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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Micron And Microscopica Acta 21 (1990), S. 150 
    ISSN: 0739-6260
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Electrical Engineering, Measurement and Control Technology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 513 (1987), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary During passage through the epididymis, spermatozoa undergo a number of changes which result in their acquisition of fertility and motility. Some of the changes that occur include loss of the cytoplasmic droplet and changes in sperm morphology, metabolism and properties of the nucleus and plasma membrane. Changes have also been reported in the acrosomic system of mammalian spermatozoa during their transit through the epididymis. In the present study, the quantitative changes of the glycoconjugate content in the acrosome of rat spermatozoa were examined during their passage through the epididymis using lectin-colloidal gold cytochemistry. Various regions of the epididymis (initial segment, caput, corpus and cauda epididymidis) were fixed by perfusion with 1% or 2% glutaraldehyde buffered in sodium cacodylate (0.1M), dehydrated in ethanol and embedded without osmication in Lowicryl K4M. Lectin-colloidal gold labeling was performed on thin sections usingRicinus communis agglutinin I (RCA I) orHelix pomatia lectin (HPL) to detectd-galactose-andN-acetyl-d-galactosamine-containing glycoconjugates, respectively. The labeling density over the acrosome of the acrosomic system was evaluated as the number of gold particles per μm2 of profile area using a Zeiss MOP-3 image analyzer. The overall mean labeling densities over the acrosome of spermatozoa for each lectin was estimated from 4 rats and over the four distinct epididymal regions. The mean labeling density of the acrosome with RCA I and HPL showed a similar pattern along the epididymis, although RCA I revealed approximately twice as many gold particles per epididymal region. In either case, there was a significant decrease in the labeling density of the acrosome of spermatozoa between the initial segment or caput epididymidis and cauda epididymidis (p〈0.01). A similar decrease was also noted between the initial segment and corpus epididymidis (p〈0.01). No change was found between the initial segment and caput epididymidis. Controls showed a virtual absence of labeling. These results suggest that in addition to a multitude of changes occurring to spermatozoa during epididymal transit, there are also significant quantitative changes in the glycoconjugate content within the acrosome.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 109 (1998), S. 431-447 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The Golgi apparatus of epididymal principal cells shares many structural features with other cell types. Saccular regions are arranged in a cis-Golgi network, eight flattened saccules, and several trans-Golgi networks (TGNs). Dilated tubules form intersaccular connecting regions which joint together saccules at the same or different levels between adjacent stacks. Wells exist as large perforations in register with the four cis-most saccules and serve as areas of vesicular interactions. TGNs are variable and can appear to peel off the stack or to be detached from it in the form of an anastomotic tubular network with pale dilated areas corresponding to prosecretory granules connected by short narrow bridges. Elongated or discoid dilated cisternae of endoplasmic reticulum (ER) (sparsely granulated) lie over the cis face of the stack, from which they are separated by an intermediate compartment filled with vesicles and tubules. The ER is also closely juxtaposed to the TGNs and the eighth saccule but interconnections are never seen between them. Vesicles of the COP variety reside at all levels of the stack and appear to bud off the cis-located ER and the edges of the saccules, while clathrin-coated vesicles appear mainly on the trans face of the stack and next to lysosomes. In the supranuclear cytoplasm, clusters of vesicles and tubules, at times budding off enveloping ER, appear to radiate toward the Golgi stacks where they fuse with cis Golgi elements. Taken together, these observations suggest dynamic functions and interactions for the various Golgi elements, associated vesicles, ER, and vesicular tubular clusters.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 227 (1990), S. 447-457 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Affinity purified antibodies prepared against proteins isolated from fibrous sheath (FS) and outer dense fibers (ODF) were utilized in an immunocytochemical study of spermatids at various steps of spermiogenesis. This study, using the immunogold technique, was performed on sections of Epon or Lowicryl embedded tissues examined with the electron microscope. In the case of FS antibodies there was a selective immunoreactivity of the FS itself from step 10 onwards, but no reactivity over the plasma membrane associated FS anlagen. In addition there was a diffuse immunoreaction over the cytoplasmic matrix from step 9 until step 18 of spermiogenesis but no reactivity over the various types of dense bodies (e.g., granulated bodies, reticulated body, etc.) seen in the cytoplasm of these spermatids. In the case of ODF antibodies the ODF were immunolabeled throughout their development from step 11 onward. In addition to a diffuse immunoreactivity of the cytoplasmic matrix of spermatids from step 9 until step 18 of spermiogenesis, there was an immunolabeling of “granulated bodies.” These bodies appeared in relation to ER cisternae during steps 10-14, increased in number and size during steps 15-17 and decreased in number thereafter leaving only a few coarsely granulated bodies in the residual cytoplasm which detached from late step 19 spermatids. No other cytoplasmic structures were labeled with the ODF antibody-gold complexes. Thus the granulated bodies appeared to serve as a transitory storage site for some proteins destined to form ODF, a major cytoskeletal element of the tail of rat spermatozoa.