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1.
Arch. esp. urol. (Ed. impr.) ; 76(8): 555-562, 28 oct. 2023. tab, graf
Artigo em Inglês | IBECS | ID: ibc-227317

RESUMO

Objective: To explore the prognostic value of combined detection of serum prostate specific antigen (PSA), lung cancer metastasis-associated transcript 1 (MALAT1), transmembrane serine protease 2 (TMPRSS2), and erythropoietin-specific transforming gene variant 1 (ETV1) in prostate cancer. Methods: Ninety patients with prostate cancer who were treated in hospital were divided into two groups according to tumor node metastasis stage: Stage I−II group (n = 34) and stage III−IV group (n = 56). The serum levels of PSA, MALAT1, and TMPRSS2-ETV1 were detected in both groups and correlated with prostate cancer status to determine their value as indicators of disease progression and prognosis. Results: Age, body mass index (BMI), and Gleason score differed significantly between the study group and the control group (p < 0.05). The expression levels of serum PSA and MALAT1 were higher in group III–IV than in group I–II, and the positive expression rate of TMPRSS2-ETV1 was significantly higher in group III–IV than in the control group (p < 0.05). Pearson’s correlation analysis showed that serum PSA, MALAT1, and TMPRSS2-ETV1 were significantly correlated with prostate cancer (p < 0.05). Differences in PSA levels correlated with differences in age, BMI, type of pathology, and Gleason score, whereas differences in serum MALAT1 levels correlated with differences in age, BMI, and type of pathology. Gleason scores differed significantly between patients with positive and negative TMPRSS2-ETV1 indicators (p < 0.05). Multivariate logistic regression analysis showed that serum PSA, MALAT1, and TMPRSS2-ETV1 were independent risk factors affecting the prognosis of prostate cancer (p < 0.05). The areas under the curve (AUCs) of serum PSA, MALAT1, and TMPRSS2-ETV1 as prognostic predictors in prostate cancer were 0.692, 0.731, and 0.709, respectively, whereas the AUC of the combination was 0.819 (AU)


Assuntos
Humanos , Masculino , Feminino , Idoso , Idoso de 80 Anos ou mais , Antígeno Prostático Específico/sangue , Serina Proteases/sangue , Neoplasias da Próstata/sangue , Neoplasias da Próstata/mortalidade , Biomarcadores Tumorais/sangue , Progressão da Doença , Prognóstico , Estadiamento de Neoplasias
2.
Clin. transl. oncol. (Print) ; 24(6): 1124-1133, junio 2022.
Artigo em Inglês | IBECS | ID: ibc-203811

RESUMO

ObjectiveslncRNA ABHD11 antisense RNA 1 (ABHD11-AS1) acts as an oncogene involved in papillary thyroid carcinoma (PTC) occurrence and progression. ABHD11-AS1 exerts biologic functions by some miRNAs and proteins to regulate multiple targets. Identification of novel mechanism of ABHD11‐AS1 could be helpful in therapeutic targeting for PTC treatment.MethodsDifferentially expressed lncRNAs were selected from TCGA database. qRT‐PCR analysis was applied to examine the expression of ABHD11‐AS1 in PTC cell lines and tissues. The relationship of ABHD11-AS1 expression and clinicopathological features was analyzed by Kaplan–Meier analysis.Two PTC cell lines (TPC-1 and KTC-1) were transfected with pcDNA 3.1, pcDNA3.1-ABHD11-AS1, si-NC and si-ABHD11-AS1, respectively, to verify the ABHD11-AS1 oncogene-regulating capacity to promote tumor progression. The cell metastasis and proliferation had been evaluated both in vitro and in vivo.ResultsHigh expression of ABHD11‐AS1 was found in PTC tissues (P < 0.01), which was significantly correlated with lymph node metastasis (P < 0.05). ABHD11-AS1 overexpression noticeably promoted cell proliferation, migration, and invasion capabilities, which were obviously decreased upon ABHD11-AS1 knockdown. ABHD11-AS1 positively regulated EGFR/EPS15L1 pathway, as EGFR, EPS15L1, STAT3, and p-STAT3 were activated.ConclusionABHD11‐AS1 promotes tumor progression in PTC by regulating EPS15L1/EGFR pathway.


