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  • 1
    Electronic Resource
    Electronic Resource
    Protein Phosphatases 1 and 2A Dephosphorylate B-50 in Presynaptic Plasma Membranes from Rat Brain (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 59 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The protein B-50 is dephosphorylated in rat cortical synaptic plasma membranes (SPM) by protein phospha-tase type 1 and 2A (PP-1 and PP-2A)-like activities. The present studies further demonstrate that B-50 is dephosphorylated not only by a spontaneously active PP-1-like enzyme, but also by a latent form after pretreatment of SPM with 0.2 mM cobalt/20 μg of trypsin/ml. The activity revealed by cobalt/trypsin was inhibited by inhibitor-2 and by high concentrations (μM) of okadaic acid, identifying it as a latent form of PP-1. In the presence of inhibitor-2 to block PP-1, histone H1 (16–64 μg/ml) and spermine (2 mM) increased B-50 dephosphorylation. This sensitivity to poly-cations and the reversal of their effects on B-50 dephosphorylation by 2 nM okadaic acid are indicative of PP-2A-like activity. PP-1- and PP-2A-like activities from SPM were further displayed by using exogenous phosphorylase a and histone H1 as substrates. Both PP-1 and PP-2A in rat SPM were immunologically identified with monospecific antibodies against the C-termini of catalytic subunits of rabbit skeletal muscle PP-1 and PP-2A. Okadaic acid-induced alteration of B-50 phosphorylation, consistent with inhibition of protein phosphatase activity, was demonstrated in rat cortical synaptosomes after immunoprecipitation with affinity-purified anti-B-50 immunoglobulin G. These results provide further evidence that SPM-bound PP-1 and PP-2A-like enzymes that share considerable similarities with their cytosolic counterparts may act as physiologically important phosphatases for B-50.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb08913.x
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  • 2
    Electronic Resource
    Electronic Resource
    Okadaic Acid-Induced Inhibition of B-50 Dephosphorylation by Presynaptic Membrane-Associated Protein Phosphatases (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 57 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The neuronal tissue-specific protein kinase C (PKC) substrate B-50 can be dephosphorylated by endogenous protein phosphatases (PPs) in synaptic plasma membranes (SPMs). The present study characterizes membrane-associated B-50 phosphatase activity by using okadaic acid (OA) and purified 32P-labeled substrates. At a low concentration of [γ-32P] ATP, PKC-mediated [32P]phosphate incorporation into B-50 in SPMs reached a maximal value at 30 s, followed by dephosphorylation. OA, added 30 s after the initiation of phosphorylation, partially prevented the dephosphorylation of B-50 at 2 nM, a dose that inhibits PP-2A. At the higher concentration of 1 μM, a dose of OA that inhibits PP-1 as well as PP-2A, a nearly complete blockade of B-50 dephosphorylation was seen. Heat-stable PP inhibitor-2 (1–2) also inhibited dephosphorylation of B-50. The effects of OA and 1–2 on B-50 phosphatase activity were additive. Endogenous PP-1- and PP-2A-like activities in SPMs were also demonstrated by their capabilities of dephosphorylating [32P] phosphorylase a and [32P] casein. With these exogenous substrates, sensitivities of the membrane-bound phosphatases to OA and 1–2 were found to be similar to those of purified forms of these enzymes. These results indicate that PP-1- and PP-2A-like enzymes are the major B-50 phosphatases in SPMs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb08297.x
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  • 3
    Electronic Resource
    Electronic Resource
    Phosphorylation of the Casein Kinase II Domain of B-50 (GAP-43) in Rat Cortical Growth Cones (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Growth-associated phosphoprotein B-50 is a neural protein kinase C (PKC) substrate enriched in nerve growth cones that has been implicated in growth cone plasticity. Here we investigated whether B-50 is a physiological substrate for casein kinase II (CKII) in purified rat cortical growth cone preparations. Using site-specific proteolysis and known modulators of PKC, in combination with immunoprecipitation, mass spectrometry, and phosphoamino acid analysis, we demonstrate that endogenous growth cone B-50 is phosphorylated at multiple sites, on both serine and threonine