The distribution of lysosomal cathepsin D in cardiac myocytes.
Author(s) -
Robert S. Decker,
Marlene L. Decker,
A. Robin Poole
Publication year - 1980
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 - 10.1177/28.3.6986433
Subject(s) - endoplasmic reticulum , golgi apparatus , cathepsin d , cathepsin , peroxidase , immunohistochemistry , chemistry , myocyte , biochemistry , staining , microbiology and biotechnology , cytoplasm , cathepsin b , lysosome , enzyme , biology , immunology , genetics
Lysosomal cathepsin D has been localized with the electron microscope employing an indirect immunohistochemical method using peroxidase labeled, monospecific antibody Fab' subunits. The acid proteinase has been demonstrated within secondary lysosomes of cardiac myocytes and interstitial cells, but not in components of the Golgi apparatus or endoplasmic reticulum. Incubations with a variety of peroxidatic inhibitors suggests that the staining that is observed in secondary lysosomes is attributable to the peroxidase-labeled antibody and not to endogenous oxidation of DAB. The protocol outlined here provides a reproducible method to localize the major lysosomal acid proteinase of the heart at the subcellular level.
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