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PDE4A loss puts aging PFC at risk for degeneration [Neuroscience] (2014)

Carlyle, B. C., Nairn, A. C., Wang, M., Yang, Y., Jin, L. E., Simen, A. A., Ramos, B. P., Bordner, K. A., Craft, G. E., Davies, P., Pletikos, M., Šestan, N., Arnsten, A. F. T., Paspalas, C. D.

National Academy of Sciences

In: PNAS - Proceedings of the National Academy of Sciences

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Publication Date: 2014-04-02

Description: The pattern of neurodegeneration in Alzheimer’s disease (AD) is very distinctive: neurofibrillary tangles (NFTs) composed of hyperphosphorylated tau selectively affect pyramidal neurons of the aging association cortex that interconnect extensively through glutamate synapses on dendritic spines. In contrast, primary sensory cortices have few NFTs, even in late-stage disease. Understanding this...

Print ISSN: 0027-8424

Electronic ISSN: 1091-6490

Topics: Biology , Medicine , Natural Sciences in General

Published by National Academy of Sciences

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Regulation of chloride channels by protein kinase C in normal and cystic fibrosis airway epithelia (1989)

M. Li ; J. D. McCann ; M. P. Anderson ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 244(4910): 1353-6.

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Publication Date: 1989-06-16

Description: Apical membrane chloride channels control chloride secretion by airway epithelial cells. Defective regulation of these channels is a prominent characteristic of cystic fibrosis. In normal intact cells, activation of protein kinase C (PKC) by phorbol ester either stimulated or inhibited chloride secretion, depending on the physiological status of the cell. In cell-free membrane patches, PKC also had a dual effect: at a high calcium concentration, PKC inactivated chloride channels; at a low calcium concentration, PKC activated chloride channels. In cystic fibrosis cells, PKC-dependent channel inactivation was normal, but activation was defective. Thus it appears that PKC phosphorylates and regulates two different sites on the channel or on an associated membrane protein, one of which is defective in cystic fibrosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, M -- McCann, J D -- Anderson, M P -- Clancy, J P -- Liedtke, C M -- Nairn, A C -- Greengard, P -- Welsch, M J -- DK27651/DK/NIDDK NIH HHS/ -- HL29851/HL/NHLBI NIH HHS/ -- HL42385/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Jun 16;244(4910):1353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Membrane Transport, University of Iowa College of Medicine, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2472006" target="_blank"〉PubMed〈/a〉

Keywords: Calcium/physiology ; Chloride Channels ; Chlorides/*physiology ; Cystic Fibrosis/*physiopathology ; Enzyme Activation ; Humans ; In Vitro Techniques ; Ion Channels/*physiology ; Membrane Proteins/*physiology ; Protein Kinase C/*physiology ; Respiratory Physiological Phenomena ; Respiratory System/cytology/*physiopathology ; Tetradecanoylphorbol Acetate/pharmacology

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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A phosphatase cascade by which rewarding stimuli control nucleosomal response (2008)

A. Stipanovich ; E. Valjent ; M. Matamales ; [et al.]

Nature Publishing Group (NPG)

In: Nature. 453(7197): 879-84. doi: 10.1038/nature06994.

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Publication Date: 2008-05-23

