/genética , Proteínas da Membrana Bacteriana Externa/metabolismo , Metabolismo dos Carboidratos/genética , Proteínas de Transporte/genética , Proteínas de Transporte/metabolismo , Escherichia coli/genética , Escherichia coli/crescimento & desenvolvimento , Escherichia coli/metabolismo , Proteínas de Escherichia coli/análise , Proteínas de Escherichia coli/metabolismo , Técnicas de Inativação de Genes , Metabolismo dos Lipídeos/genética , Lipoproteínas/genética , Lipoproteínas/metabolismo , Viabilidade Microbiana , Peptidoglicano/genética , Peptidoglicano/metabolismo , Mapeamento de Interação de Proteínas , Proteômica/métodos
8.
PLoS One ; 9(6): e99077, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24901640

RESUMO

In biosynthesis of natural products, potential intermediates or analogs of a particular compound in the crude extracts are commonly overlooked in routine assays due to their low concentration, limited structural information, or because of their insignificant bio-activities. This may lead into an incomplete and even an incorrect biosynthetic pathway for the target molecule. Here we applied multiple compound mining approaches, including genome scanning and precursor ion scan-directed mass spectrometry, to identify potential pyrrolamide compounds in the fermentation culture of Streptomyces netropsis. Several novel congocidine and distamycin analogs were thus detected and characterized. A more reasonable route for the biosynthesis of pyrrolamides was proposed based on the structures of these newly discovered compounds, as well as the functional characterization of several key biosynthetic genes of pyrrolamides. Collectively, our results implied an unusual "iterative strategy" underlying the pyrrole polymerization in the biosynthesis of pyrrolamide antibiotics.


Assuntos
Amidas/metabolismo , Amidoidrolases/metabolismo , Antibacterianos/metabolismo , Polímeros/metabolismo , Pirróis/metabolismo , Streptomyces/metabolismo , Amidas/química , Antibacterianos/química , Biocatálise , Produtos Biológicos/química , Produtos Biológicos/metabolismo , Distamicinas/biossíntese , Distamicinas/química , Família Multigênica , Netropsina/biossíntese , Netropsina/química , Polímeros/química , Pirróis/química , Streptomyces/genética , Espectrometria de Massas em Tandem
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