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  • 1
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    Immunohistochemistry of secretory transglutaminase from rodent prostate (1990)
    Springer
    Details
    Publication Date: 1990-03-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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  • 2
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    Cytochemistry and biochemistry of acid phosphatases (1980)
    Springer
    Details
    Publication Date: 1980-01-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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  • 3
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    Intermediate filaments in sertoli cells (1992)
    Wiley
    Details
    Publication Date: 1992-01-01
    Print ISSN: 1059-910X
    Electronic ISSN: 1097-0029
    Topics: Natural Sciences in General
    Published by Wiley
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of endogenous and exogenous 5′-nucleotidase on bovine spermatozoa (1994)
    Springer
    Histochemistry and cell biology 101 (1994), S. 253-262 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A polyclonal rabbit antibody against 5′-nucleotidase purified from bull seminal plasma was used to localize the antigen on bovine spermatozoa. Spermatozoa taken from the ampulla of the vas deferens showed strong immunofluorescence at the anterior rim of the head portion. Evaluation of spermatozoa prepared from different segments of the seminal pathway indicated the presence of the antigen already in rete testis and epididymal spermatozoa. On cryostat sections of testis tissue a positive immunoreaction was found in the anterior head portion of elongated spermatids, but not in earlier forms of sperm development. This distribution corresponded with the enzyme activity and results of Western blotting in extracts of testicular and epididymal spermatozoa. Immunoelectron microscopy of ampullary spermatozoa using antibody detection with gold-labelled anti-rabbit IgG showed a clear-cut labelling of the plasma membrane in the acrosome region. Treatment of ampullary spermatozoa with 0.1% Triton X-100 did not completely remove the immunoreactive material from the acrosome, showing a very stable linkage of the protein to the plasma membrane. Treatment with phospholipase C from Bacillus thuringiensis, however, removed immunoreactive material from the plasma membrane, indicating its binding by a phosphoinositol anchor. Our findings show that endogenous 5′-nucleotidase is present on the plasma membrane covering the anterior head portion of bovine spermatozoa and indicate specialized functions during the acrosomal reaction. Soluble enzyme derived from seminal vesicle secretion covers the whole sperm surface during emission, but is not covalently bound. It provides generalized enzyme activity to the sperm surface in addition to the specialized area of the sperm head.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315912
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  • 5
    Electronic Resource
    Electronic Resource
    Cytochemistry and biochemistry of acid phosphatases (1980)
    Springer
    Histochemistry and cell biology 67 (1980), S. 99-111 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Acid phosphatases of the rat ventral prostate were studied cytochemically using different substrates. The results were compared to findings on isoelectric focussing gels stained for acid phosphatase activity. This is a highly specific and reproducible method which allows the distinction between secretory androgen-dependent and lysosomal acid phosphatases. Activity of lysosomal acid phosphatase was increased after castration, while the activity of the secretory enzyme gradually decreased after androgen deprivation. None of the substrates tested was selectively hydrolyzed by either secretory or lysosomal acid phosphatase. Phenylphosphate, creatine phosphate and choline phosphate were found to be inappropriate substrates for histochemical purposes, however, reproducible results were obtained with α-naphthylphosphate, β-glycerophosphate and p-nitrophenylphosphate. The method of isoelectric focussing (pH range 4.0–8.0) of enzymes with subsequent histochemical staining demonstrated lysosomal enzymes at pH 7.9 and 8.2 respectively. Small amounts of identical enzymes were found in liver, kidney, blood or epididymis. Secretory acid phosphatases were focussed at pH 5.5, 5.6, 5.65 and 7.15. Similar enzymes have been identified in epididymis, kidney, liver and pancreas. These results indicate that 1) at present no “specific” substrate for prostatic secretory or lysosomal acid phosphatases is available and 2) that no prostate-specific “prostatic acid phosphatase (PAP)” exists in the rat ventral prostate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490092
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  • 6
    Electronic Resource
    Electronic Resource