Assuntos
Humanos , Linhagem Celular Tumoral , Movimento Celular/genética , Proliferação de Células/genética , Receptores ErbB/genética , Receptores ErbB/metabolismo , Regulação Neoplásica da Expressão Gênica , MicroRNAs/genética , RNA Antissenso/genética , Serina Proteases/genética , Serina Proteases/metabolismo , Transdução de Sinais
3.
Rev. esp. enferm. dig ; 112(5): 383-388, mayo 2020. ilus
Artigo em Inglês | IBECS | ID: ibc-188376

RESUMO

Although SARS-CoV-2 may primarily enter the cells of the lungs, the small bowel may also be an important entry or interaction site, as the enterocytes are rich in angiotensin converting enzyme (ACE)-2 receptors. The initial gastrointestinal symptoms that appear early during the course of COVID-19 support this hypothesis. Furthermore, SARSCoV virions are preferentially released apically and not at the basement of the airway cells. Thus, in the setting of a productive infection of conducting airway epithelia, the apically released SARS-CoV may be removed by mucociliary clearance and gain access to the GI tract via a luminal exposure. In addition, post-mortem studies of mice infected by SARS-CoV have demonstrated diffuse damage to the GI tract, with the small bowel showing signs of enterocyte desquamation, edema, small vessel dilation and lymphocyte infiltration, as well as mesenteric nodes with severe hemorrhage and necrosis. Finally, the small bowel is rich in furin, a serine protease which can separate the S-spike of the coronavirus into two “pinchers” (S1 and 2). The separation of the S-spike into S1 and S2 is essential for the attachment of the virion to both the ACE receptor and the cell membrane. In this special review, we describe the interaction of SARS-CoV-2 with the cell and enterocyte and its potential clinical implications


Assuntos
Humanos , Diarreia/virologia , Infecções por Coronavirus/complicações , Pneumonia Viral/complicações , Betacoronavirus/fisiologia , Intestino Delgado/virologia , Serina Proteases/metabolismo , Enterócitos/virologia , Pandemias , Receptor Tipo 2 de Angiotensina/metabolismo , Colite/virologia
4.
Rev. lab. clín ; 12(3): 137-146, jul.-sept. 2019. ilus, tab
Artigo em Espanhol | IBECS | ID: ibc-187168

RESUMO

Las proteasas de serina son enzimas ampliamente distribuidas en la naturaleza, responsables de múltiples e importantes procesos biológicos. Durante las infecciones bacterianas los patógenos secretan y usan sus proteasas de serina como factores de virulencia para combatir contra el huésped, a través de diversos efectos como la desorganización de tejidos, la proteólisis de efectores inmunológicos o la inactivación de componentes relevantes para la fisiología del huésped; sin embargo, desde hace algunos años se ha observado que las proteasas de serina podían modular procesos fisiológicos por un mecanismo altamente específico, a través de la activación de los receptores activados por proteasas. En este artículo resumimos el conocimiento reciente sobre las proteasas de serina bacteriana y su relevancia en la fisiopatología de la infección, y destacamos la oportunidad de nuevas intervenciones antimicrobianas basadas en la inhibición de la interacción receptores activados por proteasas-proteasa


Serine proteases are enzymes widely distributed in nature, and are responsible for multiple and important biological processes. During bacterial infection, pathogens secrete and use their serine proteases as virulent factors to combat against the host, through diverse mechanisms, such as tissue disruption, proteolysis of immunological effectors or inactivation of relevant components for the host physiology. However, some years ago it was observed that serine proteases could modulate physiological processes by a highly specific mechanism, through the activation of protease activated receptors (PARs). In this paper, we review recent knowledge about bacterial serine proteases and their relevance in the pathophysiology of infection. The opportunity for new antimicrobial interventions based on the inhibition of PAR-protease interaction, is also highlighted


Assuntos
Humanos , Serina Proteases/análise , Bactérias/enzimologia , Infecções Bacterianas/fisiopatologia , Inibidores de Proteases/farmacocinética , Inibidores de Serina Proteinase/farmacocinética , Antibacterianos/farmacocinética , Infecções Bacterianas/tratamento farmacológico , Peptídeo Hidrolases/classificação , Fatores de Virulência
5.
Rev. Rol enferm ; 41(2): 117-120, feb. 2018. ilus
Artigo em Espanhol | IBECS | ID: ibc-170949

RESUMO

Objetivo. Describir la evolución de una úlcera por presión (UPP) sacra de grado III aplicando la combinación del gel de proteasa activa y la TPN. Material y métodos. Descripción de caso clínico de paciente ingresada por perforación intestinal que requirió hemicolectomía derecha, confección de fístula mucosa e ileostomía terminal y colecistectomía. Debido a diversas complicaciones, desarrolló una UPP sacra de grado III. Se iniciaron curas habituales, desbridamiento cortante y, finalmente, se decidió tratamiento con combinación del gel de proteasa activa y TPN de un solo uso. Resultados. Tras desbridamiento quirúrgico de placa necrótica y esfacelos, se aplica gel de proteasa activa y TPN de un solo uso con hidrofibra de hidrocoloide. A los 7 días, la UPP presentó abundante tejido de granulación y mayor limpieza de esfacelo, así como una disminución de 1 cm de profundidad. Conclusiones. En este caso, el proceso de cicatrización de la lesión avanzó y, por lo tanto, la lesión mejoró, aunque no se pudo observar la resolución completa por el traslado de la paciente a otro centro sanitario. Sería conveniente realizar estudios comparativos de ambas terapias por separado para valorar su costeefectividad (AU)


