Immunohistochemical localization of the beta subunit of prolyl 4-hydroxylase in human alveolar epithelial cells.
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.
Kasper
M
M
Institute of Pathology, Technical University Dresden, Germany.
Schuh
D
D
Müller
M
M
D000911:Antibodies, Monoclonal / Q000276:immunology; D004847:Epithelial Cells; D004848:Epithelium / Q000201:enzymology; D005455:Fluorescent Antibody Technique; D006801:Humans; D007124:Immunoenzyme Techniques; D007150:Immunohistochemistry; D016612:Paraffin Embedding; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism*; D011650:Pulmonary Alveoli / Q000166:cytology / Q000201:enzymology*
D000911:Antibodies, Monoclonal; D011393:Procollagen-Proline Dioxygenase