PubMed Health⌕ Search

Biomedical subjects

J Seitz

Publications and source records attributed to J Seitz.

At least 109 records · Page 6Linked to original sources
PubMed1991

Immunohistochemical localization of testicular sulphydryloxidase during sexual maturation of the Djungarian hamster (Phodopus sungorus).

Immunohistochemical localization of sulphydryloxidase was examined in the testis of the Djungarian hamster from Day 0 to Day 31 of post-natal development. The sulphydryloxidase antibody labelled prespermatogonia and the first population of spermatogonia type A within the seminiferous epithelium. Additionally, Sertoli cells exhibited immunoreactivity from Day 2 to Day 11 after birth. From Day 11 onwards, sulphydryloxidase immunoreactivity was found in germ cells after the initiation spermatogenesis from pachytene primary spermatocytes, showing the highest intensity in mid-pachytene spermatocytes. The pattern of sulphydryloxidase expression during spermatogenesis was identical to that found in adult animals. It is concluded that sulphydryloxidase immunoreactivity not only serves as a marker for early stages of spermatogenesis, especially pachytene spermatocytes, confirming earlier reports, but also for spermatogonial precursors.

Animals↗
PubMed1991

[Acute ischemia of the upper extremity caused by axillary contused trauma. Report of 3 cases].

Blunt trauma to the axillary artery is infrequently associated to unstable proximal humeral fractures or anterior dislocation of the shoulder. We report 3 patients who developed this complication. One of them had associated neurologic injury. All patients required a saphenous vein interposition graft and the patient with neurologic injury required surgical decompression of the brachial plexus. The results of arterial repair were excellent. The patient with neurologic injury recovered significantly after decompression of the plexus, since he had not partial or complete transection of the plexus which is usually a permanent lesion. Our observations support that patients with axillary lesion associated with neurologic deficits should undergo prompt exploratory surgery.

Acute Disease↗
PubMed1990

Species- and organ-specificity of secretory proteins derived from human prostate and seminal vesicles.

Polyclonal antibodies against semenogelin (SG) isolated from human seminal vesicle secretion and acid phosphatase (PAP), beta-microseminoprotein (beta-MSP), and Prostate-Specific Antigen (PSA) derived from human prostatic fluid, as well as a monoclonal antibody against beta-MSP were used for immunocytochemical detection of the respective antigens in different organs from different species. SG immunoreactivity was detected in the epithelium of the pubertal and adult human and in monkey seminal vesicle, ampulla of the vas deferens, and ejaculatory duct. PAP, beta-MSP, and PSA immunoreactivities were detected in the pubertal and adult human prostate and the cranial and caudal monkey prostate. With the exception of a weak PSA immunoreactivity in the proximal portions of the ejaculatory duct, none of the latter antisera reacted with seminal vesicle, ampullary, and ejaculatory duct epithelium. Among the non-primate species studied (dog, bull, rat, guinea pig) only the canine prostatic epithelium displayed a definite immunoreactivity with the PAP antibody and a moderate reaction with the PSA antibody. No immunoreaction was seen in bull and rat seminal vesicle and canine ampulla of the vas deferens with the SG antibody. The same was true for the (ventral) prostate of rat, bull, and dog for beta-MSP. The epithelium of the rat dorsal prostate showed a slight cross-reactivity with the monoclonal antibody against beta-MSP and one polyclonal antibody against PSA. The findings indicate a rather strict species-dependent expression of human seminal proteins which show some similarities in primates, but only marginal relationship to species with different physiology of seminal fluid.

Acid Phosphatase↗
PubMed1990

Immunohistochemistry of secretory transglutaminase from rodent prostate.

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.

Androgens↗
PubMed1990

Stage-dependent appearance of sulfhydryl oxidase during spermatogenesis in the testis of rat and hamster. An immunohistochemical study.

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.

Animals↗
PubMed1990

Distribution pattern of testicular sulphydryloxidase immuno-activity in the djungarian hamster (Phodopus sungorus) during photoperiodically induced involution and recrudescence.

The distribution pattern of testicular sulphydryloxidase (SOx) immuno-activity was investigated in the djungarian hamster during photoperiodically induced testicular involution and recrudescence. SOx immuno-activity, indicating functional integrity of labelled cells, did not change in pachytene spermatocytes and spermatids as long as these cells were present in the seminiferous epithelium. Its disappearance coincided with the degeneration of spermatocytes in phases IV and V of involution and reappeared during recrudescence, when the first spermatogenic wave had reached the pachytene stage. In tubules at phase VI of involution (showing maximal regression), the apical cytoplasm of Sertoli cells showed immuno-activity. This immuno-activity disappeared during recrudescence prior to the differentiation of pachytene spermatocytes. Changes in SOx immuno-activity resembled those of lactate dehydrogenase-X (LDH-X) in photo-inhibited testes or during puberty, indicating a close functional relationship which still remains to be elucidated. The data suggest that the hamster exposed to different photoperiods can be used as a suitable model to study the relationship between testicular morphology and function in different states of gonadal activity.

