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  • 1
    Electronic Resource
    Electronic Resource
    Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors (1999)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 400 (1999), S. 761-766 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The assembly of signalling molecules into macromolecular complexes (transducisomes) provides specificity, sensitivity and speed in intracellular signalling pathways,. Rod photoreceptors in the eye contain an unusual set of glutamic-acid-rich proteins (GARPs) of unknown function. GARPs exist as ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/23468
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  • 2
    Electronic Resource
    Electronic Resource
    Impaired formation of the inner retina in an AChE knockout mouse results in degeneration of all photoreceptors (2004)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 20 (2004), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Blinding diseases can be assigned predominantly to genetic defects of the photoreceptor/pigmented epithelium complex. As an alternative, we show here for an acetylcholinesterase (AChE) knockout mouse that photoreceptor degeneration follows an impaired development of the inner retina. During the first 15 postnatal days of the AChE–/– retina, three major calretinin sublaminae of the inner plexiform layer (IPL) are disturbed. Thereby, processes of amacrine and ganglion cells diffusely criss-cross throughout the IPL. In contrast, parvalbumin cells present a nonlaminar IPL pattern in the wild-type, but in the AChE–/– mouse their processes become structured within two ‘novel’ sublaminae. During this early period, photoreceptors become arranged regularly and at a normal rate in the AChE–/– retina. However, during the following 75 days, first their outer segments, and then the entire photoreceptor layer completely degenerate by apoptosis. Eventually, cells of the inner retina also undergo apoptosis. As butyrylcholinesterase (BChE) is present at a normal level in the AChE–/– mouse, the observed effects must be solely due to the missing AChE. These are the first in vivo findings to show a decisive role for AChE in the formation of the inner retinal network, which, when absent, ultimately results in photoreceptor degeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1460-9568.2004.03753.x
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  • 3
    Electronic Resource
    Electronic Resource
    Mutations in the gene encoding the basal body protein RPGRIP1L, a nephrocystin-4 interactor, cause Joubert syndrome (2007)
    [s.l.] : Nature Publishing Group
    Nature genetics 39 (2007), S. 882-888 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Protein-protein interaction analyses have uncovered a ciliary and basal body protein network that, when disrupted, can result in nephronophthisis (NPHP), Leber congenital amaurosis, Senior-Løken syndrome (SLSN) or Joubert syndrome (JBTS). However, details of the molecular mechanisms ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng2069
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  • 4
    Electronic Resource
    Electronic Resource
    Centrin in the photoreceptor cells of mammalian retinae (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 55-64 
    Details
    ISSN: 0886-1544
    Keywords: retina ; photoreceptor cells ; cytoskeleton ; centrin ; Ca2+-binding proteins ; mammals ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Photoreceptor cells of vertebrate retinae are highly specialized ciliary cells. Their non-motile ciliated structure is restricted to the so-called connecting cilium at the joint between the light sensitive outer segment and the metabolically active inner segment. Extensive bidirectional intracellular transport between both segments is forced to occur through this tight connecting cilium. In the present study it is shown that the Ca2+-binding, phospho-protein centrin is present in mammalian retinae. Western blot and immunoprecipitation experiments reveal that anti-centrin antibodies react with purified photoreceptor cell fractions of retinae in bands at a molecular weight of 20 kDa, the molecular weight of centrins found in other cells. Indirect immunofluorescence analysis of cryosections through retinae of different mammalian species show that centrin is present only in centrosomes and basal bodies but also more extensively at the linkage between the inner and the outer segment of the photoreceptor cells. Immunocytological studies on isolated rod cells and immunoelectron microscopy clearly demonstrate a unique presence of centrin in the connecting cilium of photoreceptor cells. High molecular identity between centrins in lower eukaryotes and mammals indicates that centrin may play a role in cellular motility and/or in microtubule severing in the mammalian retina. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970320107
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  • 5
    Electronic Resource
    Electronic Resource
    Tropomyosin is co-localized with the actin filaments of the scolopale in insect sensilla (1991)
    Springer
    Cell & tissue research 265 (1991), S. 11-17 
    Details
    ISSN: 1432-0878
