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  • 1
    Electronic Resource
    Electronic Resource
    Developmental and Age-Dependent Changes of 28-kDa Calbindin-D in the Central Nervous Tissue Determined with a Sensitive Immunoassay Method (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: For the quantitative analysis of vitamin D-dependent 28-kDa calcium-binding protein (calbindin-D) in the CNS, we have established a highly sensitive immunoassay method. The antisera were raised in rabbits with purified calbindin-D from rat kidneys, and the antibodies were purified with a calbindin-D-coupled Sepharose column. The purified antibodies were specific for calbindin-D, showing a single band on the immunoblot with the extract of rat kidney or cerebellum. The sandwich-type immunoassay system was prepared by the use of purified monospecific antibodies, and the minimum detection limit of the assay was 0.1 pg or 3.6 amol of calbindin-D, which was sufficiently sensitive for the measurement of calbindin-D content in isolated Purkinje cell bodies at the level of single cells. The average content of calbindin-D in a single Purkinje cell was 0.05 pg. Calbindin-D was detected in most of the rat tissues examined, but it was present predominantly in the kidney and CNS, especially in the cerebellum. Calbindin-D was detected at a similarly low level in the cerebral cortex, cerebellum, and brainstem of rat embryos of 15 gestational days, and it increased gradually but differently in these regions, reaching the respective adult levels by 4–5 weeks of postnatal age. In contrast, kidney calbindin-D increased sharply between 15 gestational days and 3 postnatal days, reaching the adult level by 6 days of age. Calbindin-D levels in the adult rat CNS were affected little by age, whereas the concentrations in human cerebral cortices were significantly low in the aged brain as compared with those in the young brain. However, the concentrations in various regions of cerebral cortex from patients with Alzheimer's disease showed values similar to those in the relevant regions of the age-matched control patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb09287.x
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  • 2
    Electronic Resource
    Electronic Resource
    Highly Sensitive Immunoassay for Rat Brain-Type Creatine Kinase: Determination in Isolated Purkinje Cells (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 46 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Ultrasensitive enzyme immunoassay method for the measurement of rat brain-type creatine kinase BB (CK-BB) was developed by use of purified antibodies specific to the B subunit of creatine kinase. The antibody immunoglobulin G was purified with immunoaffinity chromatography of the antiserum raised in rabbits by injecting the purified rat CK-BB. The assay system consisted of polystyrene balls with immobilized antibody F(ab′)2 fragments and the same antibody Fab' fragments labeled with β-D-galactosidase from Escherichia coli. The assay was specific to the B subunit of CK (CK-B), showing about 10% cross-reactivity with CK-MB, but it did not cross-react with CK-MM and neuron-specific γγ enolase. The minimum detection limit of the assay was 0.1 pg or 1 amol CK-BB, being sufficiently sensitive for the measurement of CK-B contents in the isolated Purkinje cell bodies at the level of single cells. The average content of CK-B in a single Purkinje cell was 1.64 pg. The CK-B concentration in rat cerebellum (about 22 μg/mg protein) was about twofold higher than that (about 13 μg/mg protein) in the cerebrum. High levels (〉 5 μ/mg protein) of CK-B were also found in the peripheral tissues such as gastrointestinal tract and urinary bladder, all of which are composed of smooth muscle. Immunohistochemical localization of CK-B antigens in the CNS revealed that the antigens is distributed not only in the neurons but also in the glial cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb08496.x
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  • 3
    Electronic Resource
    Electronic Resource
    High Expression of the γ5 Isoform of G Protein in Neuroepithelial Cells and Its Replacement of the γ2 Isoform During Neuronal Differentiation in the Rat Brain (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 73 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : High concentrations of G proteins, which include multiple isoforms of each subunit, α, β, and γ, are expressed in the adult brain. In this study, we concentrated attention on changes of these isoforms during embryonic development in the rat brain. Concentrations of γ2 as well as GoAα, GoBα, and β2 were low in early embryogenesis and then increased, whereas expression of γ5, in contrast, was initially high followed by a drop, with only very low levels observed throughout postnatal development. Among the other isoforms, Gi1α, Gsα-short, G12α, G13α, β4, γ3, γ7, and γ12 were present in the embryonic brain at low levels, but their levels markedly increased after birth. In contrast, the levels of Gi2α, Gsα-long, Gq/11α, and β1 were essentially constant throughout. Immunohistochemical staining of the brain vesicles in the embryos showed γ5 to be specifically expressed in the proliferative region of the ventricular zone, whereas γ2 was mainly present in differentiated neuronal cells of the marginal zone. Furthermore, differentiation of P19 mouse embryonal carcinoma cells to neuronal cells with retinoic acid induced the expression of γ2 and a decrease of γ5, the major isoform in the undifferentiated state. These results suggest that neuronal differentiation is responsible for the on/off switch of the expression of γ2 and γ5 subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0732369.x
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  • 4
    Electronic Resource
    Electronic Resource
    Localization of a G protein Gi2 in the cilia of rat ependyma, oviduct and trachea (1998)
    Oxford, UK : Blackwell Science, Ltd
