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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 637 (1991), 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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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 637 (1991), 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
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 202 (1982), S. 463-471 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The morphogenesis of the outer dense fibers (ODF) in rat spermatids has been studied by electron microscopy, and the synthesis and incorporation of proteins into the ODF during this process have been followed by radioautography using 3H-proline and 3H-cystine as precursors for ODF proteins. In the first phase (steps 8-14), nine very fine fibers termed anlagen of the ODF develop in association with the microtubule doublets. These first appear along the most proximal portion of the axoneme in step 8 of spermiogenesis; during steps 9-14 they gradually increase in length in a proximal-to-distal direction, being first observable along the forming midpiece and later along the principal piece as well. In the second phase (steps 15-16), the rudimentary fibers suddenly increase in diameter, with the most dramatic growth occurring in step 16, and assume a close resemblance to the mature ODF. This striking transformation, which appears to result from simultaneous deposition of electron-dense material along the length of anlagen of the ODF, coincides with a period of rapid incorporation of 3H-proline and 3H-cystine-containing proteins, which become permanent structural components of the ODF. These proteins, which comprise the bulk of the ODF, are synthesized in the cytoplasm of spermatids during the acrosome and early maturation phases. In the final phase (steps 17-19) the fibers continue to enlarge very slowly, assuming their definitive form in step 19 of spermiogenesis. Thus formation of the ODF in the rat is a lengthy multistep procedure, requiring from step 8-19 of spermiogenesis and utilizing proteins synthesized throughout most of this period.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 232 (1992), S. 25-35 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In order to analyse, at the electron microscope level, the three-dimensional configuration of the trans compartment of the Golgi apparatus rat dorsal root ganglia were treated to demonstrate cytidine monophosphatase (CMPase) activity. The localization of enzymatic activity in the Golgi apparatus varied according to cell types. In type A and C cell, CMPase was exclusively located in the transmost sacculotubular element, whereas in type B cells all the saccules of the stacks forming the Golgi ribbon and the trans-Golgi networks were impregnated. Numerous dense bodies seen at proximity were also CMPase positive. In 3 μm thick sections of type A cells examined at low magnification, the impregnated element was scattered throughout the cytoplasm and never formed a continuous structure. In type B cells, the strongly reactive trans-Golgi networks did not follow the entire length of the impregnated Golgi ribbon but were preferentially located in the concavity of its arched portions. At higher magnification and in all cell types some tubular portions of the trans-Golgi networks took the apperance of spheroidal cage-like structures, the CMPase positive anastomotic tubules forming the bars of the cage. Anastomotic tubules separated from the trans-Golgi networks formed fenestrated spheres, while nearby CMPase-reactive dense bodies exhibited a paler hilus. These observations were taken to indicate that in ganglion cells, some CMPase positive dense bodies, presumably lysosomes, formed by fragmentation of the trans-Golgi networks.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The initial segment of the epididymis of rats, fixed with glutaral-dehyde, was postfixed with reduced osmium, a technique that clearly delineates the membranes of cisternae of the endoplasmic reticulum (ER) and the various elements of the Golgi apparatus, or with tannic acid to enhance the coats of vesicles and ribosomes on ER cisternae. The material was also treated to demonstrate various phosphatase activities (NADPase, TPPase, CMPase, G-6-Pase) or impregnated with osmium tetroxide.In osmium-impregnated material, the Golgi apparatus of the epithelial principal cells of the initial segment appeared in the light microscope as a branching, anastomosing ribbon forming a large network in the supranuclear region. In the electron microscope, ER were of two types: the heavily granulated, flattened, rough ER seen in the infranuclear and juxtanuclear regions and the distended, tubular, sparsely granulated ER, showing only few ribosomes, seen interlaced with the Golgi ribbon in the supranuclear region and at the apical pole of the cell.Of particular interest in this cell was the fact that the sparsely granulated ER approximated the Golgi stack on both its cis- and trans-faces. On the cis-face of the Golgi stack, the sparsely granulated ER cisternae showed the usual finger- or bud-like protrusions directed toward the cis element of the Golgi stack and around which numerous small 80 nm vesicles or membranous tubules were clustered. The Golgi stack consisted of the following elements in a cis-trans axis: the cis osmio-philic element, a first saccule slightly dilated, saccules two to four (S2-S4), which were NADPase-positive, and saccules five to seven and the eight Golgi element, which were TPPase-positive. On the trans-aspect of the Golgi stacks, several (up to four) CMPase-positive trans-Golgi networks were observed often in close apposition to the sparsely granulated ER cisternae. One of the trans-Golgi networks showed a “peeling-off” configuration, i.e. part of it was closely apposed to the overlying Golgi element of the stack, whereas the remaining part was separated from the stack by a space occupied by a cisterna of sparsely granulated ER. The other trans-Golgi networks were completely separated from the stack and were often seen sandwiched between sparsely granulated ER cisternae. Thus, ER cisternae showed extensive areas of close apposition but no continuity with the trans-Golgi networks. Although the saccules of the Golgi stacks showed NADPase and/or TPPase activity, the trans-Golgi networks displayed CMPase activity, thus facilitating their identification from the closely associated unreactive sparsely granulated ER cisternae.The trans-Golgi networks were variable in appearance but often showed sporadic electron-lucent dilations along their length that were comparable to uncoated vesicles of similar size (150-300 nm) and appearance found in the trans-region of the Golgi apparatus and at the apical pole of the cells. Such vesicles appeared to arise from the trans-Golgi networks that eventually undergo fragmentation. Their identification as possible secretory vesicles will be discussed.
