Regulation by cAMP and vasoactive intestinal peptide of phosphorylation of specific proteins in striatal cells in culture.

Girault, Jean‐Antoine; Shalaby, Ismail A.; Rosen, N; Greengard, Paul

doi:10.1073/pnas.85.20.7790

Cited by 46 publications

(37 citation statements)

References 27 publications

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“…Therefore ARPP-21 was measured by in vitro phosphorylation with the catalytic subunit of cAMP-dependent protein kinase (a gift of A. C. Nairn) and [-32P]ATP followed by immunoprecipitation with a specific antiserum (G154) as described (20). Comparison of data obtained from immunoblots and phosphorylation/immunoprecipitation for ARPP-16, ARPP-19, and DARPP-32 showed that the two methods gave similar results (data not shown).…”

mentioning

confidence: 78%

Striatal phosphoproteins in Parkinson disease and progressive supranuclear palsy.

Girault

Raisman‐Vozari

Agid

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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This study was undertaken to evaluate the levels of cAMP-regulated phosphoproteins in the striatum of patients with neurodegenerative diseases of the dopaminergic system. Postmortem samples of caudate nucleus and putamen from 24 control subjects, 23 patients with Parkinson disease, and 13 patients with progressive supranuclear palsy were studied with immunoblotting techniques. The levels of tyrosine hydroxylase were reduced in patients with Parkinson disease (levels were 24% and 10% of controls in caudate nucleus and putamen, respectively) and with progressive supranuclear palsy (levels were 11% and 6% of controls in caudate nucleus and putamen, respectively). Five phosphoproteins, which are present in striatal neurons and are likely to play a role in the postsynaptic actions of dopamine, were measured. These

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mentioning

confidence: 78%

Striatal phosphoproteins in Parkinson disease and progressive supranuclear palsy.

Girault

Raisman‐Vozari

Agid

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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“…Involvement of protein phosphatases in the regulation of neuronal currents by 5-HT and cAMP has also been reported in Aplysia californica (21). The reduced phosphatase activity that we induced with 8-Br-cAMP or 5-HT could have resulted from a sustained activity of cAMP-regulated phosphatase inhibitors, such as protein phosphatase inhibitor 1 or the 32-kDa dopamine-and cAMP-regulated phosphoprotein (DARPP-32), that are highly expressed in colliculi neurons (20,(22)(23)(24). How the sustained activity of these inhibitors could be maintained after the transient activation of PKA remains to be demonstrated.…”

Section: Discussionmentioning

confidence: 99%

cAMP-dependent, long-lasting inhibition of a K+ current in mammalian neurons.

