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  • 1
    Electronic Resource
    Electronic Resource
    Freezing of polarization in a Pb(Zr,Ti)O3 film observed by strain imaging (1998)
    Springer
    Applied physics 66 (1998), S. S441 
    Details
    ISSN: 1432-0630
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: 3 with platinum electrodes subjected to hydrogen annealing using strain imaging. The polarization remains downward, when the applied voltage is below 3Vpp. This is caused by a positive internal electric field produced by space charges created in areas with upper platinum electrodes. The freezing of polarization induces a significant reduction in remanent polarization but does not cause large changes in permittivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003390051179
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  • 2
    Electronic Resource
    Electronic Resource
    Whole-cell-mount cytochemistry by the colloidal gold labeling method (1984)
    Springer
    Histochemistry and cell biology 81 (1984), S. 435-439 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Binding, redistribution, and endocytosis of colloidal gold (CG)-labeled concanavalin A (ConA) were studied by transmission electron microscopy (TEM) and scanning electron microscopy (SEM). Mouse peritoneal macrophages were cultured on Formvar-coated platinum grids. Either fixed or unfixed cells were labeled by the indirect ConA-CG labeling method. Specimens were critical-pointdried and observed by TEM and SEM in the same region. Surface-bound ConA-CG was easily seen by SEM. Stereomicroscopic observation by TEM clearly showed the threedimensional distribution of ConA on the cell surface as well as in the cytoplasmic vesicles and vacuoles. In the prefixed cells, CG was distributed randomly on the cell surface. When unfixed cells were labeled at 0° C, a similar binding pattern was observed, although the density of bound CG was decreased. When cells labeled with ConA-CG at 0° C were further incubated at 37° C, redistribution and endocytosis of the label were seen. Endocytosed CG in the cytoplasmic vesicles and vacuoles was clearly seen by TEM. In addition, three-dimensional location and relationship with other organelles were easily observed. Combined TEM and SEM observation of CG-labeled whole-cell-mount specimens is a useful method to study the dynamics of cellbound ligands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489746
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  • 3
    Electronic Resource
    Electronic Resource
    Use of colloidal gold and ruthenium red in stereo high-voltage electron microscopic study of Con A-binding sites in mouse macrophages (1984)
    Springer
    Histochemistry and cell biology 81 (1984), S. 441-444 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Concanavalin A (Con A)-binding sites were labeled with colloidal gold (CG), stained with ruthenium red, and observed under a high-voltage electron microscope. Mouse peritoneal macrophages were labeled by the indirect Con A/CG labeling method at 0° C. After washing, some of the cells were incubated in phosphate-buffered saline (PBS) at 37° C. The specimens were then stained with ruthenium red, to enhance the contrast of the cell surface, and embedded in Epon. Sections (0.3∼3 μm thick) were cut and examined by high-voltage electron microscopy at accelerating voltages of 200∼1,000 kV. Staining with ruthenium red provided a strong contrast of the cell surface and the invaginating tubules beneath it against the cytoplasm; in thick sections, both of them were clearly seen by stereomicroscopy. CG particles which represented Con A-binding sites were also sufficiently electron dense to be recognized by high-voltage electron microscopy of thick sections. The two- and three-dimensional distribution of CG particles on the ruthenium-red-positive cell surface was clearly visualized. At 0° C, Con A-binding sites were randomly distributed on the cell surface. The redistribution and endocytosis of Con A-binding sites were seen at 37° C. The three-dimensional organization of membrane invagination, which represented the process of endocytosis, was clearly seen by stercomicroscopy. The combination of CG labeling and ruthenium red staining is a useful method for high-voltage electron microscopic analysis of the two- and three-dimensional distribution of CG-labeled ligands on the cell surface in thick sections.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489747
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of glycoconjugates in normal human skin using biotinyl lectins and avidin-horseradish peroxidase (1983)
    Springer
