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  • 1
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of seminal proteins in salivary and lacrimal glands of the rat (1995)
    Springer
    Cell & tissue research 280 (1995), S. 171-181 
    Details
    ISSN: 1432-0878
    Keywords: Salivary glands ; Lacrimal gland ; Male accessory sex glands ; Immunohistochemistry ; Androgen-dependent protein secretion ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Antibodies against 10 different secretory proteins from the accessory sex glands of the male rat were used for immunohistochemical studies of salivary and lacrimal glands from intact and castrated rats, at the light- and electron-microscopic levels. In the parotid gland, secretory acinar cells showed immunoreactivity with antibodies against prostatic binding protein, cystatin-related peptide and acid phosphatase (isoenzyme pI 8.0; 5.6) typical of ventral prostate, and seminal vesicle secretion VI. Western blotting analysis indicated that immunoreactivity against prostatic binding protein was attributable to a subunit, presumably C3. Acid phosphatase pI 5.6 showed a molecular weight of 66 kDa, which is at variance with the prostatic form. Immunoreactivity for secretory transglutaminase, derived from the coagulating gland, was restricted to myoepithelial and stromal cells. In castrated animals, the immunoreactivity of acinar cells was reduced to the background level, whereas stromal transglutaminase immunoreactivity was unaltered. The distribution pattern of immunoreactivity for the proteins mentioned was almost identical in the lacrimal gland. Significant differences were however observed in the immunoreactivity of the inframandibular gland, where serous glandular cells were non-immunoreactive for seminal proteins, with the exception of acid phosphatase isoenzyme pI 8.0. Granules present in the convoluted granular ducts were immunoreactive particularly for acid phosphatase (isoenzyme pI 5.6)but much less for cystatin-related peptide; immunoreactivity was reduced after castration. The straight portion of the inframandibular duct system was immunoreactive for transglutaminase, but no influence of castration was visible. The distribution of immunoreactivity for seminal proteins present in the salivary and lacrimal glands and the pronounced androgen-dependence of their expression point to functional relationships of the respective proteins at both glandular sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00304522
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of seminal proteins in salivary and lacrimal glands of the rat (1995)
    Springer
    Cell & tissue research 280 (1995), S. 171-181 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Salivary glands ; Lacrimal gland ; Male accessory sex glands ; Immunohistochemistry ; Androgen-dependent protein secretion ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Antibodies against 10 different secretory proteins from the accessory sex glands of the male rat were used for immunohistochemical studies of salivary and lacrimal glands from intact and castrated rats, at the light- and electron-microscopic levels. In the parotid gland, secretory acinar cells showed immunoreactivity with antibodies against prostatic binding protein, cystatin-related peptide and acid phosphatase (isoenzyme pI 8.0; 5.6) typical of ventral prostate, and seminal vesicle secretion VI. Western blotting analysis indicated that immunoreactivity against prostatic binding protein was attributable to a subunit, presumably C3. Acid phosphatase pI 5.6 showed a molecular weight of 66 kDa, which is at variance with the prostatic form. Immunoreactivity for secretory transglutaminase, derived from the coagulating gland, was restricted to myoepithelial and stromal cells. In castrated animals, the immunoreactivity of acinar cells was reduced to the backgroun d level, whereas stromal transglutaminase immunoreactivity was unaltered. The distribution pattern of immunoreactivity for the proteins mentioned was almost identical in the lacrimal gland. Significant differences were however observed in the immunoreactivity of the inframandibular gland, where serous glandular cells were non-immunoreactive for seminal proteins, with the exception of acid phosphatase isoenzyme pI 8.0. Granules present in the convoluted granular ducts were immunoreactive particularly for acid phosphatase (isoenzyme pI 5.6) but much less for cystatin-related peptide; immunoreactivity was reduced after castration. The straight portion of the inframandibular duct system was immunoreactive for transglutaminase, but no influence of castration was visible. The distribution of immunoreactivity for seminal proteins present in the salivary and lacrimal glands and the pronounced androgen-dependence of their expression point to functional relationships of the respective proteins at both gla ndular sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00304522
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  • 3
    Electronic Resource
    Electronic Resource
    Distribution and subcellular localization of a lysosome-associated protein in human genital organs (1997)
    Springer
