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1.
Indian J Hum Genet ; 2012 Jan; 18(1): 83-86
Artículo en Inglés | IMSEAR | ID: sea-139448

RESUMEN

BACKGROUND: Outer inflammatory protein A (OipA) is an outer membrane protein of Helicobacter pylori that is involved in inducing IL-8 and intracellular signaling. In this study, we have predicted exposure amino acid sequences of OipA for insertion in permissive sites of CstH subunit of Eschierchia coli CS3 pilli for bacterial surface display. MATERIALS AND METHODS: Databases: National Center for Biotechnology Institute and Protein Data Bank. Servers: PHD, SABLE, GOR 4, SignalP3.0, TBBpred, PRODIV-TMHMM, TMRPres2D, CPH Models, PHYRE, GETAREA, VADAR, Pep state and pep window. Software: Swiss PDB viewer and Discovery studio. RESULTS: In silico prediction of exposure amino acid sequences of OipA led to detection of six sequences of amino acid, 76-87, 106-112, 170-182, 222-230, 242-258, and 278-290. These sequences inserted between amino acid sequences 66-67, 100-101, and 109-110 of CstH that were predicted by Eskandari et al. as permissive sites of CstH. CONCLUSION: OipA has the ability to induce IL-8 from gastric epithelial cells and some papers are mentioned that this outer membrane protein involve to attachment and intracellular signaling. Receptor of OipA and adhesion motifs on this protein is unknown. Detection of exposure motifs aids to recognition of adhesion motifs and receptor of OipA on gastric epithelial cells. In this study, we have predicted exposure amino acid sequences for insert to subunit CstH of CS3 pilli E. coli for surface display.


Asunto(s)
Secuencia de Aminoácidos/análisis , Proteínas de la Membrana Bacteriana Externa/análisis , Simulación por Computador/métodos , Escherichia coli/fisiología , Células Epiteliales/microbiología , Helicobacter pylori/fisiología , Péptidos y Proteínas de Señalización Intracelular/análisis , Proteínas Inflamatorias de Macrófagos/análisis , Estómago/citología , Interfaz Usuario-Computador
2.
Journal of Korean Medical Science ; : 621-628, 2007.
Artículo en Inglés | WPRIM | ID: wpr-48773

RESUMEN

The distinction between benign and malignant thyroid tumors is critical for the management of patients with thyroid nodules. We applied immunohistochemical staining for galectin-3, HBME-1, cytokeratin 19 (CK19), high molecular weight cytokeratin (HMWCK), cyclin D1 and p27(kip1) in 295 thyroid lesions to determine their diagnostic accuracy. The expression of all markers was significantly associated with differentiated thyroid carcinoma (DTC).The sensitivity for the diagnosis of DTC was 94.7% with galectin-3, 91.3% with HBME-1, and 90.3% with CK19. The specificities of these markers were 95.5%, 69.7%, and 83.1%, respectively. Combining these markers, co-expression of galectin-3 and CK19 or galectin-3 and HBME-1 was seen in 93.2% of carcinomas but in none of the benign nodules. Comparing follicular variant of papillary carcinoma (FVPC) with follicular carcinoma (FC), the expression of galectin-3, CK19, and HMWCK was significantly higher in FVPC. When comparing FC with FA, the expression of galectin-3 and HBME-1 was significantly higher in FC. These results suggest that 1) galectin-3 is a useful marker in the distinction between benign and malignant thyroid tumors, 2) the combined use of HBME-1 and CK19 can increase the diagnostic accuracy, and 3) the use of CK19 and HMWCK can aid in the differential diagnosis between PC and FC.


Asunto(s)
Humanos , Adenocarcinoma Folicular/diagnóstico , Carcinoma Papilar Folicular/diagnóstico , Ciclina D1/análisis , Inhibidor p27 de las Quinasas Dependientes de la Ciclina/análisis , Diagnóstico Diferencial , Galectina 3/análisis , Inmunohistoquímica , Péptidos y Proteínas de Señalización Intracelular/análisis , Queratina-19/análisis , Queratinas/análisis , Sensibilidad y Especificidad , Glándula Tiroides/química , Nódulo Tiroideo/diagnóstico , Biomarcadores de Tumor/análisis
3.
Experimental & Molecular Medicine ; : 310-319, 2006.
Artículo en Inglés | WPRIM | ID: wpr-51258

RESUMEN

Myristoylated alanine-rich C kinase substrate (MARCKS) is a widely distributed protein kinase C (PKC) substrate and has been implicated in actin cytoskeletal rearrangement in response to extracellular stimuli. Although MARCKS was extensively examined in various cell culture systems, the physiological function of MARCKS in the central nervous system has not been clearly understood. We investigated alterations of cellular distribution and phosphorylation of MARCKS in the hippocampus following kainic acid (KA)-induced seizures. KA (25 mg/kg, i.p.) was administered to eight to nine week-old C57BL/6 mice. Behavioral seizure activity was observed for 2 h after the onset of seizures and was terminated with diazepam (8 mg/kg, i.p.). The animals were sacrificed and analyzed at various points in time after the initiation of seizure activity. Using double-labeling immunofluorescence analysis, we demonstrated that the expression and phosphorylation of MARCKS was dramatically upregulated specifically in microglial cells after KA-induced seizures, but not in other types of glial cells. PKC alpha, beta I, beta II and delta, from various PKC isoforms examined, also were markedly upregulated, specifically in microglial cells. Moreover, immunoreactivities of phosphorylated MARCKS were co-localized in the activated microglia with those of the above isoforms of PKC. Taken together, our in vivo data suggest that MARCKS is closely linked to microglial activation processes, which are important in pathological conditions, such as neuroinflammation and neurodegeneration.


Asunto(s)
Ratones , Animales , Regulación hacia Arriba/efectos de los fármacos , Factores de Tiempo , Convulsiones/inducido químicamente , Proteína Quinasa C-delta/análisis , Proteína Quinasa C-alfa/análisis , Proteína Quinasa C/análisis , Biosíntesis de Proteínas/efectos de los fármacos , Fosforilación/efectos de los fármacos , Microscopía Confocal , Microglía/citología , Ratones Endogámicos C57BL , Proteínas de la Membrana/análisis , Ácido Kaínico/toxicidad , Isoenzimas/análisis , Péptidos y Proteínas de Señalización Intracelular/análisis , Inmunohistoquímica
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