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The localization of immobilin, a glycoprotein known to be present and to immobilize spermatozoa in the lumen of the epididymis, was investigated using light and electron microscope immunocytochemistry. In the light microscope, a distinct immunoperoxidase reaction product was observed in the lumen over the brush border of the epithelial nonciliated cells of the efferent ducts, while only a faint reaction was seen over their supranuclear region. In the proximal area of the initial segment of the epididymis no immunoperoxidase staining was observed either over epithelial cells or in the lumen. In the middle area of the initial segment, several epithelial principal cells became intensely immunostained but the majority were unstained; a weak reaction appeared in the lumen. In the distal area of the initial segment, more principal cells became immunostained, and while some were intensely reactive, others were moderately or weakly stained or unreactive. In the intermediate zone and proximal caput epididymidis, the principal cells showed the maximal immunoreactivity with all principal cells being reactive; staining in the lumen also reached its maximal reactivity in these areas. Immunostaining of principal cells gradually decreased along the epididymal duct and disappeared in the cauda epididymidis, however, an intense reaction persisted in the lumen. In the distal area of the cauda epididymidis, clear cells were reactive. In the electron microscope, immunogold labeling of reactive principal cells of the middle and distal areas of the initial segment, intermediate zone, and caput epididymidis was detected over cisternae of endoplasmic reticulum, stacks of Golgi saccules, and spherical electron lucent (200-400 nm in diameter) vesicles. The latter were present on the trans face of the Golgi stack, in the vicinity of the Golgi apparatus, and close to the apical cell surface; they are considered as secretory vesicles involved in the secretion of immobilin. In the distal area of the cauda epididymidis, epithelial clear cells showed an intense immunogold labeling over their endocytic apparatus. Immunogold labeling in the lumen of the epididymis was found over a fine flocculent material dispersed between the sperm. This material was especially abundant in the cauda epididymidis and did not appear to be bound to the surface of the sperm. The present results suggest that principal cells of the epididymis are involved in the secretion of immobilin, but that a differential secretory pattern exists between epididymal segments with maximal secretory activity occurring in the intermediate zone and proximal caput epididymidis, while no secretion takes place in the cauda epididymidis. Excess immobilin appears to be endocytosed for degradation by clear cells of the cauda epididymidis.
    Additional Material: 30 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The localization of sulfated glycoprotein-1 (SGP-1) in the extratesticular duct system was analyzed using an affinity purified antibody raised against the protein in conjunction with light (LM) and electron (EM) microscope immunocytochemistry. In the LM an intense immunoperoxidase reaction product was observed over the cytoplasm of Sertoli cells as well as over the tails of late spermatids. The rete epithelial cells and noncilliated cells of the efferent ducts also showed an intense uniform reaction over their entire cytoplasm. In the EM, immunogold labeling was noted over the entire endocytic apparatus of these cells including coated pits, endosomes, multivesicular bodies, and secondary lysosomes. Since there was no labeling of the luminal contents including sperm along the epididymis, it was concluded that the Sertoli-derived SGP-1 must dissociate from the sperm and be taken up by epithelial cells at the level of the rete testis and efferent ducts.In all regions of the epididymis, except the cauda, the principal cells showed, in the LM, an intense reaction over bodies of various shapes and sizes in their supranuclear region; this corresponded in the EM to a strong immunogold labeling of secondary lysosomes. No labeling was noted, however, over coated pits, endosomes, or pale multivesicular bodies, suggesting that SGP-1 was not being endocytosed from the lumen. Similar observations were noted for the epithelial clear cells along the entire epididymis. In the cauda epididymidis, principal cells presented a weak immunolabeling of their secondary lysosomes.Northern blot analysis revealed a strong 2.6 Kb band corresponding to the mRNA of SGP-1 in the efferent ducts and all regions of the epididymis with the exception of the cauda. Coincident with the mRNA expression of SGP-1 it was found that small clusters of gold particles representing anti SGP-1, presumably membrane bound, were associated with the Golgi apparatus as well as in close proximity to secondary lysosomes. There was, however, no evidence for the secretion of SGP-1 into the lumen. These results suggest that SGP-1 is synthesized by the epithelial cells of the male duct system and ferried by small vesicles derived from the Golgi apparatus to secondary lysosomes. Because SGP-1 has recently been shown to have substantial sequence similarity to prosaposin, it may be speculated that SGP-1 is instrumental in the degradation of membrane glycolipids present within secondary lysosomes of epithelial cells of the extratesticular duct system.