Animals↗
PubMed1990

Biochemical properties of secretory proteins from rat seminal vesicles.

The secretions of rat seminal vesicles from the so-called copulatory plug when getting in contact with the secretions of the coagulating gland. Depending on the sexual activity of the respective animal and the extraction conditions, the protein pattern of the seminal vesicle secretion varies to some extent. We have studied the biochemical properties of the proteins SVS I, SVS II, sulfhydryl oxidase and SVS III-VIII. The most interesting protein is SVS II which is the main substrate of coagulating gland transglutaminase and serves as the most important monomer during semen coagulation. It is highly soluble in acidic solutions. The monomeric polypeptide has a molecular mass of 49 kDa, is glycosylated with fucose, glucose, mannose and N-acetylated sugars and has a highly basic pI of 10.5. Particularly interesting are its functional and structural relationships with actin. It is the first described protein with actin modulating properties that is secreted in an androgen-dependent manner.

Animals↗
PubMed1990

Immunohistochemical localization of the glucocorticoid receptor in pancreatic beta-cells of the rat.

We used a monoclonal antibody against an epitope located in the N-terminal moiety of the rat glucocorticoid receptor to identify the glucocorticoid receptor-containing cells in the rat pancreas. Monospecific polyclonal antisera against insulin, glucagon, somatostatin, and amylase were applied to serial sections in colocalization studies to identify the respective endocrine and exocrine cells. Glucocorticoid receptor immunoreactivity was exclusively present in nuclei and cytoplasm of the beta-cells of pancreatic islets. Western blots using the glucocorticoid receptor antibody resulted in identical 94K immunoreactive proteins in both liver and pancreas. After adrenalectomy, the glucocorticoid receptor immunoreactivity of beta-cells decreased significantly. A computer-assisted method of semiquantitative evaluation of the glucocorticoid receptor immunoreactivity demonstrated a significant decrease in the staining intensity of the beta-cells by 23.5% and in that of insulin antibodies by 10.4%, while amylase immunoreactivity was only slightly decreased. Serum levels of corticosterone determined by RIA decreased from 225 micrograms/ml in sham-operated animals to 55 micrograms/ml in animals 14 days after adrenalectomy, while the tissue content of amylase decreased by 45%. The immunohistochemical findings give circumstantial evidence of the presence of glucocorticoid receptor in beta-cells. We interpret our data as indicating an indirect effect of glucocorticoids on amylase synthesis via a glucocorticoid-insulin-exocrine cell pathway.

Adrenalectomy↗
PubMed1990

Transglutaminase immunoreactivity in the male genital tract of the rat.

The distribution of transglutaminase immunoreactivity in the male genital system of the rat has been studied at the light and electron microscopic levels using a highly specific polyclonal antibody. The antibody is obviously secreted in an apocrine fashion in the dorsal prostate as well as the coagulating gland. This moiety is responsible for semen clotting. In addition to the secretory moiety, epididymal sperm contain endogenous immunoreactive material in the cytoplasmic droplet. Whether this is added to the sperm within the epididymis--as is the immunoreactive material on the sperm head--or already present in developing sperm has to be elucidated by further immunoelectron microscopic studies.

Animals↗
PubMed1989

Differential reaction of secretory and non-secretory proteins in hormone-treated Dunning tumor.

Tumor cells from of the Dunning R-3327 PAP tumor were grown in vivo in the flank region of male Copenhagen rats for 4 months. Untreated control animals, castrated animals, and untreated or castrated animals supplemented with testosterone and estramustine (alone or in combination) bearing tumors were used for immunocytochemical studies of the tumor cells. Antibodies against the following secretory proteins were applied to paraffin sections of formalin-fixed tissue: anti-SVS II, anti-PBP, anti-transglutaminase, anti-acid phosphatase (isoenzymes, isoelectric points [pI] 5.6, 7.1, 8.0), non-secretory proteins comprised antiglucocorticoid-receptor, and antibodies against extracellular matrix proteins and intermediate filaments. A differential expression of marker proteins subsequent to the various treatments was observed immunohistochemically. Castration induced a loss of secretory activity, an increase in keratin-immunoreactive cells, and regressive activity in the secretory cells. Immunoreactivity of the glucocorticoid receptor in the nuclei of the basal cells was also decreased. Testosterone substitution only partially restored secretory activity of tumor cells in castrated animals. In experiments where estramustine had been administered to normal or castrated animals, metaplastic transformation of the epithelium, focal reduction, or increase of secretory and/or regressive activity and persistence of glucocorticoid receptor-like immunoreactivity was observed. The findings indicate that different hormonal situations provide conditions for the development of rather heterogeneous reaction patterns of different tumor cells, allowing partial regression of individual clones of tumor cells along with stimulation of others.

