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  • Immunocytochemistry  (27)
  • Springer  (27)
  • 2010-2014
  • 2005-2009
  • 1995-1999  (27)
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  • 1
    ISSN: 1432-0878
    Keywords: Key words: Placental stem villi ; Perivascular contractile sheath ; Molecules of adhesion plaques ; Extracellular matrix molecules ; Immunocytochemistry ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. In previous studies, we have shown that smooth muscle cells and myofibroblast subpopulations of the perivascular stem villous sheath of the human placenta contain focal adhesion plaques and talin immunoreactivity. The close association of these cells to elastic and collagen fibres have led to the assumption of a functional myofibroelastic unit within the perivascular stem villous sheath. Interactions between the extracellular matrix and smooth muscle cells depend on a variety of structural protein assemblies. In the present study, we examined, by immunocytochemistry, whether the molecular assembly of extracellular matrix proteins and molecules of focal adhesions, known to be essential for signal transduction in smooth muscle cells, are also found in smooth muscle cells of the perivascular stem villous sheath of the human placenta. Vascular and extravascular smooth muscle cells were immunoreactive for α-actinin, vinculin, paxillin and tensin, the integrin chains α1 and β1, and the basement membrane components laminin and heparan/-chondroitin sulfate proteoglycan perlecan. pp125FAK did not react. In the extracellular matrix of blood vessel walls and the perivascular stem villous sheath, we found immunoreactivity of fibronectin and collagen types I, VI and undulin (collagen type XIV). From our data we conclude that within the perivascular stem villous sheath, there exists a system of signal transduction molecules, indicating a cross talk between the smooth muscle cells of this sheath and their surrounding extracellular matrix.
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  • 2
    ISSN: 1432-0878
    Keywords: Key words: GABA receptor ; RDL subunit ; Nervous system ; Immunocytochemistry ; Drosophila melanogaster (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. An antibody raised against a peptide based on the C-terminal derived amino acid sequence from a cloned Drosophila melanogaster (fruit fly) gene, Rdl (resistant to dieldrin), was used to investigate localization of a GABA receptor subunit in adult male D. melanogaster. Many regions in the brain and thoracic ganglia were stained with this antibody. For example, staining was detected in the medulla, lobula and lobular plate optic neurpiles. Also stained were the antennal lobe glomeruli, the ellipsoid body of the central complex and the mushroom bodies. These results suggest possible roles for an RDL-like GABA receptor subunit in the processing of olfactory, visual and mechanosensory information in the nervous system of D. melanogaster.
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  • 3
    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.
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  • 4
    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.
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  • 5
    ISSN: 1432-0878
    Keywords: Key words Insect nervous system ; Immunocytochemistry ; Neural development ; Neuropeptide ; Neurohormone ; Locustatachykinin ; Spodoptera litura (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Neuropeptides with similarities to vertebrate tachykinins, designated tachykinin-related peptides (TRPs), have been identified in several insect species. In this investigation we have utilized an antiserum raised to one of the locust TRPs, locustatachykinin-I (LomTK-I), to determine the distribution pattern of LomTK-like immunoreactive (LTKLI) neurons in the developing nervous system of the moth Spodoptera litura. A number of LTKLI neurons could be followed from the larval to the adult nervous system: a set of median neurosecretory cells (MNCs) in the brain, a pair of brain descending neurons and a few sets on neurons in the ventral nerve cord. The distribution of LTKLI neurons in the adult brain is very similar to that seen in other insect species with prominent arborizations in the central body, antennal lobes, mushroom body calyces, optic lobe neuropils and other distinct neuropil areas in the protocerebrum and tritocerebrum. A new finding is the presence of LTKLI neurosecretory cells with axon terminals in the anterior aorta and corpora cardiaca, suggesting for the first time a neurohormonal role of tachykinin-related peptide(s) in insects. During postembryonic development the number of LTKLI neurons in the ventral nerve cord decreases somewhat, whereas the number increases in the brain. Thus the functional roles of TRPs may change to some extent during development.
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  • 6
    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.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of plant growth regulation 15 (1996), S. 95-102 
    ISSN: 1435-8107
    Keywords: Cell cycle ; Cytokinin ; Soybean cells ; Glycine max ; Immunocytochemistry ; S phase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract An immunocytochemical method was used to determine the proportion of cells in the DNA synthesis (S phase) of the mitotic cycle in suspension cultures of soybean (Glycine max (L.) Merr. cv. Acme) callus of cotyledonary origin, the stably cytokinin-dependent tissue used in the cytokinin bioassay devised by Carlos O. Miller. A standard cell synchronization protocol involving hydroxyurea was used to demonstrate the applicability of the immunocytochemical method to this cell culture. Cells were brought to mitotic arrest by cytokinin withdrawal, and the cell division cycle was restarted by the addition of cytokinin. We have followed the pattern of resumption of S phase after the readdition of cytokinin. This pattern reveals the existence of three subpopulations of cells in cytokinin-starved cultures, consistent with the occurrence of three cytokinin-requiring events in the cell cycle: one in mitosis, one in S phase, and one in the G1 phase.
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  • 8
    ISSN: 1435-604X
    Keywords: Heat shock protein 70 (hsp70) ; Carbon dioxide laser ; Sodium arsenite ; Human diploid fibroblast ; Electrophoresis ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Physics , Technology
    Notes: Abstract In a previous study, it was demonstrated that heat shock protein 70 (hsp70) was induced by short duration (〈1 s) carbon dioxide (CO2) laser radiation (10.6Μm. To further characterize the stress response after laser irradiation, the time course of synthesis and cellular localization of hsp70 has been followed. As it had been shown that laser irradiation elevated the temperature to about 67±2
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  • 9
    ISSN: 1615-6102
    Keywords: Ferritin ; Nitrogen fixation ; Nodule development ; Plastid ; Legume ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In eukaryotic organisms ferritin is a protein involved in the storage of iron. The occurrence of ferritin and its relationship to the effectiveness of the nitrogen-fixing activity have been previously studied during the early stages of the nodule development by biochemical methods. We have used immunocytochemistry techniques to determine the precise location of ferritin and the behavior of this protein along the nodule development. The major localization was found in plastids and amyloplasts of infected and uninfected cells of the three legume nodules studied. A decrease of the immunolabelling was observed in infected cells of lupin and soybean senescing nodules and in the senescent zone of indeterminate alfalfa nodules. In the cortex of soybean and lupin nodules, ferritin increased during nodule ageing and the immunogold particles were mainly located in crystalline structures. The putative role of ferritin and plastids during nodule development is discussed.
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  • 10
    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.
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