    European journal of neuroscience 10 (1998), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In previous studies, the localization of a pertussis toxin-sensitive G protein was demonstrated in ependymal cilia, but the identification of the subtype of G protein was inconsistent. To clarify this issue, we studied the localization of Goα, Gi1α, Gi3α and Gi2α in the ciliated ependymal cells and in the cilia of some other tissues of rats using specific antibodies. The cilia of the ependymal cells that line the ventricular cavity of the brain were intensely immunoreactive for Gi2α, but not for Goα, Gi1α or Gi3α. Immunoblot analysis demonstrated higher levels of Gi2α in the ependymal cilia-rich pellet than in the motor area of the parietal cortex. At the ultrastructural level, the immunoreactivity specific for Gi2α was found predominantly in the cilia, but rarely in the microvilli or the basal bodies of ependymal cells. In cross-sections, the immunoreactivity specific for Gi2α was observed only in cell membranes, in particular, in the inner electron-dense leaflet of the trilaminar structure. In addition to that in the ependymal cilia, such specific localization of Gi2α was observed in the motile cilia in other tissues, including the oviduct and trachea. By contrast, the stereocilia in the ductus deferens were not immunopositive for Gi2α. These findings suggest that Gi2 might play an important role in the signal transduction in ciliary membrane-associated function(s) of the ependymal cells, oviduct and trachea.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1460-9568.1998.00088.x
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  • 5
    Electronic Resource
    Electronic Resource
    Selective localization of G protein γ5 subunit in the subventricular zone of the lateral ventricle and rostral migratory stream of the adult rat brain (2001)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 79 (2001), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: G proteins play important roles in transmembrane signal transduction, and various isoforms of each subunit, α, β and γ, are highly expressed in the brain. The Gγ5 subunit is a minor isoform in the adult brain, but we have previously shown it to be highly expressed in the proliferative region of the ventricular zone in the rat embryonic brain. We show here that Gγ5 is also selectively localized in a proliferative region in the adult rat brain, including the subventricular zone of the lateral ventricle and rostral migratory stream. The Gαi2 subunit colocalized with Gγ5 in these regions, the two subunits being present in neuronal precursors and ependymal cells but not in proliferating astrocytes. In addition, intense staining of Gγ5 was seen in axons of the olfactory neurons, which are known to regenerate. These results suggest specific roles for Gγ5 in precursor cells during neurogenesis so that this isoform might be a useful biological marker.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2001.00662.x
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  • 6
    Electronic Resource
    Electronic Resource
    Ontogeny of GTP-binding proteins, Gi and Go, in rat retina (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 235-240 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The distribution and the levels of Gi1 (plus Gi3), Gi2, and Go in rat retina were studied immunohistochemically and immunochemically during development. At embryonic day (E) 15, Gi1α/Gi3α was observed in the inner layer of the neural retina, the future nerve fiber layer (NFL), while Gi2α was observed both in the inner and outer layers of the neural retina. No immunoreactivity for Goα was observed. At E18, Gi1α/Gi3α and Gi2α appeared in the inner plexiform layer (IPL), while Goα was faintly immunoreactive only in the NFL. At birth, Gi2α/Gi3α and Goα appeared in the ganglion cell layer. Gi2α was intensely immunoreactive in the NFL and IPL. At postnatal day (P) 10, the inner portions of the retina, from the NFL to the outer plexiform layer, were immunoreactive to Gi1α/Gi3α, Gi2α, and Goα. Gi1α/Gi3α and Goα were distributed characteristically in a laminated pattern in the IPL, but Gi2α was present homogeneously in the IPL. At P12, Gi2α appeared in the outer nuclear layer. As the postnatal days advanced, the laminated pattern of immunoreactivity to Goα in the IPL became diffuse, but immunoreactivity to Gi1α/Gi3α remained. The results of enzyme immunoassays showed that the concentration of Goα increased rapidly from P10 to P15 and reached almost the adult level at P20–P30, while Gi2α decreased until P15 and was almost constant thereafter. These results showed that the distribution of Gi1α/Gi3α, Gi2α, and Goα differs during development, suggesting that each G protein in the developing retina has a unique function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050037
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  • 7
    Electronic Resource
    Electronic Resource
    Contribution of carbon monoxide-producing cells in the gastric mucosa of rat and monkey (1998)
    Springer
    Histochemistry and cell biology 109 (1998), S. 369-373 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Recent studies have shown that carbon monoxide (CO) may function as a gaseous signaling molecule in a similar way to nitric oxide. In the gastrointestinal tract, immunoreactivity against a CO-producing enzyme, heme oxygenase-2 (HO-2), was reported in epithelial cells and neurons of submucosal and myenteric plexus. However, details of the epithelial cells in the gastric mucosa remain unknown. The aim of this study was to clarify if mRNA for HO-2 is expressed in the rat stomach, if HO-2 protein is present in the mucosa, and to define the cell types of the HO-2-immunoreactive cells. HO-2 mRNA and protein were detected in fundic and pyloric mucosa of rat stomach using an RNA protection assay and western blot analysis. Immunohistochemical study showed that HO-2 was localized in parietal cells of the fundic glands and gastrin cells of the pyloric glands of both rat and monkey. The results suggest that HO-2 enzyme is produced in the gastric mucosa, and that CO is released from parietal cells and gastrin cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050237
