Synopsis
The subcellular locations of β-glucuronidase and acid phosphatase in peripheral tissue of a transplantable rat tumour were studied using histochemical methods. In noninvading tumour cells, particulate and diffuse cytoplasmic locations were recorded for both enzymes; but in tumour cells at the invading edge, β-glucuronidase, unlike acid phosphatase, was rarely detected in a particulate location. Particles containing these enzymes were usually 0.2–0.4 μm in diameter. In cells more remote from both invasive and non-invasive tumour peripheries, larger particles (0.5–1.0 μm in diameter) were more often observed. Pretreatment or simultaneous treatment of sections with Triton X-100 was found to remove most, if not all, particulate β-glucuronidase and acid phosphatase. The smaller deposits of azo dye or lead sulphide represent sites of lysosomal enzymes, and the larger deposits of azo dye or lead sulphide lie in autophagic vacuoles. Diffuse precipitates of azo dye found in the cytoplasm in the absence of exogenous substrate for β-glucuronidase were found to be attributable to β-glucuronidase activity; this indicated the presence of endogenous substrate(s) the possible identity of which is discussed.
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Poole, A.R. Histochemical studies of the activities and locations of β-glucuronidase and acid phosphatase in the Guerin T8 epithelioma. Histochem J 2, 343–351 (1970). https://doi.org/10.1007/BF01005002
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DOI: https://doi.org/10.1007/BF01005002