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  • 1
    ISSN: 1432-0878
    Keywords: Nucleus preopticus ; Nucleus lateralis tuberis ; Corticotropin-releasing factor (CRF) ; Arginine vasotocin (AVT) ; Immunocytochemistry ; Catostomus commersoni (Teleostei)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The peroxidase-antiperoxidase immunocytochemical procedure was used to study the distribution of ovine corticotropin-releasing factor (CRF) and arginine vasotocin (AVT) immunoreactivities sequentially in the same sections or in adjacent sections of the brain and pituitary of Catostomus commersoni. It was found that all CRF-immunoreactive (IR) neurons in the nucleus preopticus (NPO) also contained AVT immunoreactivity. Co-localization of both immunoreactivities was also observed in fibres forming the preoptic-pituitary tract and in the neurohypophyseal digitations, the IR-CRF and IR-AVT fibres projecting mainly to the neurointermediate lobe (NIL) of the pituitary. An additional population of exclusively IR-AVT neurons and fibres in the NPO, preoptic-pituitary tract and NIL was also observed. Exclusive CRF-immunostaining was found in neurons of the nucleus lateralis tuberis (NLT), in fibres distributed in some diencephalic nuclei and in the neurohypophyseal digitations in the region of the rostral pars distalis (RPD). These results suggest (i) that CRF- and AVT-like substances, present in NIL fibres (probably originating in the NPO), may have an integrated role in the release of the cell products from the pars intermedia, and (ii) that the control of corticotrops in the rostral pars distalis, innervated exclusively by IR-CRF fibres (probably originating in the NLT), does not require a simultaneous presence of CRF- and AVT-like substances.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Subcommissural organ ; Secretory activity, neural control ; Transplantation ; Long-spacing collagen ; Immunocytochemistry ; Molecular markers (neuronal, glial) ; Electron microscopy ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary There is increasing evidence that, in the rat, a serotonin-mediated neural input may have an inhibitory influence on the secretory activity of the subcommissural organ (SCO). In the present investigation the rat SCO was studied 7, 30 and 90 days after transplantation under the kidney capsule, an area devoid of local serotonin-containing nerves. The grafted tissue was examined by use of immunocytochemistry employing a series of primary antisera, lectin histochemistry and transmission electron microscopy. The grafted SCO survived transplantation and contained, in addition to secretory ependymal and hypendymal SCO-cells, also elements immunoreactive with antisera against glial fibrillary acidic protein or S-100 protein. In transplants, SCO-cells produced a material displaying the characteristic immunocytochemical and lectin-binding properties of SCO-cells observed under in-situ conditions. The ependymal cells lined 1–3 small cavities, which contained secretory material. A fully developed structural equivalent of Reissner's fiber was, however, never found. The immunocytochemical and ultrastructural study of the grafted SCO showed an absence of nerve fibers within the graft and suggested a state of enhanced secretory activity. A network of protruding basal lamina structures connected the secretory cells to the newly formed capillaries revascularizing the SCO. One week after transplantation, long-spacing collagen started to appear in expanded areas of such laminar networks and also in the perivascular space. It is suggested (i) that the formation of long-spacing forms of collagen is triggered by factors provided by the SCO-secretory cells, and (ii) that secretory material of the ependymal and hypendymal cells may reach the reticular extensions of the basal lamina. In contrast to the SCO in situ, the grafted SCO-cells showed a positive immunoreaction for neuron-specific enolase. They became surrounded by a S-100-immunoreactive glial sheath that separated them from other transplanted cell types and the adjacent kidney tissue of the host.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 236 (1984), S. 171-180 
    ISSN: 1432-0878
    Keywords: Immunocytochemistry ; Ultrastructure ; Supraoptic nucleus ; Neuropil ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The neuropil located ventral to the SON was investigated by the use of immunoperoxidase staining for neurophysins, oxytocin and vasopressin, and electron miroscopy. The study was performed in six groups of rats: 1) control; 2) infusion of isotonic saline into the CSF; 3) infusion of hypertonic saline into the CSF; 4) drinking hypertonic saline for 4 days; 5) same as group 4 but injection of colchicine into the CSF on second day of dehydration; 6) salt loading for 3 months. In the control rats the ventral neuropil contained a few immunoreactive processes, the general morphology of which was completely different from that of the neurosecretory axons emerging from the SON at its dorsal aspect. In rats of groups 3 to 6 the ventral processes (VP) became loaded with neurosecretory granules, whereas the perikarya and axons were depleted. Based on their general morphology and reactivity pattern it is suggested that the VP are dendrites. Most of these “dendrites” were embedded in a glial cushion formed by the processes of a particular type of marginal glia. Some of these “dendrites” enveloped an arteriole penetrating the optic tract. All VP were rich in synaptic contacts. The possibility that the VP of neurosecretory cells may be functionally related to the subarachnoid CSF and the arteriolar blood flow is discussed.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 292 (1998), S. 239-250 
    ISSN: 1432-0878
    Keywords: Key words Subcommissural organ ; Reissner’s fiber ; Glycoprotein sequencing ; Large size mRNA ; Bovine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The bulk of the secretion of the subcommissural organ is formed by glycoproteins that appear to be derived from two precursor forms of 540 and 320 kDa. Upon release into the ventricle, these glycoproteins aggregate to form Reissner’s fiber. We report the isolation of three cDNA clones from a cDNA library prepared from bovine subcommissural organ RNA, by using an anti-Reissner’s fiber serum for immunoscreening. Inserts of 0.7, 1.2, and 2.5 kb were amplified by the polymerase chain reaction, subcloned into pUC18 vector, and sequenced. Although restriction mapping of the three inserts initially suggested that all of them were derived from the same mRNA, sequence analysis showed that a short non-homologous region was present in the 0.7-kb insert when compared with the 1.2-kb and 2.5-kb inserts, suggesting that they corresponded to two different, although highly homologous, mRNAs. Northern analyses showed a single mRNA species of approximately 9.5 kb present in the subcommissural organ and missing in the choroid plexus, brain cortex, and liver. In situ hybridization confirmed that the expression of the RNA was restricted to cells of the bovine subcommissural organ. Polyclonal antibodies raised against a synthetic peptide, whose amino-acid sequence was deduced from the 2.5-kb cDNA, reacted specifically with the bovine and rat subcommissural organ-Reissner’s fiber complex. In immunoblots of bovine subcommissural organ, this antibody revealed the precursor 540-kDa form and its putative processed form of 450 kDa. It is concluded that the cloned cDNA encodes for the major constitutive glycoprotein of Reissner’s fiber, here designated as RF-Gly I. The sequenced region of RF-Gly I displays a high degree of homology with some regions of the von Willebrand factor and certain mucins; it also displays two motifs homologous with repeats present in proteins of the spondin family and other proteins. A core sequence of the RF-Gly I repeats suggests that this molecule displays protein-binding properties.
    Type of Medium: Electronic Resource
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