Adenocarcinoma↗
PubMed1989

Photoaffinity labelling of nuclear steroid 5 alpha-reductase of rat ventral prostate.

In order to get more information on the molecular structure of the rat prostatic 5 alpha-reductase (3-oxo-5 alpha-steroid: NADP+ 4-ene-oxidoreductase, EC 1.3:1.22) a systematic photoaffinity labelling study has been performed. To irreversibly freeze the status quo of interaction, either testosterone, the physiological ligand, or diazo-MAPD (21-diazo-4-methyl-4-aza-5 alpha-pregnane-3,20-dione), a specific 5 alpha-reductase inhibitor, was irradiated with isolated nuclei or with purified nuclear membranes or with solubilized nuclear membrane proteins and checked for optimal labelling conditions. The principal substances covalently labelled were phospholipids and at a minor ratio proteins. Analysis by SDS-PAGE and autoradiofluorography revealed two labelled polypeptides with molecular weights of 20 kDa and 26 kDa. The following evidence indicates that these polypeptides might be derived from the enzyme 5 alpha-reductase: both proteins are labelled only when specific ligands for 5 alpha-reductase are used; binding can be reduced by the addition of an excess of unlabelled ligand; enzyme activity is irreversibly suppressed when irradiated in the presence of these ligands; only subcellular fractions containing 5 alpha-reductase reveal the labelled proteins; in all 5 alpha-reductase containing preparations with increasing specific activity, independent of the polypeptide pattern, the same proteins are labelled.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMed1989

Immunological relationships between specific sperm proteins and secretory polypeptides from seminal vesicles.

Rat and bovine testicular and posttesticular spermatozoa, in situ or removed from the seminal pathways were studied for the presence and the binding of seminal vesicle secretory proteins. A protein cross-reactive with an antibody against rat seminal secretory sulfhydryloxidase was found in mitochondria of pachytene primary spermatocytes which are sequestered during spermiogenesis and collected in the residual bodies of late spermatids. This indicates the replacement of one generation of mitochondria by another during spermiogenesis. Using an antibody against the SVS II polypeptide from rat seminal vesicles, an intrinsic immunoreactive protein was detected in the principal piece of the sperm tail as well as an extrinsic protein (presumably secreted by the epididymis) on the sperm head. The actin-capping capacity of SVS II indicates the functional relation of this immunoreactive membrane protein with actin or an actinrelated protein. Ampullary bovine spermatozoa, contrary to their epididymal precursors contain immunoreactive major protein, secreted from bull seminal vesicles, firmly incorporated into the (sub) plasmalemmal protein in the middle piece. In this case, a secretory protein from seminal vesicles is incorporated into the sperm proteins. This is presumably an important process, related with the initiation of hypermotility of spermatozoa.

Animals↗
PubMed1988

Binding of a major secretory protein from bull seminal vesicles to bovine spermatozoa.

The seminal vesicles synthesize in an androgen-dependent manner a neutral protein of 13.5 kDa molecular weight that makes up about 40% of their secretion ("major protein"). An antiserum against this protein raised in rabbits was used to localize the antigen within the seminal vesicles. In addition to intraluminal secretion of the seminal vesicles and the ampulla of the vas deferens, ejaculated and ampullary spermatozoa revealed an intense immunoreaction, which was restricted to the neck region of the sperm head and the middle piece, while the principal piece of the tail as well as the sperm head were devoid of immunoreactive material. Comparison of spermatozoa taken from the tail of the epididymis with ampullary spermatozoa showed that about 90% of the latter, but only 10-20% of the former presented this distributional pattern of immunoreactive sites. Epididymal epithelium as well as calf seminal vesicle epithelium showed no immunoreactivity with major protein antiserum. Using a pre-embedding staining technique with gold-labeled primary or secondary antibodies, respectively, no immunostaining could be achieved at the ultrastructural level. Incubation experiments of epididymal spermatozoa in EGTA-containing solutions in the absence of calcium resulted in a gradual labilization and eventual loss of the plasma membrane of the sperm middle piece. After removal of (at least part of) the plasma membrane, bound major protein could be visualized immunohistochemically close to the mitochondria of the middle piece using a gold-labeled primary or secondary antibody. The acceptor site for major protein therefore seems to reside inside the plasma membrane of the sperm middle piece.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1988

Immunocytochemical localization of actin and tubulin in rat testis and spermatozoa.