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  • 8
    Electronic Resource
    Electronic Resource
    Ontogeny of alpha-crystallin subunits in the lens of human and rat embryos (1994)
    Springer
    Cell & tissue research 276 (1994), S. 151-154 
    Details
    ISSN: 1432-0878
    Keywords: Eye ; Lens ; Development, ontogenetic ; αA-crystallin ; αB-crystallin ; Immunohistochemistry ; Human ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The distribution of αA- and αB-crystallin in the developing lens of human (Carnegie stages 13 to 23) and rat embryos (embryonic days E11 to 18) was examined immunohistochemically. In a human embryo at stage 13, the lens placode was already immunoreactive to αB-crystallin, but not to αA-crystallin. At stage 15, the lens vesicle was intensely immunoreactive both to αA- and αB-crystallin. From stages 16 to 23, the lens epithelial cells and fiber cells were immunoreactive to αA- and αB-crystallin. In rat embryos, αA-crystallin appeared in the lens pit at E12, and αB-crystallin appeared in the elongating lens fiber cells at E14. From E15 to E18, the lens epithelial cells and fiber cells were immunoreactive to αA-crystallin. The lens fiber cells were also immunoreactive to αB-crystallin, but the epithelial cells were not. These findings suggest that αB-crystallin appears earlier than αA-crystallin in the human lens, but at a later period than αA-crystallin in the rat lens. αB-Crystallin was not detected in the epithelial cells of the rat lens, but was perisistently present in the epithelial cells of the human lens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00354794
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  • 9
    Electronic Resource
    Electronic Resource
    Ontogeny of alpha-crystallin subunits in the lens of human and rat embryos (1994)
    Springer
    Cell & tissue research 276 (1994), S. 151-154 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Eye – Lens – Development, ontogenetic –αA-crystallin –αB-crystallin – Immunohistochemistry – Human – Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The distribution of αA- and αB-crystallin in the developing lens of human (Carnegie stages 13 to 23) and rat embryos (embryonic days E11 to 18) was examined immunohistochemically. In a human embryo at stage 13, the lens placode was already immunoreactive to αB-crystallin, but not to αA-crystallin. At stage 15, the lens vesicle was intensely immunoreactive both to αA- and αB-crystallin. From stages 16 to 23, the lens epithelial cells and fiber cells were immunoreactive to αA- and αB-crystallin. In rat embryos, αA-crystallin appeared in the lens pit at E12, and αB-crystallin appeared in the elongating lens fiber cells at E14. From E15 to E18, the lens epithelial cells and fiber cells were immunoreactive to αA-crystallin. The lens fiber cells were also immunoreactive to αB-crystallin, but the epithelial cells were not. These findings suggest that αB-crystallin appears earlier than αA-crystallin in the human lens, but at a later period than αA-crystallin in the rat lens. αB-Crystallin was not detected in the epithelial cells of the rat lens, but was persistently present in the epithelial cells of the human lens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00354794
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  • 10
    Electronic Resource
    Electronic Resource
    Ultrastructure of developing muscle in the upper limbs of the human embryo and fetus (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 241 (1995), S. 417-424 
    Details
    ISSN: 0003-276X
    Keywords: Myogenesis ; Upper limb bud ; Human embryo ; Ultrastructure ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: The ultrastructure of the myogenesis, which proceeds along with the appearance of muscle-specific proteins and isozymes, has not been fully described in the upper limb of staged human embryos.Methods: Eight human embryos (Carnegie stage 14-22) and two fetuses (11 and 12 weeks of gestation) were fixed with 5% glutaraldehyde, 4% paraformaldehyde, and 0.2% picric acid in 0.1 M phosphate buffer, pH 7.2. The upper limbs were dissected out and processed for transmission electron microscopy, and sections of the biceps brachii muscle were cut and examined.Results: At stage 14, the myoblasts were loosely scattered in the ventral proximal region of the upper limb bud and had a small amount of cytoplasm with a few intracellular organelles. At stage 16, the myoblasts were spindle shaped and oriented parallel to the axis of the upper limb bud. These cells had irregularly shaped nuclei with prominent nucleoli, rough endoplasmic reticulum (ER), and mitochondria, but no myofilaments were observed. At stages 17-19, rough ER, free ribosomes, and mitochondria increased in number and thick and thin filaments with faint Z-lines appeared in the peripheral cytoplasm of the myotube. The plasma membranes of some neighboring myotubes were continuous, suggesting that these cells were in the initial stages of the fusion process. At stage 22, the striated pattern of the myofilaments became evident and tubular structures appeared around them and near the plasma membrane. In the fetus at the 11th week, the basal lamina began to surround the myotubes, and T-tubules with sarcoplasmic reticulum were observed. Dyads and triads were observed in the myotube of the 12th week fetus.Conclusion: These findings suggest that rapid myogenesis occurs during the late embryonic period in human upper limbs and that the ultrastructural characteristics of mature myotubes are established during the early fetal period. © 1995 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092410317
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