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  • 1
    Electronic Resource
    Electronic Resource
    The light microscopic localization of substance P- and somatostatin-like immunoreactive cells in the larval tiger salamander retina (1986)
    Springer
    Experimental brain research 63 (1986), S. 93-101 
    Details
    ISSN: 1432-1106
    Keywords: Larval tiger salamander retina ; Substance P ; Somatostatin ; Amacrine cells ; Interplexiform cells ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Light microscopic immunocytochemistry was utilized to localize the populations of substance P (SP)- and somatostatin (SOM)-like immunoreactive cells in the larval tiger salamander retina. Of 104 SP-immunostained cells observed, 82% were Type 1 amacrine cells. Another 8% of the SP-cells were classified as Type 2 amacrine cells, while 10% of the SP-cells had their cell bodies located in the ganglion cell layer and were designated as displaced amacrine cells. Each type of SP-like immunoreactive cell was observed in the central and peripheral retina. SP-immunopositive processes were observed in the inner plexiform layer as a sparse plexus in sublamina 1 and as a denser network of fibers in sublamina 5. Seventy-eight percent of the 110 somatostatin-immunopositive cells observed were designated as Type 1 amacrine cells. Another 12% of SOM-cells were classified as displaced amacrine cells, while only two SOM-immunopositive Type 2 amacrine cells were observed. Nine percent of the SOM-cells were designated as interplexiform cells, based on their giving rise to processes distributing in the outer plexiform layer as well as processes ramifying in the inner plexiform layer. Each type of SOM-immunoreactive cell was observed in the central and peripheral retina, with the exception of the Type 2 amacrine cells, whose somas were only found in the central retina. Lastly, SOM-immunopositive processes in the inner plexiform layer appeared as a fine plexus in sublamina 1 and as a somewhat denser network of fibers in sublamina 5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00235650
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization, Localization, and Biosynthesis of an Interstitial Retinol-Binding Glycoprotein in the Human Eye (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Human eyes contain an Mr 135K retinol-binding protein that is analogous to interstitial retinol-binding protein (IRBP) in the subretinal space of bovine eyes. It is a glycoprotein, because it binds 125I-concanavalin A, 125I-wheat germ agglutinin and 125I-Lens culinaris hemagglutinin. It does not bind Ricinus communis agglutinin I. After desialation, it binds Ricinus communis agglutinin I, but loses its capacity to bind wheat germ agglutinin. These observations, coupled with the known specificities of these lectins, suggest that at least one of the oligosaccharide chains is a sialated, biantennary complex type containing fucose. Both by direct analysis of dissected ocular tissues and by immunocytochemistry it was shown that human interstitial retinol binding protein is an extracellular protein that is confined predominantly to the subretinal space. Monkey retinas incubated in vitro in medium containing [3H]leucine were shown to synthesize and secrete this protein into the medium, a conclusion that was confirmed by immunoprecipitation with an immunoglobulin fraction prepared from rabbit antibovine IRBP serum. Virtually no other labeled proteins were detectable in the medium. It is concluded that interstitial retinol-binding protein meets many of the requirements for a putative transport protein implicated in the transfer of retinol between the pigment epithelium and retina during the visual cycle, and that the neural retina may play an important role in regulating its amount in the subretinal space.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb12758.x
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  • 3
    Electronic Resource
    Electronic Resource
    Localization of neurotensin-like immunoreactive amacrine cells in the larval tiger salamander retina (1988)
    Springer
    Experimental brain research 70 (1988), S. 33-42 
    Details
    ISSN: 1432-1106
    Keywords: Retina ; Larval tiger salamander ; Neurotensin ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Light microscopic immunocytochemistry was used to localize the populations of NT-like immunoreactive amacrine cells in the larval tiger salamander retina. Seventy-nine percent of NT-immunostained cells observed in transverse cryo-prepared sections were classified as Type 1 amacrine cells. Another 6% were classified as Type 2 amacrine cells, while 15% of the NT-cells had their cell bodies situated in the ganglion cell layer and were tentatively designated as displaced amacrine cells. Each type of NT-like immunoreactive cell was observed in the central and peripheral retina. NT-immunostained processes were observed to ramify in sublayers 3 and 5 of the inner plexiform layer. An examination of retinal whole mounts revealed that NT-amacrine cells were distributed throughout the center and periphery of the retina at a density of 82 ± 24 cells/ mm2. The dendritic fields of NT-immunostained amacrine and displaced amacrine cells were observed to be either symmetrically or asymmetrically distributed about their somas. Symmetrical dendritic fields were generally oval-shaped and ranged in diameter from 250 to 500 μm (major axis) by 150 to 250 μm (minor axis). Asymmetrical dendritic fields were observed to encompass one-half or less of an imaginary circle surrounding their soma of origin and were orientated in all directions. The processes forming asymmetrical dendritic fields ranged from 75 to 260 μm in length. Furthermore, partial overlap was often observed between the dendritic fields of adjacent NT-amacrine cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271844
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  • 4
    Electronic Resource
    Electronic Resource
    The biosynthesis of protamine during spermatogenesis of the mouse: Extraction, partial characterization, and site of synthesis (1971)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 78 (1971), S. 13-24 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A highly basic, testis-specific, chromosomal protein (MP) can be extracted with acid from testis cells of the mouse, but not from mature spermatozoa. A similar protein (MP') can be isolated from spermatozoa if they are first disrupted with β-mercaptoethanol and urea. The two proteins (MP and MP') are identical as characterized by polyacrylamide gel electrophoresis, Bio-Gel P-10 chromatography, amino-acid analysis and equilibrium ultracentrifugation. They are presumably mouse protamine. Both measurements of the sedimentation velocities of testis cells which synthesize mouse protamine and of the activity of spermatozoa after a pulse label with radioactive arginine show that protamine is synthesized 19 days after the last meiotic S-phase, that is, at an advanced stage of spermiogenesis.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040780104
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