Description: Dopamine orchestrates motor behaviour and reward-driven learning. Perturbations of dopamine signalling have been implicated in several neurological and psychiatric disorders, and in drug addiction. The actions of dopamine are mediated in part by the regulation of gene expression in the striatum, through mechanisms that are not fully understood. Here we show that drugs of abuse, as well as food reinforcement learning, promote the nuclear accumulation of 32-kDa dopamine-regulated and cyclic-AMP-regulated phosphoprotein (DARPP-32). This accumulation is mediated through a signalling cascade involving dopamine D1 receptors, cAMP-dependent activation of protein phosphatase-2A, dephosphorylation of DARPP-32 at Ser 97 and inhibition of its nuclear export. The nuclear accumulation of DARPP-32, a potent inhibitor of protein phosphatase-1, increases the phosphorylation of histone H3, an important component of nucleosomal response. Mutation of Ser 97 profoundly alters behavioural effects of drugs of abuse and decreases motivation for food, underlining the functional importance of this signalling cascade.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2796210/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2796210/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stipanovich, Alexandre -- Valjent, Emmanuel -- Matamales, Miriam -- Nishi, Akinori -- Ahn, Jung-Hyuck -- Maroteaux, Matthieu -- Bertran-Gonzalez, Jesus -- Brami-Cherrier, Karen -- Enslen, Herve -- Corbille, Anne-Gaelle -- Filhol, Odile -- Nairn, Angus C -- Greengard, Paul -- Herve, Denis -- Girault, Jean-Antoine -- DA10044/DA/NIDA NIH HHS/ -- MH74866/MH/NIMH NIH HHS/ -- P01 DA010044/DA/NIDA NIH HHS/ -- P01 DA010044-020002/DA/NIDA NIH HHS/ -- P01 DA010044-030002/DA/NIDA NIH HHS/ -- P01 DA010044-04/DA/NIDA NIH HHS/ -- P01 DA010044-040002/DA/NIDA NIH HHS/ -- P01 DA010044-05/DA/NIDA NIH HHS/ -- P01 DA010044-050002/DA/NIDA NIH HHS/ -- P01 DA010044-06/DA/NIDA NIH HHS/ -- P01 DA010044-060002/DA/NIDA NIH HHS/ -- P01 DA010044-07/DA/NIDA NIH HHS/ -- P01 DA010044-070002/DA/NIDA NIH HHS/ -- P01 DA010044-08/DA/NIDA NIH HHS/ -- P01 DA010044-080002/DA/NIDA NIH HHS/ -- P01 DA010044-09/DA/NIDA NIH HHS/ -- P01 DA010044-090002/DA/NIDA NIH HHS/ -- P01 DA010044-10/DA/NIDA NIH HHS/ -- P01 DA010044-100002/DA/NIDA NIH HHS/ -- P01 DA010044-11/DA/NIDA NIH HHS/ -- P01 DA010044-110005/DA/NIDA NIH HHS/ -- P01 DA010044-12/DA/NIDA NIH HHS/ -- P01 DA010044-120005/DA/NIDA NIH HHS/ -- P01 DA010044-129002/DA/NIDA NIH HHS/ -- P01 DA010044-13/DA/NIDA NIH HHS/ -- P01 DA010044-130005/DA/NIDA NIH HHS/ -- P01 DA010044-139002/DA/NIDA NIH HHS/ -- P01 DA010044-14/DA/NIDA NIH HHS/ -- P01 DA010044-140005/DA/NIDA NIH HHS/ -- P01 DA010044-149002/DA/NIDA NIH HHS/ -- P01 DA010044-14S1/DA/NIDA NIH HHS/ -- P50 MH074866/MH/NIMH NIH HHS/ -- P50 MH074866-010001/MH/NIMH NIH HHS/ -- P50 MH074866-019001/MH/NIMH NIH HHS/ -- P50 MH074866-020001/MH/NIMH NIH HHS/ -- P50 MH074866-029001/MH/NIMH NIH HHS/ -- P50 MH074866-030001/MH/NIMH NIH HHS/ -- P50 MH074866-039001/MH/NIMH NIH HHS/ -- P50 MH074866-040001/MH/NIMH NIH HHS/ -- P50 MH074866-049001/MH/NIMH NIH HHS/ -- P50 MH074866-050001/MH/NIMH NIH HHS/ -- P50 MH074866-059001/MH/NIMH NIH HHS/ -- England -- Nature. 2008 Jun 12;453(7197):879-84. doi: 10.1038/nature06994. Epub 2008 May 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Inserm, UMR-S 839, 75005 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18496528" target="_blank"〉PubMed〈/a〉

Keywords: Animals ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Dopamine/metabolism ; Dopamine and cAMP-Regulated Phosphoprotein 32/chemistry/genetics/*metabolism ; Food ; Histones/metabolism ; Learning ; Male ; Mice ; Mice, Inbred C57BL ; Motivation ; Motor Activity/physiology ; Neostriatum/cytology ; Neurons/metabolism ; Nucleosomes/*metabolism ; Phosphoprotein Phosphatases/antagonists & inhibitors/*metabolism ; Phosphorylation/drug effects ; Phosphoserine/metabolism ; Protein Transport ; Rats ; *Reward ; *Signal Transduction/drug effects ; Substance-Related Disorders

Print ISSN: 0028-0836

Electronic ISSN: 1476-4687

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Published by Nature Publishing Group (NPG)

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Enhancement of the glutamate response by cAMP-dependent protein kinase in hippocampal neurons (1991)

P. Greengard ; J. Jen ; A. C. Nairn ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 253(5024): 1135-8.

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Publication Date: 1991-09-06

