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  • 1
    Electronic Resource
    Electronic Resource
    Physical properties and function of phallolysin (1983)
    s.l. : American Chemical Society
    Biochemistry 22 (1983), S. 4574-4580 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00288a035
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  • 2
    Electronic Resource
    Electronic Resource
    Tissue-type transglutaminase expression in the Dunning tumor (1993)
    Springer
    Urological research 21 (1993), S. 9-15 
    Details
    ISSN: 1434-0879
    Keywords: Dorsal prostate ; Enzyme activity ; Immunohistochemistry ; Mammary gland ; Secretory transglutaminase ; Tissue-type transglutaminase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Transglutaminases with different functions and tissue distribution patterns can be distinguished by specific antibodies and by inhibition of enzyme activity in the presence of guanosine triphosphate (GTP). The most common form is the so-called tissue-type transglutaminase that is apparently involved in membrane, stabilization processes, e.g. during apoptosis, and can be inhibited by incubation with GTP at low calcium concentrations. A secretory transglutaminase that cannot be inhibited by GTP is synthesized in an androgen-dependent manner in the dorsal prostate of the rat, the site suggested to represent the origin of the Dunning tumor used as an experimental model in prostate cancer research. Here we studied the expression of transglutaminases in different Dunning tumor lines — mainly in the highly differentiated H subline - and characterized the enzyme both biochemically and immunocytochemically. A very high enzyme activity was found only in the less well differentiated HI-F tumor line. Immunohistochemical reactions and Western blot analysis showed that there is no secretory transglutaminase present in any of the Dunning tumor lines studied. Transglutaminase activity of the Dunning tumor results from the so-called tissue-type enzyme that is nonorgan specific. The absence of a secretory form of transglutaminase does not suport the contention of a prostatic origin o the Dunning tumor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00295185
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  • 3
    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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  • 4
    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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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Arterial $$Pa_{CO_2 }$$ during chronic hyperthermia in sheep (1980)
    Springer
    Pflügers Archiv 384 (1980), S. 143-147 
    Details
    ISSN: 1432-2013
    Keywords: Acid-base balance ; pHa ; Bicarbonate ; Thermal polypnea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract This study was undertaken to determine if the decrease in $$Pa_{CO_2 }$$ and the concomitant increase in pHa seen during acute (less than 24 h) hyperthermia in all mammals was modified when the hyperthermia was maintained for periods longer than 1 day. Catheters were placed in the descending aortas of anesthetized ewes (pentobarbital, 30 mg/kg, i.v.). After recovery from the surgery, arterial blood samples were drawn daily during a 7 day control period and an 8 day period of continuous hyperthermia. In all animals $$Pa_{CO_2 }$$ decreased and remained low during the entire hyperthermic period. $$Pa_{CO_2 }$$ (torr) andT r (°C) were inversely correlated by the equation: $$Pa_{CO_2 }$$ = −6.08T r+267.8 (r=0.84). There was an initial alkalosis with hyperthermia, however pH tended to decrease after the fifth day of hyperthermia. Calculated bicarbonate decreased during hyperthermia. The evidence suggested that when body temperature was increased in sheep, $$Pa_{CO_2 }$$ was maintained at a lower value. The low $$Pa_{CO_2 }$$ value was maintained independent of changes in pHa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00584430
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  • 8
    Electronic Resource
    Electronic Resource
    Sulfhydryl oxidase immunoreactivity in seminiferous tubules of infertile men (1992)
    Springer
    Cell & tissue research 267 (1992), S. 209-214 
    Details
    ISSN: 1432-0878
    Keywords: Testis ; Sulfhydryl oxidase ; Hypospermatogenesis ; Sertoli cell integrity ; Immunocytochemistry ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sulfhydryl oxidase (SOx) immunoreactivity was investigated in the seminiferous epithelium of human biopsy material from the testes of 33 adult men with disturbed fertility. SOx immunoreactivity was expressed in normal seminiferous epithelium in type-A spermatogonia (27±4% of all spermatogonia) (n=4), in spermatocytes and round spermatids. Mature spermatozoa as well as Sertoli cells were unlabelled. within the interstitium, Leydig cells were immunopositive. In biopsies of oligozoospermic men showing hypospermatogenesis (n=24), an increase in labelled spermatogonia up to more than 90% was observed in biopsies, where seminiferous epithelia revealed only spermatogonia and Sertoli cells. Within the group of oligozoospermic patients there was a significant increase of labelled spermatogonia from 43±13% (〉20 mill/ejaculate) (n=7) to 55±16% ( 20 and 〉20 mill/ejaculate) (n=6) to 68±8% (〈5 mill/ejaculate) (n=11) and a significant (P=0.01) decrease of score count from 7.0±2.7 to 2.0±1.8. In this group the increase of labelled spermatogonia was correlated with sperm concentrations in the ajaculate (correlation coefficient: r=-0.6). In biopsies of azoospermic patients showing maturation arrest at the level of spermatocytes or spermatids (n=5) the percentage of labelled spermatogonia was within the range of 24% to 59%. Immunoreactivity in Sertoli cells was only found in single degenerating cells and in tubules showing Sertoli Cell Only Syndrome (SCO) without lumen formation. Sertoli cells within immature seminiferous cords were immunonegative, indicating that Sertoli cell SOx immunoreactivity is rather a sign of physiological alterations in degenerating cells than dependent on the stage of differentiation. Leydig cells did not show changes of immunoreactivity in any biopsy. It is concluded that SOx expression in spermatogonia may serve as a marker for spermatogenic efficiency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00302957
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  • 9
    Electronic Resource
    Electronic Resource
    Immunohistochemical distribution of sulfhydryl oxidase in the human testis (1991)
    Springer
    Cell & tissue research 266 (1991), S. 23-28 
    Details
    ISSN: 1432-0878
    Keywords: Testis ; Spermatogenesis ; Leydig cells ; Sulfhydryl oxidase ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sulfhydryl oxidase (SOx) is an enzyme that catalyzes the oxidation of sulfhydryl compounds. It is present in mitochondria of certain testicular cells at specific stages of functional activation. In the mature human testis moderate SOx immunoreactivity is found in Leydig cells, and lacking in Sertoli and in peritubular cells. The Adark spermatogonia usually contain immuno-reactive mitochondria, while in Apale spermatogonia immunoreactivity is mostly low. In stage V of spermatogenesis, Apale spermatogonia were found containing immunoreactive material. Leptotene (stages IV and V) and zygotene (stage VI) primary spermatocytes display a moderate immunoreaction. It is strongest in pachytene spermatocytes of stages I–IV, decreases in stage V, and is low during diakinesis and in secondary spermatocytes. Late spermatids usually show a stronger immunoreactivity than early spermatids. At stage V of spermatogenesis the late spermatids contain only few immunoreactive particles. Spermatozoa are free of SOx-immunoreactive mitochondria. In residual bodies small amounts of SOx-immunoreactive particles are seen. Compared to rat and hamster testis, SOx immunoreactivity of the human testis is less clearly stage-dependent and it is not confined to certain germ cell stages. As deduced from the findings in patients with spermatogenic disorders, the SOx immunoreactivity of spermatogonia in human testis seems to be of diagnostic relevance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00678707
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  • 10
    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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