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  • Immunocytochemistry  (13)
  • bioavailability
  • Springer  (14)
  • International Union of Crystallography
  • 2005-2009
  • 1995-1999  (14)
  • 1980-1984
  • 1965-1969
  • 1995  (14)
Collection
Keywords
Publisher
Years
  • 2005-2009
  • 1995-1999  (14)
  • 1980-1984
  • 1965-1969
Year
  • 1
    Electronic Resource
    Electronic Resource
    Localization of the 110 kDa receptor for laminin in brains of embryonic and postnatal mice (1995)
    Springer
    Cell & tissue research 279 (1995), S. 371-377 
    Details
    ISSN: 1432-0878
    Keywords: Laminin ; Nerve tracts ; Ontogenetic development ; Brain ; Immunocytochemistry ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Laminin, a large glycoprotein of the basement membrane that promotes the growth of nerve cell processes in vitro has also been detected in the brains of developing embryos in situ where it is postulated to promote or guide neural outgrowth. We have investigated the histological and developmental patterns of a receptor to a specific pentapeptide sequence in the A chain of the laminin molecule (PA22-2 or IKVAV) that has been identified as a neuron growth-promoting sequence. Standard immunocytochemical procedures were used to localize the receptor by means of a polyclonal antibody to affinity-purified receptor (MR=110 kDa) from mouse brains. Results for postnatal stages (P) stages (P 1,7,8,25,30,and adult) show that the 110 kDa receptor is localized in fibers in the cortex and hippocampus, in astroglial cells at the surface of the cortex, and in neuronal cell bodies in the hippocampus. In contrast, the A-chain ligand is localized in cell bodies in the same regions at P stages. For embryonic stages (E) (E 14 and E 16) the receptor is localized in bundles of fibers in the superficial and deep cortical layers, and in cell bodies in these regions at E 14 only. Staining for the A chain ligand of the receptor was first seen postnatally. We speculate that the inverse histological pattern of receptor and ligand with respect to cell bodies and fibers may reflect a role in controlling axon guidance during development or repair during regeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318494
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  • 2
    Electronic Resource
    Electronic Resource
    Localization of the 110 kDa receptor for laminin in brains of embryonic and postnatal mice (1995)
    Springer
    Cell & tissue research 279 (1995), S. 371-377 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Laminin ; Nerve tracts ; Ontogenetic development ; Brain ; Immunocytochemistry ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Laminin, a large glycoprotein of the basement membrane that promotes the growth of nerve cell processes in vitro has also been detected in the brains of developing embryos in situ where it is postulated to promote or guide neural outgrowth. We have investigated the histological and developmental patterns of a receptor to a specific pentapeptide sequence in the A chain of the laminin molecule (PA22-2 or IKVAV) that has been identified as a neuron growth-promoting sequence. Standard immunocytochemical procedures were used to localize the receptor by means of a polyclonal antibody to affinity-purified receptor (MR=110 kDa) from mouse brains. Results for postnatal stages (P) stages (P 1,7,8,25,30,and adult) show that the 110 kDa receptor is localized in fibers in the cortex and hippocampus, in astroglial cells at the surface of the cortex, and in neuronal cell bodies in the hippocampus. In contrast, the A-chain ligand is localized in cell bodies in the same regions at P stages. For embryonic stages (E) (E 14 and E 16) the receptor is localized in bundles of fibers in the superficial and deep cortical layers, and in cell bodies in these regions at E 14 only. Staining for the A chain ligand of the receptor was first seen postnatally. We speculate that the inverse histological pattern of receptor and ligand with respect to cell bodies and fibers may reflect a role in controlling axon guidance during development or repair during regeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050293
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  • 3
    Electronic Resource
    Electronic Resource
    The AQP2 water channel: Effect of vasopressin treatment, microtubule disruption, and distribution in neonatal rats (1995)
    Springer
    The journal of membrane biology 143 (1995), S. 165-175 
    Details
    ISSN: 1432-1424