Description: Receptor channels activated by glutamate, an excitatory neurotransmitter in the mammalian brain, are involved in processes such as long-term potentiation and excitotoxicity. Studies of glutamate receptor channels expressed in cultured hippocampal pyramidal neurons reveal that these channels are subject to neuromodulatory regulation through the adenylate cyclase cascade. The whole-cell current response to glutamate and kainate [a non-NMDA (N-methyl-D-aspartate) receptor agonist] was enhanced by forskolin, an activator of adenylate cyclase. Single-channel analysis revealed that an adenosine 3',5'-monophosphate-dependent protein kinase (PKA) increases the opening frequency and the mean open time of the non-NMDA-type glutamate receptor channels. Analysis of synaptic events indicated that forskolin, acting through PKA, increased the amplitude and decay time of spontaneous excitatory postsynaptic currents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greengard, P -- Jen, J -- Nairn, A C -- Stevens, C F -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1135-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716001" target="_blank"〉PubMed〈/a〉

Keywords: Adenosine Triphosphate/pharmacology ; Animals ; Animals, Newborn ; Cells, Cultured ; Colforsin/pharmacology ; Electric Conductivity/drug effects ; Glutamates/metabolism/*pharmacology ; Hippocampus/*physiology ; Ion Channel Gating/drug effects ; Ion Channels/drug effects/*physiology ; Kainic Acid/*pharmacology ; Kinetics ; Membrane Potentials/drug effects ; N-Methylaspartate/*pharmacology ; Neurons/drug effects/*physiology ; Protein Kinases/*metabolism ; Rats ; Receptors, Glutamate ; Receptors, Neurotransmitter/drug effects/*physiology

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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A network of control mediated by regulator of calcium/calmodulin-dependent signaling (2004)

S. V. Rakhilin ; P. A. Olson ; A. Nishi ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 306(5696): 698-701. doi: 10.1126/science.1099961.

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Publication Date: 2004-10-23

Description: Calmodulin (CaM) is a major effector for the intracellular actions of Ca2+ in nearly all cell types. We identified a CaM-binding protein, designated regulator of calmodulin signaling (RCS). G protein-coupled receptor (GPCR)-dependent activation of protein kinase A (PKA) led to phosphorylation of RCS at Ser55 and increased its binding to CaM. Phospho-RCS acted as a competitive inhibitor of CaM-dependent enzymes, including protein phosphatase 2B (PP2B, also called calcineurin). Increasing RCS phosphorylation blocked GPCR- and PP2B-mediated suppression of L-type Ca2+ currents in striatal neurons. Conversely, genetic deletion of RCS significantly increased this modulation. Through a molecular mechanism that amplifies GPCR- and PKA-mediated signaling and attenuates GPCR- and PP2B-mediated signaling, RCS synergistically increases the phosphorylation of key proteins whose phosphorylation is regulated by PKA and PP2B.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rakhilin, S V -- Olson, P A -- Nishi, A -- Starkova, N N -- Fienberg, A A -- Nairn, A C -- Surmeier, D J -- Greengard, P -- DA10044/DA/NIDA NIH HHS/ -- DA12958/DA/NIDA NIH HHS/ -- MH40899/MH/NIMH NIH HHS/ -- NS34696/NS/NINDS NIH HHS/ -- P01 DA010044/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 22;306(5696):698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15499021" target="_blank"〉PubMed〈/a〉

Keywords: Animals ; Calcineurin/metabolism ; Calcineurin Inhibitors ; Calcium/*metabolism ; Calcium Channels, L-Type/metabolism ; Calcium Signaling ; Calmodulin/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neostriatum/cytology/metabolism ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Receptor, Muscarinic M1/metabolism ; Receptors, Dopamine D1/metabolism ; *Signal Transduction

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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Electronic Resource

P2-Purinergic Receptors on Vascular Endothelial Cells (1990)

PIROTTON, S. ; LECOMTE, M. ; ROBAYE, B. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Annals of the New York Academy of Sciences 603 (1990), S. 0

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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.1749-6632.1990.tb37712.x

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THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM (1980)

Nairn, A. C. ; Grand, R. J. A. ; Wall, C. M. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Annals of the New York Academy of Sciences 356 (1980), S. 0

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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.1749-6632.1980.tb29653.x

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8

Electronic Resource

MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin (1992)

Hartwig, J. H. ; Thelen, M. ; Resen, A. ; [et al.]

[s.l.] : Nature Publishing Group

Nature 356 (1992), S. 618-622

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ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] MARCKS in its phosphorylated and dephosphorylated forms bound to F-actin in a specific and saturable manner (Fig. 1). Both the phosphorylated and dephosphorylated forms of the protein cosedimented with skeletal muscle F-actin at a low stoichiometry of about 1 MARCKS polypeptide per 50 actin ...

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1038/356618a0

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