Objective. To describe the evolution of a grade III sacral pressure ulcer (PU) by applying a combination of active protease gel and negative-pressure wound therapy (NPWT). Material and methods. A clinical case of a patient admitted with intestinal perforation requiring right hemicolectomy, mucous fistula, terminal ileostomy and cholecystectomy. Due to several complications, the patient developed a stage III sacral pressure ulcer. Regular cures and debridement were performed. The final treatment of choice was a combination of active protease gel and single-use NPWT. Results. After surgical debridement of necrotic plaque and scrapings, active protease gel and single-use NPWT with hydrocolloid hydrofibre was applied. By the 7th day of treatment, the PU presented abundant granulation tissue, decreased depth by 1 cm. and presented cleaner slough. Conclusions. In this case, the wound’s healing process progressed to a more favorable stage and the injury improved. Unfortunately, the complete healing process couldn’t be followed due to the patient’s transfer to another health center. It would be desirable to conduct comparative studies of both therapies, applied combined and separately, to assess cost-effectiveness (AU)


Assuntos
Humanos , Feminino , Idoso , Úlcera por Pressão/terapia , Cuidados de Enfermagem/métodos , Tratamento de Ferimentos com Pressão Negativa , Serina Proteases/uso terapêutico , Úlcera por Pressão/enfermagem , Desbridamento/métodos , Cicatrização , Técnicas de Fechamento de Ferimentos/enfermagem , Fatores de Risco
6.
Allergol. immunopatol ; 45(6): 579-591, nov.-dic. 2017. graf, ilus
Artigo em Inglês | IBECS | ID: ibc-168467

RESUMO

Proteolytic activity is fundamental to survival, so it is not surprising that all living organisms have proteases, especially seine protease. This enzyme in its numerous isoforms and homologues, constitutes the quintessential offence and defence factors, in the form of surface proteins, secreted molecules, gut digestive enzymes, venom in specialised glands or plant latex, among other manifestations. Occurring as trypsin, chymotrypsin, elastase, collagenase, thrombin, subtilisin etc., it mediates a diverse array of functions, including pathological roles as inflammatory, coagulatory to haemorrhagic. This review emphasizes that despite the superficial differences in mechanisms, most health issues, be they infectious, allergic, metabolic, or neural have a common conduit. This enzyme, in its various glycosylated forms leads to signal misinterpretations, wreaking havoc. However, organisms are endowed with serine protease inhibitors which might restrain this ubiquitous yet deleterious enzyme. Hence, serine proteases-driven pathogenesis and antagonising role of inhibitors is the focal point of this critical review (AU)


No disponible


Assuntos
Humanos , Serina Proteases/imunologia , Inflamação/imunologia , Hipersensibilidade/imunologia , Peptídeo Hidrolases/imunologia , Inibidores de Proteases/farmacocinética , Glicosilação , Mediadores da Inflamação/imunologia
7.
Allergol. immunopatol ; 44(6): 580-593, nov.-dic. 2016. graf, tab
Artigo em Inglês | IBECS | ID: ibc-157881

RESUMO

Currently, mankind is afflicted with diversified health issues, allergies being a common, yet little understood malady. Allergies, the outcome of a baffled immune system encompasses myriad allergens and causes an array of health consequences, ranging from transient to recurrent and mild to fatal. Indoor allergy is a serious hypersensitivity in genetically-predisposed people, triggered by ingestion, inhalation or mere contact of allergens, of which mite and cockroaches are one of the most-represented constituents. Arduous to eliminate, these aeroallergens pose constant health challenges, mostly manifested as respiratory and dermatological inflammations, leading to further aggravations if unrestrained. Recent times have seen an unprecedented endeavour to understand the conformation of these allergens, their immune manipulative ploys and other underlying causes of pathogenesis, most importantly therapies. Yet a large section of vulnerable people is ignorant of these innocuous-looking immune irritants, prevailing around them, and continues to suffer. This review aims to expedite this field by a concise, informative account of seminal findings in the past few years, with particular emphasis on leading frontiers like genome-wide association studies (GWAS), epitope mapping, metabolomics etc. Drawbacks linked to current approaches and solutions to overcome them have been proposed


No disponible


Assuntos
Humanos , Pyroglyphidae/patogenicidade , Hipersensibilidade Respiratória/epidemiologia , Baratas/patogenicidade , Serina Proteases/imunologia , Mapeamento de Epitopos , Metabolômica/métodos , Estudo de Associação Genômica Ampla/métodos
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