    Keywords: Water channels ; Vasopressin ; Rat kidney ; Immunocytochemistry ; Microtubules ; Cell polarity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Aquaporin 2 is a collecting duct water channel that is located in apical vesicles and in the apical plasma membrane of collecting duct principal cells. It shares 42% identity with the proximal tubule/thin descending limb water channel, CHIP28. The present study was aimed at addressing three questions concerning the location and behavior of the AQP2 protein under different conditions. First, does the AQP2 channel relocate to the apical membrane after vasopressin treatment? Our results show that AQP2 is diffusely distributed in cytoplasmic vesicles in collecting duct principal cells of homozygous Brattleboro rats that lack vasopressin. In rats injected with exogenous vasopressin, however, AQP2 became concentrated in the apical plasma membrane of principal cells, as determined by immunofluorescence and immunogold electron microscopy. This behavior is consistent with the idea that AQP2 is the vasopressin-sensitive water channel. Second, is the cellular location of AQP2 modified by microtubule disruption? In normal rats, AQP2 has a mainly apical and subapical location in principal cells, but in colchicine-treated rats, it is distributed on vesicles that are scattered throughout the entire cytoplasm. This is consistent with the dependence on microtubules of apical protein targeting in many cell types, and explains the inhibitory effect of microtubule disruption on the hydroosmotic response to vasopressin in sensitive epithelia, including the collecting duct. Third, is AQP2 present in neonatal rat kidneys? We show that AQP2 is abundant in principal cells from neonatal rats at all days after birth. The detection of AQP2 in early neonatal kidneys indicates that a lack of this protein is not responsible for the relatively weak urinary concentrating response to vasopressin seen in neonatal rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00233445
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  • 4
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of ribonuclease in yolk granules of adult Rana cttesbeiana oocytes (1995)
    Springer
    Cell & tissue research 280 (1995), S. 259-265 
    Details
    ISSN: 1432-0878
    Keywords: Oocyte ; Yolk granules ; Ribonuclease ; Immunocytochemistry ; Bullfrog, Rana catesbeiana (Anura)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To determine the localization of the pyrimidine-guanine sequence-specific ribonuclease in Rana catesbeiana (bullfrog) oocytes, the RNase was first isolated and used to prepare a specific rabbit antiserum. Only one protein of similar molecular size to the RNase was immunoprecipitated from ovary homogenate by the antiserum, but two bands were observed by Western blotting analysis. These two proteins were shown by further purification of antibody and Western blotting analysis to have similar antigenicity. Immunoprecipitation and Western blotting of tissue homogenates showed that the RNase was found predominantly in the ovary, but not in other tissues. The specific localization of the RNase was determined by immuno-electron microscopy of oocyte sections incubated with the specific antiserum; the yolk granules, but not other organelles, were found to contain the RNase. Most of the RNase was evenly distributed in the lateral amorphous area of the yolk granule but not in the central yolk crystal area which contains stored vitellogenin proteins. Our results indicate that the RNase is compartmentalized in the yolk granules of oocytes, which might prevent damage to cellular RNAs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307797
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  • 5
    Electronic Resource
    Electronic Resource
    Secretory glycoproteins of the subcommissural organ of the dogfish (Scyliorhinus canicula): evidence for the existence of precursor and processed forms (1995)
    Springer
    Cell & tissue research 283 (1995), S. 75-84 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Subcommissural organ ; Secretory glycoproteins ; Antibodies ; Immunochemistry ; Immunocytochemistry ; Dogfish ; Scyliorhinus canicula (Elasmobranchii)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The subcommissural organ of the dogfish, Scyliorhinus canicula (L), has been investigated by use of antibodies and lectins applied to blots and tissue sections processed for light and electron microscopy. Antibodies have been raised against each of the bands that have previously been identified in immunoblots by the use of antisera raised against secretory glycoproteins extracted from the dogfish subcommissural organ, viz., the 600-kDa band and two gel regions including the 475 to 400-kDa and the 145-kDa bands obtained from preparative gels; they