Kasper M, Schuh D, Müller M
Institute of Pathology, Technical University Dresden, Germany.
Acta Histochem. 1994 Sep;96(3):309-13. doi: 10.1016/s0065-1281(11)80040-1.
The beta subunit of prolyl 4-hydroxylase, the protein-disulfide isomerase (PDJ), catalyzes the hydroxylation of proline residues of collagens and proteins with collagen-like structure, a step essential for the folding of the procollagen chains to form triple-helices. In the present study, we report the selective immunohistological localization of PDI in type II alveolar and bronchial epithelial cells. The detection of the hidden antigen with the monoclonal antibody 5B5 is usually not successful in paraffin sections but was possible after microwave pretreatment of tissue sections. In cases of severe lung injury (fibrosing alveolitis) enhanced immunoreactivity was found for this enzyme in epithelial, endothelial as well as interstitial cells and in alveolar macrophages. The results indicate a possible involvement of the pulmonary epithelial cells in the upregulation of collagen production during the process of fibrosis.
脯氨酰4-羟化酶的β亚基，即蛋白质二硫键异构酶（PDI），催化胶原蛋白和具有胶原样结构的蛋白质中脯氨酸残基的羟化反应，这是前胶原链折叠形成三螺旋的关键步骤。在本研究中，我们报告了PDI在II型肺泡和支气管上皮细胞中的选择性免疫组织化学定位。用单克隆抗体5B5检测隐藏抗原在石蜡切片中通常不成功，但在对组织切片进行微波预处理后是可行的。在严重肺损伤（纤维化肺泡炎）的病例中，发现该酶在上皮细胞、内皮细胞、间质细胞以及肺泡巨噬细胞中的免疫反应性增强。结果表明，在纤维化过程中，肺上皮细胞可能参与了胶原蛋白产生的上调。