    Additional Material: 26 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 230 (1991), S. 489-501 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The perforatorium is the subacrosomal portion of the perinuclear theca that encapsulates the nucleus of spermatozoa. In the rat, the perforatorium is a curved pointed structure, which in cross section is triangular in outline over the apical half and beyond the tip of the nucleus. The perforatorium, composed of several proteins, appears as a distinct structural entity only at the very end of spermiogenesis. In this study, polyclonal antibodies prepared against the entire isolated perforatorial fraction and against the major 16 and 34 kDa perforatorial polypeptides were used to determine the distribution of perforatorial proteins in germinal cells at various steps of differentiation. Immunoperoxidase staining at the LM level and quantitative immunogold labeling at the EM level were used. The labeling patterns with all three antibody preparations were identical. The immunolabeling first appeared in early pachytene spermatocytes and increased progressively, with a statistically significant upward trend, in both the nuclei and cytoplasm of spermatocytes and spermatids until step 9 of spermiogenesis. Up to this step the labeling concentration was significantly higher over the nucleus than over the cytoplasm. During nuclear condensation in steps 9 and 12 spermatids, there was a progressive loss of all the labeling over the nucleus and a corresponding increase of labeling over the cytoplasm. During steps 16-18, the early signs of condensation of perforatorial proteins occurred next to the inner acrosomal membrane. Then during step 19 there was a sudden condensation of perforatorial proteins into a definitive perforatorium. Thus proteins destined to form this cytoskeletal structure reside in both the nucleus and cytoplasm of spermatocytes and spermatids until nuclear condensation of the latter. Thereafter, they are restricted to the spermatid's cytoplasm and finally condense around the elongated nucleus at the end of spermiogenesis.
    Additional Material: 25 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 213 (1985), S. 33-43 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: During steps 1-7 of spermiogenesis the Golgi apparatus contributes to the formation of the acrosomic system which develops at the surface of the nucleus. Later, in step 8, the Golgi apparatus detaches from the acrosome and remains suspended in the elongated cytoplasm until it degenerates during step 16. Using 3H-fucose as a tracer and the radioautographic technique, we observed that the Golgi apparatus incorporates the tracer and delivers the labeled glycoproteins to the developing acrosomic system during steps 1-7 of spermiogenesis, to multivesicular bodies during steps 1-9, and to the remaining cytoplasm and plasma membrane during steps 1-15. Throughout these steps of spermiogenesis the Golgi apparatus does not show major changes in structure; it is composed of a cortex made up of connected stacks of saccules and a medulla showing a loose aggregate of vesicular profiles. Glycoprotein synthesis in this Golgi apparatus, before and after it contributes lysosomal glycoproteins to the growing acrosomic system, was quantitatively assessed in electron microscope EM radioautographs of tissue sections from animals sacrificed at 1, 4, 8, and 24 h of 3H-fucose injection. The incorporation of the labeled sugar was found to remain quantitatively similar during steps 1-15 of spermiogenesis, and therefore, no shift in glycoprotein synthesis took place following separation of the Golgi apparatus from the acrosomic system. Throughout these steps, fucose molecules are first incorporated in the cortex of the organelle and subsequently transported to the medulla, where they temporarily accumulate before being delivered, depending on the step of spermiogenesis, to the acrosomic system, to the multivesicular bodies, and also, presumably, to the plasma membrane.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 225 (1989), S. 46-55 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The formation of the fibrous sheath (FS) and outer dense fibers (ODF), two major cytoskeletal components of the tail of spermatozoa, was analyzed in the seminiferous epithelium by immunoperoxidase techniques applied to paraffin-embedded testicular sections. Antibodies were prepared from purified FS and ODF fractions and from major 75 and 14.4 kDa FS polypeptides and major 32-26 14.4 kDa ODF polypeptides. The immunostaining results showed that the production of FS and ODF proteins appeared to be exclusive to step 9-19 spermatids and lasted over the duration of a full cycle of the seminiferous epithelium, or 12.8 days. During this period there was seemingly an initial lag of short duration between the synthesis and assembly of FS and ODF proteins followed by a long process of coordinated activity. Peak cytoplasmic immunoreactivity was reached in step 15 for FS proteins and midstep 16 for ODF proteins and and remained elevated thereafter for approximately 80 hr for both FS and ODF proteins. The immunoreactivity was more uniform and diffused for FS proteins and granulated or clumpy for ODF proteins. Assembly of FS proteins along the axoneme proceeded in a distal to proximal direction while for ODF proteins assembly proceeded in a proximal to distal direction. The main route of elimination of residual cytoplasmic FS and ODF proteins appeared to take place through the cytoplasmic droplets and residual bodies, respectively. There appeared to be no variation in step reactivity between the major ODF polypeptides tested and only minor variation in step reactivity between the major FS polypeptides tested. However, although the 14.4 kDa polypeptides of FS and ODF share antigenic determinants, they do not appear to be identical, because they presented different immunolocalizations during spermiogenesis and different directions of assembly along the axoneme.