are referred to as Ab-600, Ab-475/400, and Ab-145. These antisera and the lectins concanavalin A and wheat germ agglutinin have been used for the staining of: (1) blots of extracts of the dogfish subcommissural organ and optic tectum; (2) tissue sections of the dogfish brain. The findings indicate that the bands of 600, 475 and 400 kDa contain compounds that should be regarded as secretory glycoproteins of the dogfish subcommissural organ. The 600-kDa and 400-kDa bands are labeled by concanavalin A; wheat germ agglutinin labels the 475-kDa band strongly and the other two weakly. Ab-600 reacts with the bands at 600, 475 and 400 kDa and stains materials stored in the rough endoplasmic reticulum and secretory granules of 200–600 nm in diameter. The 600-kDa compound is probably a precursor form. Ab-475/400 stains the same three bands revealed by Ab-600; immunocytochemically, it reacts with two types of secretory granules (200–600 and 800–1200 nm in diameter) but it does not label the rough endoplasmic reticulum. Ab-145 reveals the bands at 600, 475 and 400 kDa and a diffuse zone in the region of 145 kDa; in light-microscopic immunocytochemistry, it behaves as Ab-475/400. The 475-kDa and 400-kDa glycoproteins, and a compound of approximately 145 kDa thus probably correspond to processed forms. Ab-475/400 stains granules present in cell processes ending on local blood vessels and at the leptomeninges. Since this antiserum selectively labels secretory granules, this finding may be taken as evidence for a basal route of secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050514
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  • 6
    Electronic Resource
    Electronic Resource
    Ultrastructural distribution of endogenous immunoglobulin-G in human term amniochorion (1995)
    Springer
    Cell & tissue research 281 (1995), S. 367-374 
    Details
    ISSN: 1432-0878
    Keywords: Placenta ; Amniochorion ; Cytotrophoblast cells ; Immunoglobulin G ; Immunocytochemistry ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Maternal immunoglobulin-G (IgG) is known to be transported across the placental syncytiotrophoblast during the period when the human fetus is incapable of manufacturing these defensive molecules. In this study we investigated the possible role of the amniochorion, that surrounds the amniotic cavity in which the fetus lies, in the transfer of immunoglobulin. Endogenous IgG was localised in the amniochorion by confocal immunofluorescence microscopy and by ultrastructural labelling of ultrathin frozen tissue sections using the protein A-gold technique. Immunoreactivity was identified in the extracellular matrix tissues and necrotic amniotic epithelial cells. Healthy amniotic epithelial cells and cytotrophoblast cells of the chorion laeve were devoid o endogenous IgG. These results suggest a possible non-specific paracellular transport pathway between cytotrophoblast cells, which may conceivably contribute to the acquisition of passive immunity by the fetus, and offer a rational explanation for the presence of small quantities of maternal IgG in the amniotic fluid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00583405
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  • 7
    Electronic Resource
    Electronic Resource
    GABA and glutamate-like immunoreactivity at synapses received by dorsal unpaired median neurones in the abdominal nerve cord of the locust (1995)
    Springer
    Cell & tissue research 280 (1995), S. 325-333 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Nervous system ; insect ; DUM neuron ; Synapses ; Immunocytochemistry ; GABA ; Glutamate ; Locusta migratoria (Insecta) ; Schistocerca gregaria (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Dorsal unpaired median (DUM) neurones in the abdominal ganglia of the locust were impaled with microelectrodes and some were injected intracellularly with horseradish peroxidase so that their synapses could be identified in the electron microscope. Simultaneous recordings from DUM neurones in different abdominal ganglia revealed that they received common postsynaptic potentials from descending interneurones. Post-embedding immunocytochemistry using antibodies against GABA and glutamate was carried out on ganglia containing HRP-stained neurones. GABA-like immunoreactivity was found in 39% (n=82) of processes presynaptic to abdominal DUM neurones and glutamate-like immunoreactivity in 21% (n=42) of presynaptic processes. Output synapses from the DUM neurites were rarely observed within the neuropile. Structures resembling presynaptic dense bars but not associated with synaptic vesicles, were seen in some large diameter neurites.