residues. Consistent with previous reports, stimulation of PKC activity increased the phosphorylation of only those proteolytic fragments containing Ser41. Under basal conditions, however, phosphorylation was predominantly associated with fragments not containing Ser41. Mass spectrometry of tryptic digests of B-50, which had been immunoprecipitated from untreated growth cones, revealed that in situ phosphorylation occurs within peptides B-50181–198 and B-5082–98. These peptides contain the major and minor in vitro CKII phosphosites, respectively. In addition, cyanogen bromide digestion of immunoprecipitated chick B-50 generated a 4-kDa C-terminal B-50 phosphopeptide, confirming that phosphorylation of the CKII domain occurs across evolutionary diverse species. We conclude that B-50 in growth cones is not only a substrate for PKC, but also for CKII.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69052206.x
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  • 4
    Electronic Resource
    Electronic Resource
    RNA METABOLISM IN THE GOLDFISH RETINA DURING OPTIC NERVE REGENERATION (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 31 (1978), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— In goldfish, regeneration of the optic nerve following axotomy is accompanied by changes in retinal RNA metabolism. Approximately 4 days after unilateral optic nerve crush, there is an increased uptake of 3H-labeled precursors of RNA into cells of the retina as well as an increase in labeling of total retinal RNA following incubation for 3–4 h in vitro. Subfractionation indicates that the resultant labeled free ribosomai RNA has a much higher specific activity than that from membrane-bound ribosomes in post-crush, as compared to normal retinas. Total retinal RNA content also increases, reaching a peak value about 8 days after axotomy, coincident with the time of observed maximum labeling of ribosomal RNA. No change in the total protein or DNA content of the retina is detected during this period as a result of the optic nerve crush.Saturating amounts of uridine or adenosine in the medium eliminate the general effects of enhanced uptake of the precursors on RNA labeling. Elevated labeling of poly(A)-containing RNA in retinal cytoplasm is nevertheless detected 10–14 days after optic nerve crush with no change in the labeling of the polyadenylate segment. A decrease in the labeling of poly(A)-containing nuclear RNA, from a significantly greater amount than that of normal retinas to a significantly lower one, occurs during the period of observed increased labeling of cytoplasmic poly(A)-containing RNA. The results indicate that in addition to changes in RNA precursor metabolism, optic nerve regeneration is characterized by alterations in the labeling of free and membrane-bound retinal ribosomes as well as in the post-transcriptional processing of messenger RNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1978.tb12462.x
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  • 5
    Electronic Resource
    Electronic Resource
    Uridine Metabolism in the Goldfish Retina During Optic Nerve Regeneration: Whole Retina Studies (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Accumulation of radioactivity from [3H]uridine in incubations of whole goldfish retinas is increased in the ipsilateral retina during a period of regeneration that follows unilateral optic nerve crush. Brief incubations to investigate the nature of enhanced labeling of the acid-soluble fraction showed a peak uptake 4 days following crush, with a gradual decrease to control levels by 21 days following crush. That nucleoside uptake may not mediate the effect is supported by the observation that the rate of uptake of 5′-deoxyadenosine, a nonmetabolizable nucleoside analog, is the same in post-crush (PC) and normal (N) retinal incubations. Following brief incubations of PC and N retinas with [3H]uridine, there is enhanced labeling in PC retinas relative to N retinas of recovered UMP, UDP, UTP, and uridine nucleotide sugars, whereas recovery of labeled uridine itself is slightly decreased. The results suggest that the increased accumulation of radioactivity in PC retinas following incubation with uridine reflects an increase in the activities of retinal uridine kinase and uridine nucleotide kinases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb01713.x
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  • 6
    Electronic Resource
    Electronic Resource
