Immunohistochemical localization, purification, and characterization of human urinary bladder glutathione S-transferases.
Immunohistochemical localization, purification, and characterization of human urinary bladder glutathione S-transferases.
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人膀胱谷胱甘肽 S-转移酶的免疫组织化学定位、纯化和表征。
DOI：
10.1016/0304-4165(91)90086-v
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Awasthi,YC
中科院分区：
文献类型：
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作者：
Singh,SV;Roberts,B;Gudi,VA;Ruiz,P;Awasthi,YC
本文报道了人膀胱谷胱甘肽S-转移酶（GST）的免疫组织化学定位、纯化和鉴定。尽管所有三种主要的同工酶（α、μ和π）都在人膀胱中表达，但总GST活性的90%以上是π类阴离子形式。人膀胱α、μ和π类GST与其他人体组织的相应同工酶具有免疫相关性。GST π在所有分析的13个样品中均存在，而GST α和μ分别在9个和11个样品中检出。人膀胱的GST α似乎是独特的，因为与其他人体组织的GST不同，膀胱酶对与环氧活化的Sepharose 6 B亲和树脂连接的GSH具有较低的亲和力。免疫组化显示GST α主要分布于上皮细胞表面、黏膜下层和平滑肌，而μ和π类同工酶主要分布于上皮细胞表面。这些结果表明，人膀胱GST可能发挥重要作用，在提供保护，对外源性物质，因为上皮细胞被认为是几种致癌物质的目标和所有三类同工酶在这些细胞中表达。
This study describes immunohistochemical localization, purification and characterization of glutathioneS-transferase (GST) of human urinary bladder. Even though all the three major classes of isoenzymes (α, μ, and π) were expressed in human bladder, more than 90% of total GST activity was accounted for by a π class anionic form. Human bladder α, μ, and π class GSTs were immunologically related to respective isoenzymes of other human tissues. GST π was present in all 13 samples analyzed, whereas GST α and μ were detected in nine and eleven samples, respectively. GST α of human bladder appeared to be unique, because unlike this class of GSTs of other human tissues, bladder enzyme had lower affinity for GSH linked to epoxy-activated Sepharose 6B affinity resin. Immunohistochemical staining indicated localization of GST α in epithelial surface cells, underlying submucosa and smooth muscle, whereas μ and π class isoenzymes were predominantly distributed in epithelial surface cells. These results suggest that human bladder GSTs may play an important role in providing protection against xenobiotics because epithelium is considered a target for several carcinogens and all the three classes of isoenzymes are expressed in these cells.