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    URL: http://dx.doi.org/10.1007/BF00307805
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  • 8
    Electronic Resource
    Electronic Resource
    Leu-callatostatin gene expression in the blowflies Calliphora vomitoria and Lucilia cuprina studied by in situ hybridisation: comparison with Leu-callatostatin confocal laser scanning immunocytochemistry (1995)
    Springer
    Cell & tissue research 280 (1995), S. 355-364 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Leu-callatostatin ; Allatostatins ; Neuropeptides ; In situ hybridisation ; Immunocytochemistry ; Hindgut innervation ; Midgut endocrine cells ; Calliphora vomitoria ; Lucilia cuprina (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. In situ hybridisation studies using a digoxigenin-labelled DNA probe encoding the Leu-callatostatin prohormone of the blowflies Calliphora vomitoria and Lucilia cuprina have revealed a variety of neurones in the brain and thoracico-abdominal ganglion, peripheral neurosecretory neurones, and endocrine cells of the midgut. With two exceptions, the hybridising cells are the same as those previously identified in immunocytochemical studies of sections and whole-mounts using Leu-callatostatin COOH-terminal-specific antisera. Within the brain and suboesophageal ganglion, there is a variety of neurones ranging from a single pair of large cells situated in the dorsal protocerebrum, to the several pairs of neurones in the tritocerebrum, some of which, in immunocytochemical preparations, can be seen to project via axons in the cervical connective to the thoracico-abdominal ganglion. In the medulla of the optic lobes, numerous small interneurones hybridise with the probe, as do clusters of similar-sized neurones close to the roots of the ocellar nerves. These results indicate that the Leu-callatostatin neuropeptides of the brain play a variety of roles in neurotransmission and neuromodulation. There are only three pairs of Leu-callatostatin-immunoreactive neurones in the thoracico-abdominal ganglion, at least two pairs of which project axons along the median abdominal nerve to provide extensive innervation of the hindgut. The Leu-callatostatin peripheral neurosecretory cells are located in close association with both nerve and muscle fibres in the thorax. In addition to neuronal Leu-callatostatin, the presence of the peptide and its mRNA has been demonstrated in endocrine cells in the posterior part of the midgut. These observations provide an example of a named brain/gut peptide in an insect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307808
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  • 9
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of ribonuclease in yolk granules of adult Rana catesbeiana oocytes (1995)
    Springer
    Cell & tissue research 280 (1995), S. 259-265 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Oocyte ; Yolk granules ; Ribonuclease ; Immunocytochemistry ; Bullfrog ; Rana catesbeiana (Anura)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. To determine the localization of the pyrimidine-guanine sequence-specific ribonuclease in Rana catesbeiana (bullfrog) oocytes, the RNase was first isolated and used to prepare a specific rabbit antiserum. Only one protein of similar molecular size to the RNase was immunoprecipitated from ovary homogenate by the antiserum, but two bands were observed by Western blotting analysis. These two proteins were shown by further purification of antibody and Western blotting analysis to have similar antigenicity. Immunoprecipitation and Western blotting of tissue homogenates showed that the RNase was found predominantly in the ovary, but not in other tissues. The specific localization of the RNase was determined by immuno-electron microscopy of oocyte sections incubated with the specific antiserum; the yolk granules, but not other organelles, were found to contain the RNase. Most of the RNase was evenly distributed in the lateral amorphous area of the yolk granule but not in the central yolk crystal area which contains stored vitellogenin proteins. Our results indicate that the RNase is compartmentalized in the yolk granules of oocytes, which might prevent damage to cellular RNAs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307797
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  • 10
    Electronic Resource
    Electronic Resource
    GABA and glutamate-like immunoreactivity at synapses received by dorsal unpaired median neurones in the abdominal nerve cord of the locust (1995)
    Springer
    Cell & tissue research 280 (1995), S. 325-333 
    Details
    ISSN: 1432-0878
    Keywords: Nervous system, insect ; DUM neuron ; Synapses ; Immunocytochemistry ; GABA ; Glutamate ; Locusta migratoria (Insecta) ; Schistocerca gregaria (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Dorsal unpaired median (DUM) neurones in the abdominal ganglia of the locust were impaled with microelectrodes and some were injected intracellularly with horseradish peroxidase so that their synapses could be identified in the electron microscope. Simultaneous recordings from DUM neurones in different abdominal ganglia revealed that they received common postsynaptic potentials from descending interneurones. Post-embedding immunocytochemistry using antibodies against GABA and glutamate was carried out on ganglia containing HRP-stained neurones. GABA-like immunoreactivity was found in 39% (n=82) of processes presynaptic to abdominal DUM neurones and glutamate-like immunoreactivity in 21% (n=42) of presynaptic processes. Output synapses from the DUM neurites were rarely observed within the neuropile. Structures resembling presynaptic dense bars but not associated with synaptic vesicles, were seen in some large diameter neurites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307805
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