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1.
Journal of Peking University(Health Sciences) ; (6): 875-880, 2020.
Artigo em Chinês | WPRIM | ID: wpr-942089

RESUMO

OBJECTIVE@#To evaluate the clinical efficacy of short-term halo-pelvic traction (HPT) combined with surgery in the treatment of severe spinal deformities.@*METHODS@#In the study, 24 patients diagnosed as severe spinal deformity accepted the treatment of one-stage short-term HPT and two-stage surgery from January 2015 to May 2018 in our orthopedics department. 24 cases (9 males and 15 females) were retrospectively reviewed. The average age of the cohort was (28.8±10.0) years (12-48 years). The height, scoliosis angle, kyphosis angle, the height difference of shoulders, the height difference of crista iliaca, C7PL-CSVL and the perpendicular distance of S1 and the convex point of the patients were assessed at pre-traction, post-traction and post-surgery. The paired t test was used to analyze the difference among pre-traction, post-traction and post-surgery.@*RESULTS@#The average traction time of 24 cases was (2.5±1.1) weeks (1-5 weeks). The height of pre-traction and post-traction were (141.7±11.2) cm (116-167 cm) and (154.1±9.5) cm (136-176 cm) respectively, showing significant difference (P < 0.05), and the increased height was (12.4±4.6) cm (4-20 cm). The average scoliosis angle before traction was 104.9°±35.0°(25°-158°), and it was significantly decreased in post-traction[64.8°±21.0°(19°-92°)] and post-surgery[39.3°±17.0° (10°-70°)] (P < 0.05). The traction's coronal correction rate was 37.2%±10.9% (11.9%-51.2%) and the total coronal correction rate was 61.9%±12.6%(26.9%-79.0%). The average kyphosis angle before traction was 106.9°±29.2°(54°-163°), and it was significantly decreased in post-traction [63.1°±17.1°(32°-92°)] and post-surgery [39.0°±16.8°(10°-68°)](P < 0.05). The traction's sagittal correction rate was 40.0%±10.7%(16.7%-55.5%) and the total sagittal correction rate was 64.3%±10.7%(49.0%-87.5%). The average C7PL-CSVL before traction was (3.2±2.8) cm, and it was significantly decreased in post-traction [(2.5±2.5) cm] (P < 0.05). The perpendicular distance of S1 and the convex point before traction was (10.5±4.8) cm, and it was significantly decreased in post-traction[(8.4±3.5) cm] (P < 0.05).@*CONCLUSION@#The one-stage short-term HPT combined with two-stage surgery is a safe and effective procedure for severe spinal deformities. The clinical efficacy is satisfactory and the complication is relatively less.


Assuntos
Adolescente , Adulto , Feminino , Humanos , Masculino , Adulto Jovem , Cifose/cirurgia , Estudos Retrospectivos , Escoliose/cirurgia , Tração , Resultado do Tratamento
2.
Journal of Huazhong University of Science and Technology (Medical Sciences) ; (6): 37-42, 2013.
Artigo em Inglês | WPRIM | ID: wpr-343147

RESUMO

The molecular pathogenesis of leukemia is poorly understood. Earlier studies have shown both Wilms' tumor 1 suppressor gene (WT1) and CML28 abnormally expressed in malignant diseases of the hematopoietic system and WT1 played an important role in leukemogenesis. However, the relationship between molecular CML28 and WT1 has not been reported. Here we described the use of small interfering RNA (siRNA) against WT1 and CML28 in leukemic cell line K562 to examine the interaction between CML28 and WT1. WT1 and CML28 gene expression in transfected K562 cells was detected by using RQ-PCR and Western blotting. K562 cells transfected with WT1-siRNA could greatly decrease both mRNA and protein expression levels of WT1 and CML28. In contrast, CML28-siRNA did not exert effect on WT1. Further, subcellular co-localization assay showed that the two proteins could co-localize in the cytoplasm of K562 cells, but WT1/CML28 complexes were not detected by using immunoprecipitation. It was suggested that there exists the relationship between CML28 and WT1. CML28 may be a downstream target molecule of WT1 and regulated by WT1, which will provide important clues for further study on the role of CML28 and WT1 in leukemic cells.


Assuntos
Humanos , Antígenos de Neoplasias , Metabolismo , Linhagem Celular Tumoral , Complexo Multienzimático de Ribonucleases do Exossomo , Metabolismo , Células K562 , Leucemia Eritroblástica Aguda , Metabolismo , Proteínas de Neoplasias , Metabolismo , Mapeamento de Interação de Proteínas , Proteínas de Ligação a RNA , Metabolismo , Frações Subcelulares , Metabolismo , Proteínas WT1 , Metabolismo
3.
Journal of Huazhong University of Science and Technology (Medical Sciences) ; (6): 37-42, 2013.
Artigo em Inglês | WPRIM | ID: wpr-636050

RESUMO

The molecular pathogenesis of leukemia is poorly understood. Earlier studies have shown both Wilms' tumor 1 suppressor gene (WT1) and CML28 abnormally expressed in malignant diseases of the hematopoietic system and WT1 played an important role in leukemogenesis. However, the relationship between molecular CML28 and WT1 has not been reported. Here we described the use of small interfering RNA (siRNA) against WT1 and CML28 in leukemic cell line K562 to examine the interaction between CML28 and WT1. WT1 and CML28 gene expression in transfected K562 cells was detected by using RQ-PCR and Western blotting. K562 cells transfected with WT1-siRNA could greatly decrease both mRNA and protein expression levels of WT1 and CML28. In contrast, CML28-siRNA did not exert effect on WT1. Further, subcellular co-localization assay showed that the two proteins could co-localize in the cytoplasm of K562 cells, but WT1/CML28 complexes were not detected by using immunoprecipitation. It was suggested that there exists the relationship between CML28 and WT1. CML28 may be a downstream target molecule of WT1 and regulated by WT1, which will provide important clues for further study on the role of CML28 and WT1 in leukemic cells.

4.
Journal of Experimental Hematology ; (6): 1302-1306, 2012.
Artigo em Chinês | WPRIM | ID: wpr-278385

RESUMO

This study was aimed to investigate the expression of GST-CML28 in Escherichia Coli and to prepare its antibody. The constructed recombinant expression vectors CML28-pGEX-3X were transformed into Escherichia Coli BL21 under IPTG induction. The protein was abstracted from the transformers, and purified by a GSTrap FF column. The rabbits were immunized by the purified fusion protein to produce serum with anti-CML28 antibody. The serum was purified by chromatographic column stuffed with glutathione Sephamse 4B to get the antibody. The specific antibody against CML28 was further identified by ELISA, Western blot, immunohistochemistry and quantum dot luminescence. The results indicated that GST-CML28 fusion protein was expressed in Escherichia coli and its specific polyclonal antibody was obtained. It is concluded that the anti-CML28 polyclonal antibodies with high titer and specificity are successfully prepared. These antibodies provide an useful experimental tool to profoundly research the physiological significance and biological function of the CML28 gene.


Assuntos
Animais , Humanos , Coelhos , Anticorpos , Alergia e Imunologia , Metabolismo , Antígenos de Neoplasias , Alergia e Imunologia , Células Cultivadas , Escherichia coli , Metabolismo , Complexo Multienzimático de Ribonucleases do Exossomo , Alergia e Imunologia , Vetores Genéticos , Glutationa Transferase , Células Endoteliais da Veia Umbilical Humana , Biologia Celular , Proteínas de Ligação a RNA , Alergia e Imunologia , Proteínas Recombinantes de Fusão , Alergia e Imunologia
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