    Uridine Metabolism in the Goldfish Retina During Optic Nerve Regeneration: Cell-Free Preparations (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The activities of uridine kinase (EC 2.7.1.48), uridine monophosphate (UMP) kinase (EC 2.7.1.3.14), and uridine diphosphate (UDP) kinase (EC 2.7.4.6) were measured in retinal high-speed supernatant fractions following unilateral optic nerve crush in the goldfish. The enzyme activities followed a similar time course, with initial increases 2-3 days following nerve crush, peak activity at 4 days, and a gradual return to basal levels by day 21. The magnitude of the stimulation on day 4 was about 35% in each case. Activities of two enzymes of intermediary metabolism, pyruvate kinase (EC 2.7.1.40) and lactic dehydrogenase (EC 1.1.1.27), were not altered, indicating that the coordinate increases in nucleoside and nucleotide kinase activities were specific responses to the nerve injury. The increased labeling could not be explained by altered phosphohydrolytic activities. The nature of the enhancement was further studied in UDP kinase, the most active of the kinases examined. Neither low-molecular-weight components nor substrate availability could account for the observed increase in UDP kinase in the 4 day post-crush retinas. The Km, for UDP was unaltered, and a mixing experiment did not support the possibility that stimulatory or inhibitory factors played a role. The enhancement of UDP kinase activity was blocked by injection of actinomycin D following nerve crush. The results suggest that the observed increases in enzymes of uridine metabolism result from their increased formation following nerve crush.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb01714.x
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  • 7
    Electronic Resource
    Electronic Resource
    Corticosteroid-Induced Proteins in Brain (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 746 (1994), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1994.tb39227.x
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  • 8
    Electronic Resource
    Electronic Resource
    CORTICOTROPHIN RELEASING FACTOR ACTIVITY IN THE BRATTLEBORO RAT MEDIAN EMINENCE (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 394 (1982), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1982.tb37473.x
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  • 9
    Electronic Resource
    Electronic Resource
    Stereoselective binding and activity of oxotremorine analogs at muscarinic receptors in rat brain (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 4 (1992), S. 463-468 
    Details
    ISSN: 0899-0042
    Keywords: muscarinic receptors ; oxotremorine derivatives ; stereoselectivity ; adenylyl cyclase ; phosphoinositide metabolism ; receptor autoradiography ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The activities of the enantiomers of BM-5 were examined to measure muscarinic cholinergic selectivity in the central nervous system. Autoradiographic studies assessed the ability of each enantiomer to inhibit the binding of [3H]-(R)-quinuclidinyl benzilate ([3H]-(R)-QNB) to muscarinic receptors in the rat brain. (+)-(R)-BM-5 inhibited [3H]-(R)-QNB binding to rat brain sections at concentrations below 1.0 μM, while 100-fold higher concentrations of ( - )-(S)-BM-5 were required for comparable levels of inhibition. Analysis of the autoradiograms indicated that both stereoisomers had a similar distribution of high affinity binding sites. Each enantiomer displayed higher affinity for muscarinic receptors in the superior colliculi and lower affinity for receptors in the cerebral cortex and hippocampus. (+)-(R)-BM-5 and oxotremorine inhibited adenylyl cyclase activity in the cerebral cortex with efficacies comparable to that for acetylcholine. (+)-(R)-BM-5 was 26-fold more potent than ( - )-(S)-BM-5 in inhibiting adenylyl cyclase. Oxotremorine-M and carbamylcholine stimulated phosphoinositide turnover in the cerebral cortex. Oxotremorine had lower activity and (+)-(R)-BM-5 was essentially inactive at comparable concentrations. The difference in activity of the two enantiomers indicates a remarkable stereochemical selectivity for muscarinic receptors. The stereoselectivity index is comparable for both the autoradiographic assays (48) and measures of adenylyl cyclase activity (26) in the cerebral cortex. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chir.530040802
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