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目的:研究人α半乳糖苷酶和人α1,2岩藻糖基转移酶在NIH3T3细胞上协同性地抑制Gal抗原表位的表达和相关异种反应性。方法:流式细胞术比较G抗原、H抗原和人天然抗体(IgG和IgM)的表达水平,蛋白质印迹检测G抗原糖蛋白的表达,四唑盐(MTT)比色试验检测NIH3T3细胞在人血清介导的裂解作用下的活力。结果:转染人α半乳糖苷酶和人α1,2岩藻糖基转移酶的NIH3T3细胞中G抗原的表达及其与人天然抗体(IgG和IgM)的结合能力都显著下降,其抗人血清介导的细胞裂解反应能力有效提高。结论:人α半乳糖苷酶和α1,2岩藻糖基转移酶能够相互协同抑制Gal抗原表位表达和相关异种排斥反应。
AIM: To investigate the inhibitory effect of human α-galactosidase and human α1,2-fucosyltransferase on Gal epitope expression and related xenoreactivity on NIH3T3 cells. Methods: The expression of G antigen, H antigen and human natural antibody (IgG and IgM) were compared by flow cytometry. The expression of G antigen glycoprotein was detected by Western blotting. The NIH3T3 cells were detected by MTT colorimetric assay in human serum Mediated by the lysis of the vitality. Results: The expression of G antigen in NIH3T3 cells transfected with human α-galactosidase and human α1,2 fucosyltransferase and its binding ability with human natural antibodies (IgG and IgM) were significantly decreased. The anti-human Serum-mediated cell lysis reaction effectively improved. CONCLUSION: Human α-galactosidase and α1,2-fucosyltransferase can synergistically inhibit the expression of Gal epitopes and the related xenograft rejection.