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1.
Sci Rep ; 11(1): 23300, 2021 12 02.
Artículo en Inglés | MEDLINE | ID: mdl-34857832

RESUMEN

Currently, the most widely used screening methods for hyperuricemia (HUA) involves invasive laboratory tests, which are lacking in many rural hospitals in China. This study explored the use of non-invasive physical examinations to construct a simple prediction model for HUA, in order to reduce the economic burden and invasive operations such as blood sampling, and provide some help for the health management of people in poor areas with backward medical resources. Data of 9252 adults from April to June 2017 in the Affiliated Hospital of Guilin Medical College were collected and divided randomly into a training set (n = 6364) and a validation set (n = 2888) at a ratio of 7:3. In the training set, non-invasive physical examination indicators of age, gender, body mass index (BMI) and prevalence of hypertension were included for logistic regression analysis, and a nomogram model was established. The classification and regression tree (CART) algorithm of the decision tree model was used to build a classification tree model. Receiver operating characteristic (ROC) curve, calibration curve and decision curve analyses (DCA) were used to test the distinction, accuracy and clinical applicability of the two models. The results showed age, gender, BMI and prevalence of hypertension were all related to the occurrence of HUA. The area under the ROC curve (AUC) of the nomogram model was 0.806 and 0.791 in training set and validation set, respectively. The AUC of the classification tree model was 0.802 and 0.794 in the two sets, respectively, but were not statistically different. The calibration curves and DCAs of the two models performed well on accuracy and clinical practicality, which suggested these models may be suitable to predict HUA for rural setting.


Asunto(s)
Hiperuricemia/diagnóstico , Hiperuricemia/epidemiología , Población Rural/estadística & datos numéricos , Adulto , Factores de Edad , Anciano , Anciano de 80 o más Años , Índice de Masa Corporal , China/epidemiología , Árboles de Decisión , Femenino , Humanos , Hipertensión/complicaciones , Hipertensión/epidemiología , Hiperuricemia/etiología , Hiperuricemia/prevención & control , Modelos Logísticos , Masculino , Persona de Mediana Edad , Modelos Teóricos , Nomogramas , Prevalencia , Curva ROC , Factores Sexuales , Adulto Joven
2.
Med Sci Monit ; 26: e923290, 2020 Jun 25.
Artículo en Inglés | MEDLINE | ID: mdl-32584794

RESUMEN

BACKGROUND This study aimed to investigate the association between levels of serum amyloid A (SAA) and the activity of systemic lupus erythematosus (SLE). MATERIAL AND METHODS The study included 135 patients with SLE, including 52 patients with active SLE and 83 patients with inactive SLE and 149 healthy controls. The degree of activity of SLE was assessed using the SLE Disease Activity Index 2000 (SLEDAI-2K). Serum SAA levels were measured using a Cobas 8000 c702 modular analyzer. RESULTS The levels of SAA were significantly increased in patients with active SLE compared with patients with inactive SLE (median IQR, 16.65 mg/L; range, 9.35-39.68 mg/L, and median IQR, 2.30 mg/L, range, 1.30-4.80 mg/L) (p<0.001). Levels of SAA were significantly correlated with the SLEDAI-2K scores, the erythrocyte sedimentation rate (ESR), and hypersensitive C-reactive protein (Hs-CRP) in patients with SLE (r=0.726, p<0.001; r=0.631, p<0.001; r=0.774, p<0.001, respectively). Multivariate logistic regression analysis showed that the SAA values were independently associated with active SLE when controlled for white blood cell (WBC) count, red blood cell distribution width (RDW), ESR, and Hs-CRP (OR=1.772; p=0.01; 95% CI, 1.101-2.851). Receiver operating characteristic (ROC) curve analysis for SAA was used to identify patients with active SLE with an area under the curve of 0.971, a sensitivity of 90.4%, and a specificity of 94.0%. CONCLUSIONS SAA levels were significantly correlated with disease activity in patients with SLE.


Asunto(s)
Lupus Eritematoso Sistémico/metabolismo , Proteína Amiloide A Sérica/metabolismo , Adulto , Biomarcadores , Sedimentación Sanguínea , Proteína C-Reactiva/metabolismo , Estudios de Casos y Controles , Femenino , Humanos , Modelos Logísticos , Lupus Eritematoso Sistémico/fisiopatología , Masculino , Persona de Mediana Edad , Análisis Multivariante , Curva ROC , Índice de Severidad de la Enfermedad
3.
Sheng Wu Gong Cheng Xue Bao ; 23(4): 677-80, 2007 Jul.
Artículo en Chino | MEDLINE | ID: mdl-17822043

RESUMEN

In order to improve the thermostability of the Penicillium expansum Lipase (PEL), the lipase encoding genes was mutated by site-directed mutagenesis. A recombinant vector pAO815-ep8-K55R which contain double mutant genes was constructed by overlap extension PCR using the cDNA of a random-mutant lipase ep8 (a single site mutant) as the template and two special primers were used to generate another mutation site K55R. The recombinant vector was transformed into Pichia pastoris GS115 by electroporation and the recombinant mutant GS-pAO815-ep8- K55R can secret double-mutant lipase PEL-ep8-K55R-GS into the medium when it was induced by Methanol. The yield of the double-mutant lipase is 508 u/mL, which is 81% that of the wild type lipase PEL-GS (627 u/mL) and 55% that of random-mutant PEL-ep8-GS (924 u/mL). The specific activity of double-mutant lipase is 2309.1 u/mg, which is similar to random-mutant lipase PEL-ep8-GS and the wild type lipase PEL-GS. The optimum temperature of the double-mutant lipase is same with the wild type lipase PEL-GS and random-mutant lipase PEL-ep8-GS. While the Tm of the double-mutant lipase is 41.0 degrees C, 2.3 degrees C higher than the wild type lipase PEL-GS and 0.8% higher than the random-mutant lipase PEL-ep8-GS, indicating that the double-mutant lipase PEL-ep8-K55R-GS has higher thermostability.


Asunto(s)
Lipasa/genética , Lipasa/metabolismo , Proteínas Mutantes/metabolismo , Penicillium/enzimología , Electroporación , Estabilidad de Enzimas , Calor , Mutagénesis Sitio-Dirigida , Pichia/genética , Pichia/metabolismo , Ingeniería de Proteínas/métodos , Proteínas Recombinantes/biosíntesis , Proteínas Recombinantes/genética
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