Calcium/Calmodulin-Dependent Protein Phosphorylation in the Nervous System

McGuinness, Teresa L.; Lai, Yvonne; Ouimet, Charles C.; Greengard, Paul

doi:10.1007/978-1-4613-2377-8_34

Cited by 35 publications

(58 citation statements)

References 51 publications

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“…Studies from a number of laboratories have demonstrated that isoenzymes of CaM-kinase II are also present in most mammalian tissues examined. Indeed, the kinase has been highly purified from mammalian brain [7,[10][11][12][13][14], liver [8,15,16], skeletal muscle [17], heart [18], pancreas [19], retina [20], lung [21], parathyroid [22], mammary gland [23] and intestinal brush border [24], as well as neural tissues of Aplysia [25], electric eel [26], squid [27] and Drosophila [28]. The isoenzymes are characterized by a large native molecular mass (300-700 kDa), subunits in the range 50-62 kDa, and similar or identical catalytic properties against several protein substrates (references listed above and [29]).…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

“…In adult rat brain, the highest levels of CaMkinase II are found in the telencephalon regions (hippocampus, lateral septum, cortex, neostriatum, amygdaloid), with much lower activity in the cerebellum, diencephalon, mesencephalon, pons and medulla [9,38]. The ratio of subunits also varies between the different regions, with a and , subunits present in a 4: 1 ratio in rat forebrain and in a 1:4 ratio in cerebellum [12,39]. The variation in ratio of subunit polypeptides in these regions is paralleled by different ratios of the specific mRNA Vol.…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

“…Apparently all of the subunits contain both regulatory and catalytic functions. Initially, this conclusion was based on the observations that, following separation of the subunits by SDS/polyacrylamide-gel electrophoresis and renaturation, both the a and fl subunits of the rat brain kinase bind 125-labelled calmodulin [7,11,12,14] and undergo autophosphorylation [43]. This conclusion has been confirmed by the recent publication of amino acid sequences for the a [31,32], , [44] and /1' [33] subunits of the rat brain kinase deduced from cDNA clones.…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

“…3 min after stimulation [82]. In PC 12 cells it has been demonstrated that the phosphorylation sites increased by a 5 min depolarization with 56 mM-KCI correspond to the sites phosphorylated in vitro by CaM-kinase II [84]. A more detailed study using [32P]P1-labelled bovine adrenal chromaffin cells treated with acetylcholine (or 55 mM-KCI) in the presence of calcium indicated very complex temporal changes in phosphorylation sites contained in seven tryptic fragments [85].…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

“…In the presence of Ca2+/calmodulin, CaM-kinase II exhibits an intramolecular autophosphorylation reaction [11,12,15,29,43] on multiple serine and threonine residues [7,111], which temporally appears to preceed any phosphorylation of exogenous substrate [112]. Following Ca2+/calmodulin-dependent autophosphorylation the regulatory properties of the kinase are significantly altered in that assays containing EGTA (Ca2+-independent activity) now exhibit 50-80 % of total kinase activity (determined in the presence of Ca2+/calmodulin) [113][114][115][116][117].…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

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Calcium/Calmodulin-Dependent Protein Kinase II

Colbran

Soderling

1990

Current Topics in Cellular Regulation

174

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Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

See 3 more Smart Citations

Calcium/Calmodulin-Dependent Protein Kinase II

Colbran

Soderling

1990

Current Topics in Cellular Regulation

174

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Presence of calcium/calmodulin‐dependent protein Kinase II in Nerve terminals of rat brain

Walaas

Gorelick

Greengard

1989

Synapse

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Calcium/calmodulin-dependent protein kinase type II, a multimeric 550-650 kilodalton enzyme composed of major alpha (50 kilodalton) and beta/beta' (60/58 kilodalton) subunits, is present in high concentrations in mammalian brain. Previous immunocytochemical studies indicated that the enzyme is enriched in cell bodies and dendrites, but did not show a clear-cut localization in nerve terminals. The present study presents evidence, using lesion-induced degenerations of pre- and postsynaptic neuronal populations in the neostriatum and substantia nigra, that calcium/calmodulin-dependent protein kinase II, as measured both by autophosphorylation of enzyme subunits and by synapsin I kinase activity, is present in high concentrations in several populations of presynaptic terminals. Lesions of the corticostriatal tract decreased the amount of enzyme by 30-40% in the neostriatum, a decrease similar to that seen in the same region of synapsin I, a general nerve terminal marker. Lesions of the striatonigral tract induced an even more pronounced decrease of the enzyme in the substantia nigra; this decrease was larger than the lesion-induced change of synapsin I seen in the same region. Our data therefore indicate that certain nerve terminal populations in the rat brain contain high levels of calcium/calmodulin-dependent protein kinase II.

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Protein phosphorylation systems in postmortem human brain

et al. 1989

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Protein phosphorylation systems regulated by cyclic adenosine 3',5'-monophosphate (cyclic AMP), or calcium in conjunction with calmodulin or phospholipid/diacylglycerol, have been studied by phosphorylation in vitro of particulate and soluble fractions from human postmortem brain samples. One-dimensional or two-dimensional gel electrophoretic protein separations were used for analysis. Protein phosphorylation catalyzed by cyclic AMP-dependent protein kinase was found to be highly active in both particulate and soluble preparations throughout the human CNS, with groups of both widely distributed and region-specific substrates being observed in different brain nuclei. Dopamine-innervated parts of the basal ganglia and cerebral cortex contained the phosphoproteins previously observed in rodent basal ganglia. In contrast, calcium/phospholipid-dependent and calcium/calmodulin-dependent protein phosphorylation systems were less prominent in human postmortem brain than in rodent brain, and only a few widely distributed substrates for these protein kinases were found. Protein staining indicated that postmortem proteolysis, particularly of high-molecular-mass proteins, was prominent in deeply located, subcortical regions in the human brain. Our results indicate that it is feasible to use human postmortem brain samples, when obtained under carefully controlled conditions, for qualitative studies on brain protein phosphorylation. Such studies should be of value in studies on human neurological and/or psychiatric disorders.

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Calcium/Calmodulin-Dependent Protein Phosphorylation in the Nervous System

Cited by 35 publications

References 51 publications

Calcium/Calmodulin-Dependent Protein Kinase II

Calcium/Calmodulin-Dependent Protein Kinase II

Presence of calcium/calmodulin‐dependent protein Kinase II in Nerve terminals of rat brain

Protein phosphorylation systems in postmortem human brain

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