Synopsis
Four acid hydrolases in the secretory cells and the sebum of the preputial sebaceous gland of the rat were incestigated cytochemically. A strong β-glucuronidase activity was found to occur in the matrix of the perinuclear secretion granules, whereas the granule crystalloids were unreactive. The distribution of acid phosphatase at the light microscope level was similar, though the intensity of the reaction was lower and the number of positive granules smaller. By electron microscopy, the final reaction product of acid phosphatase occurred in patches at the periphery of the granule matrix, as well as in the vesicles adjoining the Golgi stacks, from which the perinuclear granules seemed to arise. In the sebum, the two hydrolases occurred in the background material between the unstained crystalloid masses. There was noN-acetyl-β-glucosaminidase or aryl sulphatase activity in the gland. The perinuclear granules appear to be secretory lysosomes which, after discharge from the disaggregating cell, release their acid hydrolases into the sebum.
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References
Barka, T. &Anderson, P. J. (1962). Histochemical methods for acid phosphatase using hexazonium pararosaniline as coupler.J. Histochem. Cytochem. 10, 741–53.
Barka, T. &Anderson, P. J. (1963).Histochemistry: Theory, Practice, and Bibliography, p. 240. New York: Harper & Row.
Beaver, D. L. (1963). Electron microscopy of the acinar cell of the rat preputial gland.Anat. Rec. 146, 47–59.
Beyler, A. L. &Szego, C. M. (1951). Endocrine regulation of beta-glucuronidase activity.Am. J. Physiol. 167, 768.
Brandes, D., Bertini, F. &Smith, E. W. (1965). Role of lysosomes in cellular lytic processes. II. Cell death during holocrine secretion in sebaceous glands.Exper. mol. Path. 4, 245–65.
Conchie, J. &Findlay, J. (1959). Influence of gonadectomy, sex hormones and other factors, on the activity of certain glycosidases in the rat and mouse.J. Endocr. 18, 132–46.
Conchie, J., Findlay, J. &Levvy, G. A. (1959). Mammalian glycosidases. Distribution in the body.Biochem. J. 71, 318–25.
Dangelo, J. G. &Munger, B. L. (1964). The ultrastructure of the rat preputial gland.J. Ultrastruct. Res. 11, 230–45.
De Duve, C. (1963). The lysosome concept. In:Lysosomes, Ciba Foundation Symposium. London: Churchill.
Dingle, J. T. (1969). The extracellular secretion of lysosomal enzymes. In:Lysosomes in Biology and Pathology. Amsterdam & London: Dingle-Fell.
Ehrenreich, J. H., Bergeron, J. J. M., Siekevitz, P. &Palade, G. E. (1973). Golgi fractions prepared from rat liver homogenates. I. Isolation procedure and morphological characterization.J. Cell Biol. 59, 45–72.
Etherton, J. E. &Botham, C. M. (1970). Factors, affecting lead capture methods for the fine localization of rat lung acid phosphatase.Histochem. J. 2, 507–19.
Fishman, W. H. & Ide, H. (1967). The de novo synthesis of the endoplasmic reticulum glycoprotein, β-glucuronidase, in androgen-stimulated mouse kidney.Seventh International Congress on Biochemistry, Tokyo, 19–25 August, p. 858.
Goldfischer, S. (1965). The cytochemical demonstration of lysosomal aryl sulfatase activity by light and electron microscopy.J. Histochem. Cytochem. 13, 520–3.
Goldfischer, S., Kikkawa, Y. &Hoffman, L. (1968). The demonstration of acid hydrolase activities in the inclusion bodies of type II alveolar cells and other lysosomes in the rabbit lung.J. Histochem. Cytochem. 16, 102–9.
Hayashi, M. (1964). Distribution of β-glucuronidase activity in rat tissues employing the naphthol AS-BI glucuronide hexazonium pararosanilin method.J. Histochem. Cytochem. 12, 659–69.
Hayashi, M. (1965). Histochemical demonstration ofN-acetyl-β-glucosaminidase employing napthol AS-BIN-acetyl-β-glucosaminide as substrate.J. Histochem. Cytochem. 13, 355–60.
Hayashi, M. (1967). Comparative histochemical localization of lysosomal enzymes in rat tissues.J. Histochem. Cytochem. 15, 83–92.
Helminen, H. J. &Ericsson, J. L. E. (1970). On the mechanism of lysosomal enzyme secretion. Electron microscopic and histochemical studies on the epithelial cells of the rat's ventral prostate lobe.J. Ultrastruct. Res. 33, 528–49.
Levvy, G. A., Mcallan, A. &Marsh, C. A. (1958). Purification of β-glucuronidase from the preputial gland of the female rat.Biochem. J. 69, 22–7.
Linker, A., Meyer, K. &Weissmann, B. (1955). Enzymatic formation of monosaccharides from hyaluronate.J. biol. Chem. 213, 237–48.
Mesquita-Guimarães, J. &Coimbra, A. (1974). The perinuclear secretion granules of the rat preputial gland. An electron microscope cytochemical study.J. Ultrastruct. Res. 47, 242–54.
Miller, B. S. &Palade, G. E. (1964). Lytic activities in renal protein absorption droplets. An electron microscopical study.J. Cell Biol. 23, 519–52.
Novikoff, P. M., Novikoff, A. B., Quintana, N. &Hauw, J-J. (1971). Golgi apparatus, GERL, and lysosomes of neurons in rat dorsal root ganglia, studied by thick section and thin section cytochemistry.J. Cell Biol. 50, 859–86.
Peracchia, C. &Mittler, B. S. (1972) Fixation by means of glutaraldehyde-hydrogen peroxide reaction products.J. Cell Biol. 53, 234–8.
Rowden, G. (1968). Aryl sulfatase in the sebaceous glands of mouse skin. A combined electron microscope and cytochemical study.J. Invest. Derm. 51, 41–50.
Thyberg, J. &Friberg, U. (1970). Ultrastructure and acid phosphatase activity of matrix vesicles and cytoplasmic dense bodies in the epiphyseal plate.J. Ultrastruct. Res. 33, 554–73.
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Mesquita-Guimarães, J., Coimbra, A. Acid hydrolases in the perinuclear secretion granules of the rat preputial gland. A light and electron microscope study. Histochem J 6, 685–692 (1974). https://doi.org/10.1007/BF01011508
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DOI: https://doi.org/10.1007/BF01011508