    Histochemistry and cell biology 79 (1983), S. 1-7 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Lectin binding patterns in normal human skin were studied using five different biotinyl lectins and avidin-horseradish peroxidase. The staining pattern was specific for each lectin. In the epidermis, peanut agglutinin (PNA) and soybean agglutinin (SBA) preferentially stained the cell membranes of keratinocytes in the spinous and granular cell layers, indicating changes in the saccharide residues during keratinocyte differentiation. In the secretory segment of an eccrine sweat gland, the superficial cells gave a strong granular staining with Ricinus communis agglutinin (RCA). Dolichos biflorus agglutinin (DBA) and SBA, on the other hand, strongly stained the basal cells. With these lectins, two types of cells in the secretory segment were clearly distinguished. These results show that (1) PNA and SBA binding sites increase during the course of keratinocyte differentiation, and (2) RCA, DBA, and SBA are good markers to distinguish two types of cells in the secretory segment of an eccrine sweat gland.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00494336
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  • 5
    Electronic Resource
    Electronic Resource
    Localization of forssman glycolipid and GM1 ganglioside intracellularly and on the surface of germ cells during fetal testicular and ovarian development of mice (1990)
    Springer
    Histochemistry and cell biology 94 (1990), S. 561-568 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Changes in the expression pattern and intracellular localization of Forssman glycolipid (FA) and GM1 ganglioside (GM1) in fetal mouse gonads were examined during germ cell differentiation by immunofluorescence microscopy and immunoelectron microscopy. In male germ cells from the 12th to 14th day p.c., anti-FA binding was localized in granular structures aggregated on one side of the cytoplasm and/or in the plasma membrane. On day 16 p.c., some germ cells still showed patch-like positive reactions in the plasma membrane, but by day 18 p.c., positive reactions for FA had completely disappeared. The female germ cells showed granular bindings of anti-FA scattered throughout their cytoplasm during the 13th to 16th day p.c., although the positive reactions in female germ cells on day 12 p.c. tended to be found in one side of cytoplasm and/or plasma membrane similar to those in male germ cells from 12th to 14th day p.c. On day 18 p.c., positive reactions remained in the plasma membrane of some germ cells, but these positive reactions disappeared before birth. Immunoelectron microscopic observation showed that the sites of anti-FA bindings were equivalent to the “small dense bodies” (SDB) and the Golgi lamellae both in male and female germ cells. On the other hand, GM1 was not detected in male germ cells at any time during fetal testicular development, whereas an anti-GM1 reaction was detected in the plasma membrane of female germ cells from the 16th to 18th day p.c. (oocytes in the first meiotic prophase). Therefore, these results indicate that kinetic translocation of FA between the plasma membrane and the SDB and Golgi lamellae takes place during germ cell differentiation in fetal gonads. Moreover, the ganglioside composition containing GM1 seems to change in association with the first meiotic prophase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271982
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  • 6
    Electronic Resource
    Electronic Resource
    Na+-dependent glucose transporter SGLT1 is localized in the apical plasma membrane upon completion of tight junction formation in MDCK cells (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 529-533 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract SGLT1, an isoform of Na+-dependent glucose transporters, is localized at the apical plasma membrane in the epithelial cells of the small intestine and the kidney. In the present study we examined its location in SGLT1 cDNA-transfected MDCK cells, which form an epithelial sheet connected by tight junctions in culture. Formation of tight junctions was monitored by staining for occludin, an integral tight junction protein. In the cells demarcated by an uninterrupted occludin meshwork, SGLT1 was specifically localized at the apical plasma membrane, showing that SGLT1 has a signal to accomplish this restricted localization. In the cells with little or no occludin accumulation in the tight junction, however, SGLT1 was present along the entire aspect of the plasma membrane. Similar distribution of SGLT1 was observed in the cells as long as the occludin meshwork remained incomplete. These observations sugget that apical localization of SGLT1 occurs upon the completion of the uninterrupted meshwork of tight junctions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02473267
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  • 7
    Electronic Resource
    Electronic Resource