    Intracellular localization of prostatic binding protein (PBP) in rat prostate by light and electron microscopic immunocytochemistry (1982)
    Springer
    Histochemistry and cell biology 76 (1982), S. 497-516 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Extra- and intracellular distribution of Prostatic Binding Protein (PBP) was studied in the different genital organs of the male rat by immunocytochemistry at the light and electron microscopic levels. PBP was extracted from cytosols of rat ventral prostate and used for immunization of rabbits. The specificity of the antiserum raised was tested by “western blotting” and immunoelectrophoresis. From the different fixatives tested for optimal structural and antigenic preservation of the ventral prostate a mixture containing 2.5% paraformaldehyde, 0.5% glutaraldehyde and 0.5% CaCl2 in cacodylate buffer, 0.05 M, pH 7.3 was selected. Using the immunofluorescence technique and the unlabeled antibody enzyme method PBP-immunoreactivity was detected at the light microscopic level in the luminal secretions of the ventral prostate. No reaction was observed with the seminal vesicle, the coagulating gland, the dorsal and lateral prostates, the epididymis and the testis. Intracellular secretory granules reacting with PBP antiserum were exclusively found in the secretory cells of the ventral prostate. Insufficiently fixed cells showed a diffuse generalized reaction of the cytoplasm indicating a leakage of the antigen from the secretory granules. Such artifacts were common in tissue sections processed with the preembedding-staining procedure. At the ultrastructural level therefore mostly the postembedding staining method was performed using both the unlabeled antibody enzyme method and the ferritin-labeled immunoglobulin technique in osmicated, Epon-embedded tissue. Labeling with either method was intense in the secretory granules and the condensing vacuoles, while the labeling density of the rough endoplasmic reticulum and the Golgi cisternae was in the background range. Castration experiments showed that secretory material displaying PBP immunoreactivity was retained within the acinar lumen of the gland for several days after castration, but was absent from most secretory cells already by four days after castration. Immunocytochemistry of PBP therefore is a very sensitive method for analysing the secretory activity and its androgen dependence of the prostate of the rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489905
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  • 7
    Electronic Resource
    Electronic Resource
    Immunohistochemistry of secretory transglutaminase from rodent prostate (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 525-530 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Transglutaminases are Ca2+-dependent intra-and extracellular enzymes catalyzing the cross-linking between proteins and/or polyamines, thereby eliciting divergent physiological effects such as fibrin clot stabilization or hair follicle cross-linking. A secretory transglutaminase (EC 2.3.2.13) was isolated from the coagulating gland of the rat. The protein is highly glycosylated. A fraction purified to homogeneity was used as an antigen to raise polyclonal antibodies in rabbits. These antibodies were used to identify the secretion sites of the protein within the male accessory sex glands as well as to study the immunological relationships of the respective antigen within different organs of different species. In the rat, the coagulating gland and likewise the dorsal prostate gave a positive immunoreaction. In the guinea pig, a closely related protein was detected in the anterior prostate. No cross-reactivity was found with membrane-bound transglutaminase from liver, erythrocytes or blood clotting factor XIIIa. The intraluminal secretion of the aforementioned glands was only weakly stained. No secretory granules were observed in the glandular epithelium but instead bleb-like structures reminiscent of apocrine secretion. A slight background stain of the epithelium remained even in castrated animals where secretion is largely suppressed. The background stain is attributed to a tissue-type, membrane-bound, non-secretory transglutaminase that is not androgen dependent, but instead synthesized only after androgen deprivation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266412
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  • 8
    Electronic Resource
    Electronic Resource
    Stage-dependent appearance of sulfhydryl oxidase during spermatogenesis in the testis of rat and hamster (1990)
    Springer