Using commercial monoclonal antibodies against actin and tubulin (alpha and beta), the respective antigens were localized on semithin and ultrathin sections of the rat testis. Tubulin immunofluorescence was found in the socalled manchette surrounding the heads of the maturating spermatids as well as the sperm tail. The distribution pattern varied with sperm development. Modified Sertoli cells found at the transition between the seminiferous tubules and the rete testis displayed much filamentous tubulin-reactive material. The immunofluorescence findings could be confirmed at the ultrastructural level using the indirect immunogold method. Actin immunofluorescence was demonstrated in vascular smooth muscle cells, interstitial macrophages and - most intensely - in peritubular cells. Inside the seminiferous tubules the Sertoli cell junctions and the ectoplasmic specializations of the Sertoli cells that follow the outer contour of spermatid heads displayed distinct actin immunofluorescence. In addition to the locations mentioned, actin-like immunoreactivity was visualized at the ultrastructural level in the chromatoid body and the subacrosomal space of spermatids as well as on the outer dense fibers of the sperm tail. Immunoblotting experiments with actin antibodies showed that in extracts from testicular spermatozoa, intact or fragmented into heads and tails, from isolated Sertoli cells grown in vitro, and from testis tissue in addition to authentic actin a protein was present in sperm tail extracts that strongly bound the actin antibody. This protein may be an actin-related protein and may be responsible for the actin-like immunoreactivity of the outer dense fibers of the sperm tail.

Actins↗
PubMed1988

The major protein of bull seminal plasma: biosynthesis and biological function.

We isolated the major protein of apparent Mr of 15,000-16,000 from seminal plasma as well as from seminal vesicle secretion of bull and proved by amino acid analysis and tryptic peptide mapping that the two proteins were identical. An antiserum against this major protein was employed to quantitate and identify the major protein in seminal plasma as well as seminal vesicle secretion. The antiserum did not cross-react with proteins from bovine or human plasma or follicular fluid respectively. Cell-free translation of poly(A)RNA from seminal vesicle tissue and immunoprecipitation yielded one major species with apparent Mr of 18,000. Using the anti-major protein antiserum, this major species was specifically immuno absorbed. Cloning and sequencing of a major protein-specific cDNA led to the identification of clone pMP17, encoding a precursor of the major protein of 128 amino acid residues. We proved that the major protein is identical to protein PDC 109 (Esch et al., Biochem. Biophys. Res. Comm. 113:861-867, 1983). The seminal vesicles synthesize major protein in an androgen-dependent fashion. In addition to intraluminal secretion of the vas deferens, ampullary spermatozoa revealed an intense immunoreaction which was restricted to the neck region of the sperm head and the middle piece, while the principal piece of the tail as well as the sperm head were devoid of immunoreactive material. Epididymal epithelium (as well as calf seminal vesicle epithelium) showed no immunoreactivity with major protein antiserum. Immunoelectron microscopy demonstrated that only spermatozoa devoid of a plasma membrane around the middle piece were able to bind the antiserum against major protein. After removal of the plasma membrane from epididymal spermatozoa, binding of major protein to subplasmalemmal binding sites was visualised using gold-labeled MP. Transblotting with gold-labeled MP demonstrated a protein of about 66 kDa which appears to represent the major protein-receptor. Binding of major protein to the receptor (after loss of the plasma membrane in the mid-piece region of the spermatozoa after contact with secretions from seminal vesicles) is interpreted as a physiological process presumably related to the onset of sperm motility.

Amino Acid Sequence↗
PubMed1987

Ultrastructure and immunohistochemistry of the lateral prostate in aged rats.

Ultrastructural, histological, and immunohistochemical studies were performed on lateral prostates of 1) aged rats from different strains, 2) rats permitted different levels of sexual activity, and 3) castrated rats. Antibodies against the following proteins were used as immunohistochemical markers: SVS II from seminal vesicle, LP 28 from lateral prostate, acid phosphatase isoenzymes from ventral prostate, transglutaminase from coagulating gland, and a commercial monoclonal antibody against cytokeratin. SVS II is a marker of lateral prostatic secretion, while immunoreactions to LP 28 and acid phosphatase (pI 7.1) were cytoplasmic. In aged animals the amount of intracellular secretion is decreased, and focally metaplastic transformation can be visualized by using immunohistochemical markers. Epithelial ultrastructure varied considerably with experimental conditions. Intensive sexual activity resulted in increased polymorphism and increased number of secretory granules within the glandular cells, while castration was followed by a rapid loss of secretory material. Also, in rats older than 10 months, a reduction in the number of secretion granules was common. The epithelium developed a positive immunoreaction to transglutaminase antibodies that were not observed in juvenile glands. Cells, presumably macrophages, which had an intense immunoreactivity for transglutaminase, were increased in number both within and outside the prostatic acini of aged rats. The possible interaction between secretory SVS II, a substrate of transglutaminase, the release of this enzyme from macrophages or its reflux from coagulating glands, the spontaneous cellular exfoliation that is due to decreased androgen levels, and dietary noxae may be of importance in the development of lateral prostatic nonbacterial inflammation in aged rats.

Acid Phosphatase↗