    Cell & tissue research 287 (1997), S. 335-342 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Lysosomal membrane antigen ; Immunohistochemistry ; Biosynthesis ; Prostate-membrane-specific antigen ; Apocrine secretion ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The tissue distribution, preferentially in the human male genital system, and the subcellular localization of the lysosome-associated membrane protein 2 (lamp 2) was studied immunohistochemically using a mouse monoclonal antibody, 2D5. Strong immunoreactivity was present in the tubular system of the kidney, in acinar cells of salivary glands and pancreas, prostate, mammary glands, placenta and in cutaneous sweat glands. Moderate immunoreactivity was observed in cerebral neuronal cells, epidermal cells, testis, epididymis, seminal vesicle and endometrium. Very low immunoreactivity was found in liver. In some of the tissues mentioned, the distribution pattern of immunoreactivity is smooth and homogeneous, while in others it is granular and concentrated in the supra- or perinuclear cytoplasm. The subcellular distribution was studied on ultracryosections and on pre-embedding-processed chopper sections of human prostate. In the latter gland, the protein is not restricted to epithelium, but is also present in stromal cells. Ultrastructurally, the immunoreactivity in secretory cells was localized in electron-translucent vacuoles and granules, including the secretory granules. A close association with cell membranes was not generally the case. Only part of the immunoreactive material was linked to the apical plasma membrane pointing to a biosynthesis independent from an association step with the apical plasma membrane. As shown by immunoelectron microscopy and Western blotting, a high amount of lamp 2 is secreted and is found in so-called prostasomes. The findings indicate that in the human prostate most of the membrane-bound lamp 2 is released from the secretory cells, presumably in an apocrine fashion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050758
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  • 4
    Electronic Resource
    Electronic Resource
    Experimental studies of apocrine secretion in the dorsal prostate epithelium of the rat (1979)
    Springer
    Cell & tissue research 198 (1979), S. 145-158 
    Details
    ISSN: 1432-0878
    Keywords: Dorsal prostate gland ; Rat ; Apocrine secretion ; Prolactin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rat dorsal prostate epithelium was studied in intact adult animals, in animals castrated for three days and in rats after inhibition of prolactin secretion. Thin sections, electron-microscopic autoradiographs and freeze-fracture replicas were used to analyze the process of apocrine secretion in this gland. The rough endoplasmic reticulum and the Golgi apparatus of the secretory cells are well developed, but secretory granules are absent. The only sign indicating release of secretory material is the appearance of blebs originating from the apical plasma membrane. Freeze-fracture replicas of the apical plasma membrane reveal that the blebs develop randomly from the bases of microvilli-like protrusions. In vitro pulse labeling of the proteins using 3H-leucine resulted in a labeling of the apical blebs. A post-castration period of three days was sufficient to reduce drastically the number and size of the apical blebs concomitant with regressive changes of the cell. Suppression of prolactin secretion for three weeks by application of lisuride, a synthetic ergot alkaloid, also induced regressive changes in the secretory cells. The apical blebs were still present, but they were shrunken and their content appeared condensed. These experimental conditions proved that the apical blebs are closely related to the functional activity of the cells and are interpreted as true apocrine secretion in the rat dorsal epithelium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00234842
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  • 5
    Electronic Resource
    Electronic Resource
    p-Chlorophenylalanine-induced proliferation of the seminal vesicle epithelium (1981)
    Springer
    Cell & tissue research 219 (1981), S. 159-172 
    Details
    ISSN: 1432-0878
    Keywords: Seminal vesicles ; Proliferation ; Autoradiography ; Biochemistry ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Intraperitoneal injection of p-chlorophenylalanine (pCPA) methylester (100 mg/kg body weight) results in an activation of the lysosomal system of the secretory cells in the rat seminal vesicle and an elevation of the activities of lysosomal enzymes within 15 min following the injection. Large autophagic vacuoles are formed, sequestering rough endoplasmic reticulum and part of the Golgi apparatus within 2 h. Shortly after the activation of the lysosomal system an elevation of both DNA and protein synthesis is measured biochemically. 6 h subsequent to the injection a wave of mitoses of the secretory cells begins, reaching a maximum 6 h later and then declining within 3 h. About 12 h following the injection a second rise in lysosomal activity begins, declining within 24 h. The entire sequence of lysosomal and proliferative activities is inhibited in antiandrogen-pretreated rats. Deduced from these findings the following hypothesis of growth regulation of the accessory sex glands is advanced: enhanced loss of intracellular material during autophagocytosis diminishes the intracellular concentration of a substance curtailing cell division below its effective threshold resulting in division of the secretory cells. The prerequisites of this mechanism are (i) a sufficient distributive capacity of the stroma for hormones (androgens) and metabolic precursors, and (ii) sufficient capacity of the basal cells for transporting the precursors to the secretory cells. Sloughing of the secretory cells separates them from these auxiliary structures (stroma and basal cells) and enables the basal cells to divide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00210025
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