    Histochemistry and cell biology 94 (1990), S. 365-371 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sulfhydryl oxidase (SOx), an enzyme that catalyzes the oxidation of sulfhydryl compounds, appears in the spermatogenic cells of rat and hamster testes in a stage-dependent manner. It first appears in pachytene spermatocytes at stage I in both the animal species studied. SOx immunoreactivity is associated with mitochondria of these cells. The fate of such mitochondria is species-dependent. In rat, the immunoreactive mitochondria aggregate during maturation phase and are retained in the residual bodies. Spermatozoa free of SOx are released into the lumen. On the other hand, in hamster, the immunoreactive mitochondria arrange themselves around the midpiece of spermatozoa. In such a case, residual bodies lack SOx. The appearance of SOx coincides with the appearance of LDH-X in the spermatogenic cells. Like many other proteins such as LDH-X, RSA-1 and cytochrome ct, SOx provides yet another example of differential gene activation associated with a developmental process of gametes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266442
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  • 9
    Electronic Resource
    Electronic Resource
    Basal cells of H-Dunning tumor are myoepithelial cells (1991)
    Springer
    Histochemistry and cell biology 95 (1991), S. 341-349 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Recent immunohistochemical studies have shown that basal cells in human prostatic epithelium are not myoepithelial cells. Since in the literature the Dunning tumor, originally described as a rat prostate carcinoma derived from the dorsolateral prostate of a Copenhagen rat, was reported to have myoepithelial cells, a comparative immunohistochemical and ultrastructural study was performed in the H-, HIF- and AT3-lines of the Dunning tumor, the male accessory sex glands (ventral, dorsal, lateral prostate, coagulating gland, bulbourethral gland) and the mammary gland of both Copenhagen and Wistar rats. Mono- and polyclonal antibodies directed against intermediate filament proteins (cytokeratin, desmin, vimentin) and the contractile proteins (α-actin, muscle type specific myosin, tropomyosin) were used along with phalloidin decoration of F-actin. As in the human prostate, none of the rat prostate lobes in either strain did contain basal cells expressing cytokeratin along with α-actin, myosin and tropomyosin. Cells representing fully differentiated myoepithelial cells, however, were present as anticipated in the mammary gland, the bulbourethral gland and the H-tumor line of the Dunning tumor. This finding is difficult to reconcile with the contention of a prostatic origin of the H-Dunning tumor. Further studies are required to classify the epithelial parental tissue in order to define the true origin of the H-Dunning tumor and the tumor lines derived thereof.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266961
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  • 10
    Electronic Resource
    Electronic Resource
    Intermediate filaments in sertoli cells (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 20 (1992), S. 50-72 
    Details
    ISSN: 1059-910X
    Keywords: Vimentin ; Cytokeratin ; Testis ; Cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Using immunohistochemical techniques both at light and electron microscopic levels, the arrangement and distribution of intermediate filaments in Sertoli cells of normal testis (in rat and human), during pre- and postnatal development (in rabbit, rat, and mouse) and under experimental and pathological conditions (human, rat), have been studied and related to the pertinent literature. Intermediate filaments are centered around the nucleus, where they apparently terminate in the nuclear envelope providing a perinuclear stable core area. From this area they radiate to the plasma membranes; apically often a close association with microtubules is seen. Basally, direct contacts of the filaments with focal adhesions occur, while the relationship to the different junctions of Sertoli cells is only incompletely elucidated. In the rat (not in human) a group of filaments is closely associated with the ectoplasmic specializations surrounding the head of elongating spermatids. Both in rat and human, changes in cell shape during the spermatogenic cycle are associated with a redistribution of intermediate filaments. As inferred from in vitro studies reported in the literature, these changes are at least partly hormone-dependent (vimentin phosphorylation subsequent to FSH stimulation) and influenced by local factors (basal lamina, germ cells). Intermediate filaments, therefore, are suggested to be involved in the hormone-dependent mechanical integration of exogenous and endogenous cell shaping forces. They permit a cycledependent compartmentation of the Sertoli cell into a perinuclear stable zone and a peripheral trafficking zone with fluctuating shape. The latter is important with respect to the germ cell-supporting surface of the cell which seems to limit the spermatogenetic potential of the male gonad.
    Additional Material: 64 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070200107
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