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1.
Zhonghua Gan Zang Bing Za Zhi ; 30(1): 63-68, 2022 Jan 20.
Artigo em Zh | MEDLINE | ID: mdl-35152671

RESUMO

Objective: To study the expression and effect of small nuclear ribonucleoprotein-associated protein B (SNRPB) on proliferation and metastasis of liver cancer tissues and cells. Methods: The bioinformatics database starBase v3.0 and GEPIA were used to analyze the expression of SNRPB in liver cancer tissue and normal liver tissue, as well as the survival and prognosis of liver cancer patients. The expression of SNRPB mRNA and protein in liver cancer cell lines were analyzed by qRT-PCR and Western blot. RNA interference technique (siRNA) was used to determine SNRPB protein expression down-regulation. The proliferation effect on hepatocellular carcinoma cells was observed by MTT assay. Transwell invasion and migration assay was used to detect the changes in the metastatic ability of liver cancer cells after SNRPB down-regulation. Western blot was used to detect the changes of epithelial mesenchymal transition (EMT) markers in liver cancer cells after down-regulation of SNRPB expression. Data were compared between two groups and multiple groups using t-test and analysis of variance. Results: The expression of SNRPB was significantly higher in liver cancer tissue than normal liver tissue, and its expression level was correlated with the prognosis of liver cancer patients. Compared with the immortalized hepatocyte LO(2), the expression of SNRPB was significantly increased in the liver cancer cells (P < 0.01). siRNA-SNRPB had significantly inhibited the expression of SNRPB mRNA and protein in liver cancer cells. MTT results showed that the absorbance value was lower in SNRPB knockdown group than negative control group, and the difference at 96 h after transfection was most significant (P < 0.01). Transwell assay results showed that compared with the negative control group, the SNRPB knockdown group (MHCC-97H: 121.27 ± 8.12 vs. 46.38 ± 7.54; Huh7: 126.50 ± 6.98 vs. 41.10 ± 8.01) invasion and migration (MHCC-97H: 125.20 ± 4.77 vs. 43.18 ± 7.32; Huh7: 132.22 ± 8.21 vs. 38.00 ± 6.78) ability was significantly reduced (P < 0.01) in liver cancer cells. Western blot showed that the expression level of epithelial phenotype marker E-cadherin was decreased after down-regulation of SNRPB, while the expression levels of mesenchymal phenotype markers N-cadherin and vimentin was increased, suggesting that down-regulation of SNRPB inhibited EMT in liver cancer cells. Conclusion: SNRPB expression is significantly increased in liver cancer tissues and cells, and it is involved in regulating the proliferation, metastasis and EMT of liver cancer cells.


Assuntos
Carcinoma Hepatocelular , Neoplasias Hepáticas , Carcinoma Hepatocelular/genética , Linhagem Celular Tumoral , Movimento Celular , Proliferação de Células , Transição Epitelial-Mesenquimal , Regulação Neoplásica da Expressão Gênica , Humanos , Neoplasias Hepáticas/genética , Proteínas Centrais de snRNP
2.
Zhongguo Yao Li Xue Bao ; 11(5): 400-6, 1990 Sep.
Artigo em Zh | MEDLINE | ID: mdl-1718142

RESUMO

Six parameters (molecular negentropy, acidic group number, basic group number, proton donor group number, proton acceptor group number, and a ratio of C atomic group number to total atomic group number) for characterizing the structure of an antibody combining site in a R1 chain of cephalosporins were selected. Although 12 parameters characterized the site A and site B in a R1 chain were used in fuzzy cluster, Fischer weighting ratio (Fi) indicated that only 5 parameters, 4 of them characterized the structure of site A, play an important part in the cluster. Therefore it was speculated that the site A was the major combining site in the antigen-antibody interaction. According to the similarity of the R1 chains, cephalosporins could be clustered into 4 groups among which less cross-reaction took place. Using the "relative Hamming distance" of the R1 chains for description of their similarity, we found that the intensity of the cross-reaction assayed by immune tests had a close correlation with the "relative Hamming distance", so the distance was used for prediction of the intensity of the cross-reaction of cephalosporins.


Assuntos
Cefalosporinas/imunologia , Epitopos/imunologia , Sítios de Ligação de Anticorpos , Cefalosporinas/química , Análise por Conglomerados , Reações Cruzadas/imunologia , Relação Estrutura-Atividade
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