    Additional Material: 31 Ill.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0003-276X
    Keywords: Prosecretory granules ; Trans-Golgi network ; Exocytosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Lactating mammary glands fixed by perfusion with 5% glutaraldehyde subsequently were postfixed with potassium ferrocyanide reduced osmium or were treated with tannic acid. Stained thin sections were examined with the electron microscope and stereopairs were prepared. The distribution of casein submicelles was analyzed in the various components of the Golgi apparatus. The Golgi stacks were composed of five or six elements, all of which contained casein submicelles 20 nm in diameter. The cis-tubular network or cis-element, as well as the underlying three or four midsaccules, showed these casein submicelles either attached to their membrane or free in the lumen. The trans-most element of the stacks formed distended prosecretory granules in which both isolated or clustered casein submicelles were suspended in an electron-lucent fluid. These micellar aggregates increased in size and became progressively more compact to form spherical dense bodies or casein micelles, in which the individual 20 nm particles could easily be resolved. Casein micelles were seen in secretory granules in addition to a wispy material of low density. The numerous small spherical vesicles (80 nm or larger) seen on the cis, lateral, or trans aspects of the stacks did not appear to contain free casein submicelles. This raises questions regarding the role of these vesicles in the transport of casein macromolecules through the Golgi stacks. It was noticeable that in this Golgi apparatus a trans-Golgi network was limited to a few small residual tubules free from casein submicelles. It thus appears that the greater part of the trans-most Golgi element gives rise to the large prosecretory granules. After leaving the Golgi region and prior to exocytosis, the secretory granules often fuse to form larger granules before exocytosis. © 1993 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 240 (1994), S. 86-103 
    ISSN: 0003-276X
    Keywords: Immobilin ; Development ; Principal cells ; Clear cells ; Secretion ; Endocytosis ; Rat epididymis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: Immobilin is a protein secreted by principal cells of the distal initial segment, intermediate zone and caput epididymidis of adult rats, which serves to immobilize spermatozoa. In the distal cauda, epithelial clear cells are involved in its endocytosis. The objective of this study was to correlate the developmental events in the maturation of the epdidymis with the timing of immobilin secretion and endocytosis in order to evaluate the testicular or epididymal factors which may influence or regulate immobilin expression.Methods: Our approach was to follow and compare the developmental expression of immobilin by light microscope immunocytochemistry in control and efferent duct ligated rats of different postnatal ages.Results: Coincident with the morphological maturation of the principal cells by postnatal day 39, immobilin displayed the characteristic secretory immunostaining pattern found in adults. This adult-like expression occurred despite the absence of spermatozoa in the lumen but was coincident with high levels of circulating and luminal androgens. In contrast, immobilin secretion in rats whose efferent ducts were ligated at day 15 was weak to non-existent in the principal cells of the caput epididymidis at day 28 and remained so into adulthood, indicating that principal cells of this region of the epididymis are dependent either directly or indirectly upon testicular factors present in the lumen for immobilin expression. However, secretion of immobilin in the principal cells of the distal initial segment was unaffected by ligation and unlike the case in control rats high levels of immobilin also continued to be secreted into adulthood by the principal cells of the proximal initial segment. Thus in the distal initial segment immobilin secretion is not regulated by luminal factors originating from the testis, while in the proximal initial segment the normal suppression of immobilin that occurs by postnatal day 39 is. Despite ligation, endocytosis of immobilin by clear cells of the distal cauda epididymidis occurred by day 49, indicating that luminal testicular factors are not essential for stimulating the uptake of immobilin by these cells.Conclusions: The results taken together suggest that there are stimulatory and inhibitory luminal testicular factors involved in the regional development of immobilin secretion in the epididymis. There are also immobilin secreting regions in the epididymis, whose secretory development is independent of luminal testicular factors. © 1994 Wiley-Liss, Inc.
    Additional Material: 42 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 196 (1980), S. 83-99 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Throughout stage VII and early stage VIII of the cycle of the seminiferous epithelium, the heads of the late spermatids, located in a juxtaluminal position, are embedded in apical processes of Sertoli cells. These processes contain cisternae of endoplasmic reticulum (ER) of two main types, i.e., flattened and tubular, which communicate with each other to form a continuous system. Throughout the long stage VII of the cycle, these two types of cisternae undergo marked changes. In early stage VII, the flattened cisternae, developing from the subsurface cisternae which compose the “junctional specialization,” form concentric sheets at the periphery and in the middle of each apical process. The less conspicuous tubular cisternae form a continuous network which is present in the bridge connecting the Sertoli cell body to the apical process, and extends along the dorsal and ventral aspects of the spermatid's head to end up as cup-shaped flattened cisternae capping the bulbs of the tubulobulbar complexes described by Russell and Clermont ('76). In mid stage VII, the flattened cisternae start to regress, while the tubular cisternae become more abundant. In late stage VII, only fragments of the flattened cisternae are present, while the tubular cisternae form a profuse and elaborate network throughout the apical process. In the following stage VIII, the tubular cisternae disperse and only remnants of ER are present at the time of the release of the spermatid into the tubular lumen. These transformations of ER cisternae suggest a complex alteration in the relationship between Sertoli cells and late spermatids prior to their release as spermatozoa.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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