    Additional Material: 7 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 243 (1995), S. 283-293 
    ISSN: 0003-276X
    Keywords: Secretion pathway ; Yeasts species ; Golgi apparatus ; Secretion granules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: In the yeast Saccharomyces cerevisiae, the Golgi apparatus consists of discrete units distributed throughout the cytoplasm. When such units are examined in three dimensions, in relatively thick sections prepared for the electron microscope, they usually appear as small tubular networks with a stained material accumulating in dilations located at the junctions of membranous tubules. To see whether such tubular networks are observed in other yeast species, the three-dimensional structure of organelles in eight additional yeast strains, endowed with diverse biological properties, are examined.Methods: Yeast strains were grown at 24°C in YPD medium (2% Bactopeptone, 1% Bactoyeast extract, and 2% glucose). Cells that were examined by electron microscopy came from exponentially growing cultures grown in a shaking water bath and maintained at a OD 600 (optical density at 600 nm) of 0.5. Cells were fixed in a fixative containing 2% glutaraldehyde in 0.1 M cacodylate buffer pH 7.4 and 0.8 M sorbitol. They were then treated for 15 min in 1% sodium metaperiodate and postfixed for 1 hr in potassium ferrocyanide-osmic acid. They were preembedded in agarose prior to dehydration and finally embedded in Epon. In these conditions, the preservation of cell organelles was improved and the cytoplasmic retraction from the cell wall was minimized. Photographs of sections tilted at ± 15° from the 0° position of the goniometric stage were used to prepare stereopairs from which the three-dimensional configuration of the organelles was visualized.Results: In all yeast strains, tubular networks appeared as separate elements or units dispersed throughout the cytoplasm. Each unit consisted of anastomosed membranous tubules. In some strains such as Saccharomyces cerevisiae, Zygosaccharomyces rouxii, or Saccharomyces pombe, such units appeared mainly as polygonal networks of intensely stained membranous tubules. Along these networks, distensions filled with stained material were similar in size to nearby secretory granules, suggesting that the latter formed by fragmentation of the tubular networks. In Hansenula polymorpha, Pichia pastoris, and Debaryomyces hansenii, networks of anastomosed tubules were closely superposed to each other and formed parallel arrays reminiscent of the stacks of Golgi saccules seen in mammalian cells. However, in contrast to what is usually found in the latter, the layers making up the parallel arrays in yeasts, were clearly continuous to each other. In other strains, i.e., Kluyveromyces lactis, Candida albicans, and Candida parapsilosis, the situation was intermediate and their cytoplasm contained only arrays of small size with two or at most three superposed layers of membranous tubules. Small vesicles in the 30-50 nm range were rarely encountered in most yeast strains.Conclusions: It is therefore concluded that tubular networks, presumably Golgi in nature, are present in all yeasts examined so far. Yet, in some strains, these tubular networks may be arranged in parallel arrays or stacks. © 1995 Wiley-Liss, Inc.
    Additional Material: 20 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 187 (1977), S. 347-365 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In normal adult rats some germ cells degenerate at several vulnerable steps of spermatogenesis. These are the type A spermatogonia, midpachytene spermatocytes, primary and secondary spermatocytes which degenerate during their respective maturation divisions and step 7 and 19 spermatids. In the present study, these degenerating cells were examined under the electron microscope, and their frequency was determined in toluidine blue stained semithin sections of testes from normal, hypophysectomized (at 5.5 days after operation) and hypophysectomized rats injected with FSH and LH separately or in combination. With the exception of the step 19 spermatids, the degenerating germ cells underwent necrosis in vacuolated spaces delimited by Sertoli cells. In the case of the affected step 19 spermatids, an apical cytoplasmic process of the Sertoli cell initially ensheathed a long segment of their flagellum, and then each degenerating cell was drawn deep in the seminiferous epithelium where it was phagocytozed by the Sertoli cell. Soon after hypophysectomy the incidence of degenerating mid-pachytene spermatocytes, step 7 and 19 spermatids which are present in stages VII or VIII of the cycle of the seminiferous epithelium, increased significantly. In contrast the number of degenerating primary or secondary spermatocytes during the meiotic divisions seen in stage XIV of the cycle or of any other germinal cell was not significantly modified. While the injection of FSH alone had no influence on the number of degenerating cells in hypophysectomized rats, injections of LH at the two doses administered (0.7 μg or 20 μg) reduced significantly the number of degenerating cells seen in stages VII-VIII of the cycle; combined injections of FSH and LH (20 μg) reduced the number of these degenerating cells to the normal low values. Thus it appeared that the mid-pachytene spermatocytes and the step 7 and 19 spermatids, all present in the adluminal compartment of the seminiferous epithelium in stages VII or VIII of the cycle, were more sensitive to the presence of absence of gonadotropic hormones than the other germ cells present in the seminiferous epithelium.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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