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Papers by Peter Parker
Springer eBooks, 1986
Anoxic LTP is a long-lasting increase in synaptic effectiveness that follows a transient anoxic e... more Anoxic LTP is a long-lasting increase in synaptic effectiveness that follows a transient anoxic episode. Such postsynaptic persistent hyperexcitability is found particularly at the hippocampal Schaffer collateral/commissural–CA1 cell synapse.1–6 The mechanisms underlying anoxic LTP has been extensively investigated but not completely understood. With the use of extraand intracellular recording techniques in vitro, Ben-Ari and his colleagues have found that the induction of anoxic LTP is voltage, NMDA receptor and redox state dependent.1,2,7 Recently, we demonstrated that the induction of anoxic LTP is prevented by intracellular injection of the Ca2+ chelator BAPTA into the postsynaptic CA1 neurons.4 Thus a rise in intraneuronal Ca2+ seems to be responsible for a chain of events resulting in an anoxic LTP. However, which Ca2+-dependent processes are essential for the induction of anoxic LTP is still awaiting elucidation. Because the activation of Ca2+-dependent protein kinase (PKC) cascades is known to play an important role in the long-lasting use-dependent strengthening and reduction in synaptic efficacy, such as long-term potentiation (LTP) in the hippocampus and longterm depression (LTD) in the cerebellum,8,9 it is of particular interest to examine whether the induction of anoxic LTP also required the activation of PKC. The present study was undertaken to elucidate this possibility by examining the effect of specific PKC inhibitors on the induction of anoxic LTP in the CA1 neurons of rat hippocampal slices in vitro.
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Journal of Biological Chemistry, 1985
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Journal of Biological Chemistry, 1995
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FEBS Letters, 1994
The mammalian Ptdlns 3‐kinase is shown to be inhibited by low nanomolar concentrations of demetho... more The mammalian Ptdlns 3‐kinase is shown to be inhibited by low nanomolar concentrations of demethoxyviridin, an antifungal agent structurally related to wortmannin. The inhibitory potency of both compounds could be observed in purified Ptdlns 3‐kinase whether or not the regulatory subunit (p85α) was present, suggesting that the inhibitors bind to the catalytic subunit (p110) of the Ptdlns 3‐kinase. These inhibitors also show similar potency against the intrinsic p85‐phosphorylating activity of the p110‐kinase. However, the structurally related Ptdlns 3‐kinase from Saccharomyces cerevisae (Vps34p) is not inhibited by either compound. Both inhibitors target the mammalian Ptdlns 3‐kinase in vitro and in vivo, implying that these compounds should be useful in suppressing Ptdlns 3‐kinase in mammalian systems. The inhibitors did not affect the mammalian Ptdlns 4‐kinase, but they are able to inhibit a membrane‐associated Ptdlns 4‐kinase from Schizosacchromyces pombe.
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FEBS Letters, 1978
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Biochemical and Biophysical Research Communications, 1993
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Pharmacology & Therapeutics, 1991
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bioRxiv (Cold Spring Harbor Laboratory), Jun 19, 2023
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Biochemical Society Transactions, Jun 1, 1999
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Research Square (Research Square), Jul 19, 2023
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Biophysical Journal, Feb 1, 2018
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Breast Cancer Research, Oct 13, 2017
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Molecular and Cellular Biology, Aug 15, 2002
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Annals of Oncology, May 1, 2015
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Elsevier eBooks, 1993
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Biochemical Journal
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Biochemical Journal, Apr 15, 1992
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Gastroenterology, 2021
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Springer eBooks, 1986
Anoxic LTP is a long-lasting increase in synaptic effectiveness that follows a transient anoxic e... more Anoxic LTP is a long-lasting increase in synaptic effectiveness that follows a transient anoxic episode. Such postsynaptic persistent hyperexcitability is found particularly at the hippocampal Schaffer collateral/commissural–CA1 cell synapse.1–6 The mechanisms underlying anoxic LTP has been extensively investigated but not completely understood. With the use of extraand intracellular recording techniques in vitro, Ben-Ari and his colleagues have found that the induction of anoxic LTP is voltage, NMDA receptor and redox state dependent.1,2,7 Recently, we demonstrated that the induction of anoxic LTP is prevented by intracellular injection of the Ca2+ chelator BAPTA into the postsynaptic CA1 neurons.4 Thus a rise in intraneuronal Ca2+ seems to be responsible for a chain of events resulting in an anoxic LTP. However, which Ca2+-dependent processes are essential for the induction of anoxic LTP is still awaiting elucidation. Because the activation of Ca2+-dependent protein kinase (PKC) cascades is known to play an important role in the long-lasting use-dependent strengthening and reduction in synaptic efficacy, such as long-term potentiation (LTP) in the hippocampus and longterm depression (LTD) in the cerebellum,8,9 it is of particular interest to examine whether the induction of anoxic LTP also required the activation of PKC. The present study was undertaken to elucidate this possibility by examining the effect of specific PKC inhibitors on the induction of anoxic LTP in the CA1 neurons of rat hippocampal slices in vitro.
Bookmarks Related papers MentionsView impact
Journal of Biological Chemistry, 1985
Bookmarks Related papers MentionsView impact
Journal of Biological Chemistry, 1995
Bookmarks Related papers MentionsView impact
FEBS Letters, 1994
The mammalian Ptdlns 3‐kinase is shown to be inhibited by low nanomolar concentrations of demetho... more The mammalian Ptdlns 3‐kinase is shown to be inhibited by low nanomolar concentrations of demethoxyviridin, an antifungal agent structurally related to wortmannin. The inhibitory potency of both compounds could be observed in purified Ptdlns 3‐kinase whether or not the regulatory subunit (p85α) was present, suggesting that the inhibitors bind to the catalytic subunit (p110) of the Ptdlns 3‐kinase. These inhibitors also show similar potency against the intrinsic p85‐phosphorylating activity of the p110‐kinase. However, the structurally related Ptdlns 3‐kinase from Saccharomyces cerevisae (Vps34p) is not inhibited by either compound. Both inhibitors target the mammalian Ptdlns 3‐kinase in vitro and in vivo, implying that these compounds should be useful in suppressing Ptdlns 3‐kinase in mammalian systems. The inhibitors did not affect the mammalian Ptdlns 4‐kinase, but they are able to inhibit a membrane‐associated Ptdlns 4‐kinase from Schizosacchromyces pombe.
Bookmarks Related papers MentionsView impact
FEBS Letters, 1978
Bookmarks Related papers MentionsView impact
Biochemical and Biophysical Research Communications, 1993
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Pharmacology & Therapeutics, 1991
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bioRxiv (Cold Spring Harbor Laboratory), Jun 19, 2023
Bookmarks Related papers MentionsView impact
Biochemical Society Transactions, Jun 1, 1999
Bookmarks Related papers MentionsView impact
Research Square (Research Square), Jul 19, 2023
Bookmarks Related papers MentionsView impact
Bookmarks Related papers MentionsView impact
Biophysical Journal, Feb 1, 2018
Bookmarks Related papers MentionsView impact
Breast Cancer Research, Oct 13, 2017
Bookmarks Related papers MentionsView impact
Molecular and Cellular Biology, Aug 15, 2002
Bookmarks Related papers MentionsView impact
Annals of Oncology, May 1, 2015
Bookmarks Related papers MentionsView impact
Elsevier eBooks, 1993
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Biochemical Journal
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Biochemical Journal, Apr 15, 1992
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Gastroenterology, 2021
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