    Colocalization of tight junction proteins, occludin and ZO-1, and glucose transporter GLUT1 in cells of the blood-ocular barrier in the mouse eye (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 543-551 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The facilitative glucose transporter GLUT1 is abundant in cells of the blood-ocular barrier and serves as a glucose transport mechanism in the barrier. To see the relationship between the glucose transfer function and junctional proteins in the barrier, we examined the localization of GLUT1 and the tight junction proteins, occludin and ZO-1, in the mouse eye. Their localization in the retina, ciliary body, and iris was visualized by double-immunofluorescence microscopy and immunogold electron microscopy. Occludin and ZO-1 were colocalized at tight junctions of the cells of the barrier: retinal pigment epithelial cells, non-pigmented epithelial cells of the ciliary body, and endothelial cells of GLUT1-positive blood vessels. Occludin was restricted to these cells of the barrier. ZO-1 was found, in addition, in sites not functioning as a barrier: the outer limiting membrane in the retina, in the cell border between pigmented and non-pigmented epithelial cells in the ciliary body, and GLUT1-negative blood vessels. These observations show that localization of occludin is restricted to tight junctions of cells of the barrier, whereas ZO-1 is more widely distributed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050316
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  • 8
    Electronic Resource
    Electronic Resource
    Connexin 43 and the glucose transporter, GLUT1, in the ciliary body of the rat (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 209-214 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  To investigate the relationship between the gap junction protein connexin 43 and the glucose transporter GLUT1, their localization was visualized by double-immunofluorescence microscopy using frozen sections as well as immunogold staining of ultrathin frozen sections. In pigmented epithelial cells, most of the GLUT1 was localized along the plasma membrane facing the blood vessels, whereas in non-pigmented epithelial cells, it was present along the plasma membrane facing the aqueous humor. Connexin 43 was abundant in the ciliary body and localized mainly in the gap junctions connecting the pigmented and non-pigmented epithelial cells. Localization of GLUT1 and connexin 43 in the blood-aqueous barrier suggests that GLUT1, connexin 43, and GLUT1 disposed in this order could be a machinery responsible for the transport of glucose across the blood-aqueous barrier.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050033
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  • 9
    Electronic Resource
    Electronic Resource
    Lectin-binding pattern in normal human gastric mucosa (1985)
    Springer
    Histochemistry and cell biology 83 (1985), S. 189-193 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Normal human gastric mucosal cells were examined by light and electron microscopy using lectins as a probe. The ABC method was used with biotinylated lectins for light microscopy and HRP-labeled lectins for electron microscopy. The human gastric mucosal cells revealed specific binding patterns for each lectin by light microscopy. Among the lectins tested, in particular, DBA gave a characteristic pattern. It specifically stained the supranuclear region of surface epithelial cells and the perinuclear region of parietal cells. By electron microscopy, the stacked cisternae and the vesicles of the Golgi apparatus of the surface epithelial cells were positive for the DBA staining. These results show that the DBA-positive supranuclear region observed by light microscopy corresponds to the Golgi apparatus. In the parietal cells, DBA, RCA and ConA bound to the intracellular secretory canaliculi which are invaginations of the cell membrane running around the nucleus in the cytoplasm. Therefore, the tubular perinuclear positive region observed by light microscopy corresponds to the membranes of the intracellular secretory canaliculi. In addition, the ConA reagent stained the endoplasmic reticulum, Golgi apparatus, nuclear envelope, and cell membrane of the parietal cell, which explains the diffuse cytoplasmic staining observed at the light microscopic level with this lectin. Lectins have proved to be very useful for the evaluation of in situ cytochemical aspects of the glycoconjugates characteristic to human gastric mucosal cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00953982
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  • 10
    Electronic Resource
    Electronic Resource
    Ribonucleic acid and lens-regeneration (1952)
    Springer
    Cellular and molecular life sciences 8 (1952), S. 217-218 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Das Verhalten von Nukleinsäuren während der Regeneration der Linse des erwachsenen Molches (Triturus pyrrhogaster) wurde untersucht, wobei hauptsächlich Toluidinblaufärbung kombiniert mit Ribosenuklease verwendet wurde. Am Zytoplasma aller Zellen des Regenerats wurde während sämtlicher Regenerationsstadien eine starke Reaktion auf Ribosenukleinsäure festgestellt. Die normale Linse zeigte im Zytoplasma keine Reaktion auf Ribosenukleinsäure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02170715
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