    Keywords: Sensilla ; Mechanoreceptors ; Scolopidia ; Actin filaments ; Tropomyosin ; Cryofixation ; Immunohistochemistry ; Immunogold ultrahistochemistry ; Periplaneta americana, Schedorhinotermes lamanianus (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immuno-electron microscopy confirms that the scolopale, a characteristically prominent cytoskeletal element of insect scolopidia, is composed mainly of actin filaments. Immunohistochemistry reveals that these filaments are co-localized with tropomyosin. Myosin S1-decoration shows that their polarity is unidirectional. Antibodies to α-actinin do not bind within the scolopale. The association of these actin filaments with tropomyosin in the absence of myosin, together with their uniform polarity, strongly suggests that, in the scolopale, they have a stabilizing rather than contractile function. Filament elasticity would appear to be important for stimulation. The degree of elasticity may well be governed by the extent of tropomyosin binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318134
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  • 6
    Electronic Resource
    Electronic Resource
    Centrin- and α-actinin-like immunoreactivity in the ciliary rootlets of insect sensilla (1991)
    Springer
    Cell & tissue research 266 (1991), S. 231-238 
    Details
    ISSN: 1432-0878
    Keywords: Ciliary rootlets ; Sensilla ; Mechanoreceptors ; α-Actinin ; Centrin ; Cryofixation ; Immunohistochemistry ; Periplaneta americana, Schedorhinotermes lamanianus (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Long ciliary rootlets are a characteristic feature of the dendritic inner segments of the sensory cells in insect sensilla. These rootlets are composed of highly ordered filaments and are regularly cross-striated. Collagenase digestion and immunohistochemistry reveal that the rootlets are probably not composed of collagen fibers. However, double-labeling experiments with phalloidin and anti-α-actinins show that antibodies to α-actinin react with the ciliary rootlets of the sensilla, but do not stain the scolopale, which is composed of actin filaments as visualized by phalloidin. Antibodies to centrin, a contractile protein isolated from flagellar rootlets of green algae, also stain the ciliary rootlets. Within the ciliary rootlets of insect sensilla, α-actinin may be associated with filaments other than actin filaments. The immunohistochemical localization of a centrin-like protein suggests that contractions probably occur within the rootlets. The centrin-like protein may play a role during the mechanical transduction or adaptation of the sensilla.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318178
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  • 7
    Electronic Resource
    Electronic Resource
    Distribution of F-actin in the compound eye of the blowfly, Calliphora erythrocephala (Diptera, Insecta) (1991)
    Springer
    Cell & tissue research 263 (1991), S. 399-403 
    Details
    ISSN: 1432-0878
    Keywords: Compound eyes ; Cytoskeleton ; Actin filaments ; Cytochemistry ; Phalloidin ; Calliphora erythrocephala (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Filaments that probably consist of actin have been observed by electron microscopy in various cells and structures of the compound eye of insects and crustaceans. The overall distribution of F-actin in the compound eye of Calliphora erythrocephala was studied using fluorescent phalloidins as specific probes for F-actin. F-actin is localized (1) in the rhabdomeres, (2) in the Semper cells, (3) in the basement membrane, and (4) associated with desmosomes and membranes. It is concluded that the actin filaments present in the compound eye are involved in mechanical stabilization (e.g., within microvillar processes of the Semper cells and in association with intercellular contacts) and in motile phenomena (e.g., in the rhabdomeric microvilli).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318782
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  • 8
    Electronic Resource
    Electronic Resource
    Actin filaments: the main components of the scolopale in insect sensilla (1990)
    Springer
    Cell & tissue research 261 (1990), S. 85-96 
    Details
    ISSN: 1432-0878
    Keywords: Sensilla ; Scolopidia ; Thermoreceptors ; Hygroreceptors ; Actin filaments ; Cryofixation ; Highpressure freezing ; Immunohistochemistry ; Antheraea pernyi, Periplaneta americana, Schedorhinotermes lamanianus (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Two types of insect sensilla, mechanosensitive scolopidia and thermo-/hygrosensitive poreless sensilla contain a scolopale, which consists of numerous microtubules embedded in bundles of filaments (7–10 nm in diameter). The bundles are readily seen in the electron microscope in cryofixed (high-pressure freezing and rapid injection) and substituted samples. The filaments can be identified as actin filaments by using fluorescent phalloidins. Both electron microscopy and Triton-extraction exeriments reveal mechanical linkage between the main components in both types of sensilla. Since myosin appears to be absent in the scolopale, the actin filaments are unlikely to be involved in any contraction mechanism; these filaments more probably provide mechanical stability. The functional properties of the scolopale are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00329441
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