Ansanay

Dumuis

Sebben

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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We report the long-term modulation of K+ channels by cAMP in cultured murine colliculi neurons. A short (1-2 s) application of 8-Br-cAMP induced a long-lasting broadening of the action potential, a loss of after-hyperpolarization, and a reduction in spike accommodation. In agreement with these changes, 8-Br-cAMP produced a longlasting (2 hr) inhibition of a K+ current. These effects were also observed after a short activation of the pituitary adenylyl cyclase-activating polypeptide, 6-adrenergic, and 5-hydroxytryptamine type 4 (5-HT4) receptors, all known to increase cAMP. A transient activation of the cAMP-dependent protein kinase and a long-lasting inhibition of phosphatases (up to 2 hr) were detected. The blockade of the K+ current resulting from a brief application of 8-Br-cAMP or 5-hydroxytryptamine was prolonged from 2 to 4 hr when proteinserine/threonine phosphatases 1 and 2A were inhibited with 10 nM okadaic acid. The critical steps following the cAMPdependent protein kinase activation and resulting in a longterm blockade of phosphatases are discussed in this report.Neurotransmitters and hormones elevate the intracellular level of cAMP through their interaction at the membrane surface with specific receptors which are positively coupled to adenylyl cyclase via a stimulatory guanine nucleotide-binding protein (Gs protein). The cellular responses to an increase in intracellular cAMP are determined by the cell-specific substrate proteins that are phosphorylated by the cAMPdependent protein kinase (PKA). These neuronal substrate proteins include proteins involved in transmitter release, neurotransmitter synthesis, and ion channel function. Ion channels known to be phosphorylated by PKA include the glutamate and nicotinic acetylcholine receptors and voltage-dependent Na+, Ca2+, and K+ channels such as transient (IA), delayed, and Ca2+-activated K+ channels (1, 2).We have recently identified a cAMP-inhibited K+ current in cultured colliculi neurons isolated from the embryonic mouse (3). However, the physiological significance of this receptormediated K+ channel modulation remains to be determined. One physiological consequence of cAMP-mediated inhibition of K+ channels is the prolonged enhancement of transmitter release which underlies the long-term sensitization of the Aplysia californica gill withdrawal reflex (4, 5). Although some forms of long-term potentiation of synaptic transmission in the mammalian brain have been shown to involve either K+ channels (6) or cAMP (7-9), there is no direct evidence for an implication of cAMP-regulated K+ channels. We addressed this question by examining the long-term effects of a brief elevation of the intracellular concentration in cAMP on excitability and K+ current activity in cultured colliculi neurons For protein phosphatase assays, 100 ,uM 8-Br-cAMP or 10 p.M serotonin (5-hydroxytryptamine, 5-HT) was added to the culture medium for 5 min at 37°C. The neurons were then washed three times with culture medium. The neuron suspension was immediately homogenized a...

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“…It has recently been shown that phosphorylation of in the choroid plexus of the rat is regulated by norepinephrine and 5-HT (Snyder et al, 1992) and that DARPP-32 therefore may play a role in the control of secretion of cerebrospinal fluid. An increase in phosphorylation of striatal ARPP-21, ARPP-19, and ARPP-16 by vasoactive intestinal peptide in vitro has also been demonstrated (Girault et al, 1988).…”

Section: Functional Implicationsmentioning

confidence: 96%

Expression of mRNAs encoding ARPP-16/19, ARPP-21, and DARPP-32 in human brain tissue

et al. 1994

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In this study we have isolated and sequenced human cDNAs for the phosphoproteins DARPP-32, ARPP-21, and ARPP-16/19, and have compared these sequences to previously characterized bovine and rat cDNAs. In situ hybridization and Northern blot analysis with the human cDNA probes were used to study the expression of mRNAs encoding ARPP-16/19, ARPP-21, and DARPP-32 in human postmortem brain tissue. In situ hybridization was performed using horizontal whole hemisphere sections. Five representative levels of the brain ranging from 71 mm to 104 mm ventral to vertex were examined. All three probes showed distinct hybridization patterns in the caudate nucleus, putamen, nucleus accumbens, and the amygdaloid complex. For ARPP-16/19 mRNA, a hybridization signal comparable to the signal in caudate nucleus, putamen, and nucleus accumbens was also detected in the neocortex. ARPP- 21 and DARPP-32 mRNA, on the other hand, were present in lower levels in neocortical regions. DARPP-32 mRNA was abundant in the cerebellar cortex at the level of the Purkinje cell layer. High levels of ARPP- 16/19 and ARPP-21 mRNA were also found in the cerebellar cortex, where they were confined to deeper layers. The present result demonstrate that mRNAs for the three phosphoproteins are expressed in overlapping, but also distinct, areas of the human brain that in many cases coincide with previously described distribution of the dopamine D1 receptor.

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Regulation by cAMP and vasoactive intestinal peptide of phosphorylation of specific proteins in striatal cells in culture.

Cited by 46 publications

References 27 publications

Striatal phosphoproteins in Parkinson disease and progressive supranuclear palsy.

Striatal phosphoproteins in Parkinson disease and progressive supranuclear palsy.

cAMP-dependent, long-lasting inhibition of a K+ current in mammalian neurons.

Expression of mRNAs encoding ARPP-16/19, ARPP-21, and DARPP-32 in human brain tissue

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