Immunocytochemical demonstration of cytochrome c oxidase with an immunoperoxidase method: a specific stain for mitochondria in formalin-fixed and paraffin-embedded human tissues.
Author(s) -
Carlos D. Bedetti
Publication year - 1985
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/33.5.2580882
Subject(s) - immunoperoxidase , immunostaining , mitochondrion , cytochrome c oxidase , staining , cytoplasm , stain , antiserum , pathology , biology , microbiology and biotechnology , chemistry , immunohistochemistry , biochemistry , antibody , medicine , monoclonal antibody , immunology
Cytochrome c oxidase (CO) is the terminal electron carrier of the respiratory chain and is localized exclusively in the inner membrane of the mitochondria. Using a specific rabbit antiserum against bovine heart CO, mitochondria were specifically stained in sections of formalin-fixed paraffin-embedded human tissues by an immunoperoxidase method. The intensity of the immunostaining in different human tissues correlated mainly with the number of mitochondria and abundance of mitochondrial cristae, i.e., surface area of the inner mitochondrial membrane. Mitochondrion-rich cells, such as myocardial and gastric parietal cells, had very strong cytoplasmic staining. This technique was especially useful for the specific identification of oncocytes in normal tissues and in lesions composed of oncocytes. In addition, the immunoperoxidase method for CO makes possible retrospective investigations of lesions composed of oncocytes, since routine paraffin blocks of formalin-fixed tissue are quite suitable for such studies.
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