Immunocytochemical localization of catalase and heat-labile enoyl-CoA hydratase in the livers of normal and peroxisome proliferator-treated rats.
Immunocytochemical localization of catalase and heat-labile enoyl-CoA hydratase in the livers of normal and peroxisome proliferator-treated rats.
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发表时间：
1982
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通讯作者：
M. Bendayan;J. Reddy
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作者：
M. Bendayan;J. Reddy
过氧化氢酶和不耐热烯酰辅酶A水合酶（过氧化物酶体脂肪酸β-氧化螺旋的第二种酶）的细胞内定位已在正常和过氧化物酶体增殖剂处理的大鼠肝脏中使用蛋白A-金免疫细胞化学方法进行了研究。通过饮食给予Wy-14,653（[4-氯-6-(2,3-xylidino)2-嘧啶硫基]乙酸）诱导大鼠肝脏中的过氧化物酶体增殖。正如预期的那样，过氧化氢酶仅存在于正常和过氧化物酶体增殖剂治疗的大鼠肝实质细胞的所有过氧化物酶体基质中。不耐热的烯酰辅酶A水合酶先前已被证明在免疫化学上与80,000分子量的过氧化物酶体增殖相关多肽相同，也被限制在过氧化物酶体基质中。过氧化物酶体核未显示任何这些蛋白质的抗原位点。过氧化氢酶免疫细胞化学标记的定性和定量评估为增殖的过氧化物酶体中与正常过氧化物酶体相比该酶的量减少提供了直接的视觉证据。相反，增殖的过氧化物酶体含有较高水平的热不稳定烯酰辅酶A水合酶。
The intracellular localization of catalase and the heat-labile enoyl-CoA hydratase (second enzyme of the peroxisomal fatty acid beta-oxidation spiral) has been investigated using the protein A-gold immunocytochemical procedure in normal and peroxisome proliferator-treated rat livers. Peroxisome proliferation in rat liver was induced by the dietary administration of Wy-14,653 ([4-chloro-6-(2,3-xylidino)2-pyrimidinylthio]acetic acid). As expected, catalase was demonstrable exclusively in the matrix of all peroxisomes in hepatic parenchymal cells of normal and peroxisome proliferator-treated rats. The heat-labile enoyl-CoA hydratase, which was shown previously to be immunochemically identical with 80,000-molecular weight peroxisome proliferation-associated polypeptide, was also confined to the peroxisome matrix. The peroxisome nucleoids displayed no antigenic sites for any of these proteins. Both qualitative and quantitative evaluation of immunocytochemical labeling of catalase provide direct visual evidence for the decreased amount of this enzyme in proliferated peroxisomes when compared with normal peroxisomes. In contrast, the proliferated peroxisomes contained higher levels of heat-labile enoyl-CoA hydratase.