Cytochemistry and biochemistry of acid phosphatases VI: Immunoelectron microscopic studies on human prostatic and leukocytic acid phosphatases

Abstract

Using different antisera against secretory and lysosomal prostatic acid phosphatases, the localization of the respective antigens was studied in the human prostate at the ultrastructural level. Secretory acid phosphatase was confined exclusively to the secretory vacuoles of the glandular cells. Discharge of the secretory material occurs in a merocrine type of secretion. The identical antigen could be localized in the primary and secondary granules of neutrophil and eosinophil granulocytes separated from human peripheral blood. The antiserum used was also cross-reactive with the canine prostate, where a very distinct immunoreaction was observed with the secretory granules of the glandular cells. The antibodies directed against lysosomal acid phosphatases prepared from prostatic homogenates consistently gave a positive immunoreaction with dense bodies, lipofuscin, and secretory granules. The respective antigens were present also in neutrophil and eosinophil granulocytes. These findings do not identify the existence of a prostate-specific acid phosphatase, which does not exist. The secretory form of the isoenzymes, however, is clearly distinct from the lysosomal form, both of which are present in granulocytes. Therefore the origin of acid phosphatases elevated in peripheral blood in cases of metastatic prostatic cancer could be either the carcinomatous cells or leukocytes destroyed during the process of metastasis.

Cytochemistry and biochemistry of acid phosphatases VII: Immunohistochemistry of canine prostatic acid phosphatase

“…Our antibody against canine prostatic acid phosphatase was similarly specific, binding exclusively to mature secretion granules but no other cytoplasmic organelles. This labeling pattern was identical with that previously described in the human gland [28] and likewise for rat prostate acid phosphatase (Seitz and Aumiiller, unpublished) or prostatic binding protein secreted by the rat ventral prostate [37,38]. The labeling of the Golgi apparatus, however, as described by Song et al [39], is presumably due to low fixation quality, allowing a redistribution of the antigen.…”

“…Their figures, however, indicate that not only secretory granules were stained; instead, some immunofluorescence was found in the basal and perinuclear cytoplasm. Another xenospecific antibody directed against human prostatic secretory acid phosphatase applied to canine prostate in our previous immunoelectron microscopic study [28] gave a strong and highly specific labeling of secretion granules within the glandular cells, whereas labeling of other cytoplasmic organelles was in the background range. Our antibody against canine prostatic acid phosphatase was similarly specific, binding exclusively to mature secretion granules but no other cytoplasmic organelles.…”

“…Prof. F. Sinowatz, Department of Veterinary Histology, University of Munich, kindly provided us with five specimens of canine prostatic carcinoma. Human prostatic tissue, either Bouin-fixed and paraffin-embedded or glutaraldehyde-fixed and epon-embedded, was available from our previous studies [4,28].…”

Pharmacologically induced ultrastructural and lmmunohistochemical changes in the prostate of the castrated dog

“…Sections were cut at 5 pm thickness and mounted on chromalum gelatine-coated glass slides. The following antigens were visualized immunohistochemically according to Sternberger et a1 [5] using monospecific commercial antisera (Dako, Copenhagen, Denmark; Boehringer, Mannheim, Federal Republic of Germany) : vimentin, desmin, canine secretory acid phosphatase [6] and cross-reactive human acid phosphatase [7]. Control incubations were done using preimmune sera or antibovine serum albumin.…”

Arylsulfatase B Is Present in Crystalloid-Containing Granules of Human Eosinophil Granulocytes

“…Activation might occur during the formation of small granules from crystalloid-containing ones or during vesicular transport o f the contents derived from crystalloidcontaining granules. There is an analogy with acid phospha tase, which is enzymatically masked in unstimulated eosi nophils, although the enzyme can be shown to be present by antibodies [16,17].…”