Changes in the subcellular distribution of calmodulin-kinase II during brain development

Kelly, Paul; Vernon, Paula

doi:10.1016/0165-3806(85)90265-2

Cited by 91 publications

(75 citation statements)

References 48 publications

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“…Similarly, in synapses, immunogold labeling for CaMKII (Figs. 2,7) was absent at P2, very low at P10, and showed a large increase from P10 to P35 (i.e., consistent with early biochemical studies of CaMKII showing that it was low in synapse protein of the early postnatal forebrain; Kelly and Vernon, 1985). The high amount of labeling subjacent to the PSD (both at P10 and P35) is consistent with the findings of studies on hippocampal synapses in vitro (Dosemeci et al, 2001).…”

Section: Proteins Binding To Glutamate Receptors and Magukssupporting

confidence: 84%

“…The absence of CaMKII from early postnatal hippocampal synapses was predicted from studies of CaMKII in synapse protein of the early postnatal forebrain, where CaMKII is largely cytosolic (Kelly and Vernon, 1985). This may have been represented in our study by the occasional gold particles seen in the cytoplasm but not near the synapse itself.…”

Section: Discussionsupporting

confidence: 49%

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Ontogeny of postsynaptic density proteins at glutamatergic synapses

Petralia

Sans

Wang

et al. 2005

Molecular and Cellular Neuroscience

209

196

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In glutamatergic synapses, glutamate receptors (GluRs) associate with many other proteins involved in scaffolding and signal transduction. The ontogeny of these postsynaptic density (PSD) proteins involves changes in their composition during development, paralleling changes in GluR type and function. In the CA1 region of the hippocampus, at postnatal day 2 (P2), many synapses already have a distinct PSD. We used immunoblot analysis, subcellular fractionation, and quantitative immunogold electron microscopy to examine the distribution of PSD proteins during development of the hippocampus. Synapses at P2 contained substantial levels of NR1 and NR2B and most GluRassociated proteins, including SAP102, SynGAP, the chain of proteins from GluRs/SAP102 through GKAP/Shank/Homer and metabotropic glutamate receptors, and the adhesion factors, cadherin, catenin, neuroligin, and Nr-CAM. Development was marked by substantial decreases in NR2B and SAP102 and increases in NR2A, PSD-95, AMPA receptors and CaMKII. Other components showed more moderate changes.

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Section: Proteins Binding To Glutamate Receptors and Magukssupporting

confidence: 84%

Section: Discussionsupporting

confidence: 49%

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Petralia

Sans

Wang

et al. 2005

Molecular and Cellular Neuroscience

209

196

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“…Why does inhibiting CaN activity in young animals produce multiple results, i.e., prevent induction of LTD, LTP, and synaptic disinhibition (LTD of inhibitory synapses by tetanus)? We propose that although the developing pattern of Ca 2ϩ -dependent protein kinases in brain is similar to that for CaN, their expression is not synchronous (Turner et al, 1984;Kelly and Vernon, 1985;Kelly et al, 1987;Hashimoto, 1988;Yoshida et al, 1988;Hirata et al, 1991) such that shifting the equilibrium between kinases and CaN in postnatal versus adult brain produces different effects on synaptic plasticity. CaN activity may play a dual role in synaptic plasticity during postnatal development and is required for LTD and LTP.…”

Section: Discussionmentioning

confidence: 99%

Postsynaptic Calcineurin Activity Downregulates Synaptic Transmission by Weakening Intracellular Ca²⁺Signaling Mechanisms in Hippocampal CA1 Neurons

Wang¹,

Kelly²

1997

J. Neurosci.

Self Cite

110

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“…However, the stoichiometry of the 50-kDa and 60-kDa subunits of CaM kinase I1 appears to vary in different regions of the brain, e. g. forebrain versus cerebellum [49, 501. Recent studies also suggest that the subunit composition of CaM kinase I1 is altered during neuronal differentiation from predominantly 60-kDa subunit in neonates to a holoenzyme with an increased content of the 50-kDa subunit in the adult forebrain [51] (Kelly et al, unpublished results). Taken together, such data point to the presence of isoenzymic forms, which are differentially expressed in mammalian tissues.…”

Section: Discussionmentioning

confidence: 99%

Calmodulin‐dependent multifunctional protein kinase

Shenolikar¹,

Lickteig²,

Hardie

et al. 1986

European Journal of Biochemistry

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Calcium/calmodulin-dependent multifunctional protein kinases, extensively purified from rat brain (with apparent molecular mass 640 kDa), rabbit liver (300 kDa) and rabbit skeletal muscle (700 kDa), were analysed for their structural, immunological, and enzymatic properties. The immunological cross-reactivity with affinitypurified polyclonal antibodies to the 50-kDa catalytic subunit of the brain calmodulin-dependent protein kinase confirmed the presence of common antigenic determinants in all subunits of the protein kinases. One-dimensional phosphopeptide patterns, obtained by digestion of the autophosphorylated protein kinases with S. aureus V8 protease, and two-dimensional fingerprints of the '251-labelled proteins digested with a combination of trypsin and chymotrypsin, revealed a close similarity between the two subunits (51 kDa and 53 kDa) of the liver enzyme. Similar identity was observed between the 56-kDa and/or 58-kDa polypeptides of the skeletal muscle calmodulindependent protein kinase. The data suggest that the subunits of the liver and muscle protein kinases may be derived by partial proteolysis or by autophosphorylation. The peptide patterns for the 50-kDa and 60-kDa subunits of the brain enzyme confirmed that the two catalytic subunits represented distinct protein products. The comparison of the phosphopeptide maps and the two-dimensional peptide fingerprints, indicated considerable structural homology among the 50-kDa and 60-kDa subunits of the brain calmodulin-dependent protein kinase and the liver and muscle polypeptides. However, a significant number of unique peptides in the liver 51-kDa subunit, skeletal muscle 56-kDa, and the brain 50-kDa and 60-kDa polypeptides were observed and suggest the existence of isoenzyme forms. All calmodulin-dependent protein kinases rapidly phosphorylated synapsin I with a stoichiometry of 3 -5 mol phosphate/mol protein. The two-dimensional separation of phosphopeptides obtained by tryptic/chymotryptic digestion of 32P-labelled synapsin I indicated that the same peptides were phosphorylated by all the calmodulin-dependent protein kinases. Such data represent the first structural and immunological comparison of the liver calmodulin-dependent protein kinase with the enzymes isolated from brain and skeletal muscle. The findings indicate the presence of a family of highly conserved calmodulin-dependent multifunctional protein kinases, with similar structural, immunological and enzymatic properties. The individual catalytic subunits appear to represent the expression of distinct protein products or isoenzymes which are selectively expressed in mammalian tissues.Protein phosphorylation is widely recognised as a major mechanism by which hormones elicit control of cellular processes leading to a variety of physiological responses [l]. The modification of cellular proteins is mediated by specific protein kinases following changes in the intracellular concentration of selected effector molecules or 'second messengers'. In this regard the ubiquitous presence of cyclic-AMP...

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Changes in the subcellular distribution of calmodulin-kinase II during brain development

Cited by 91 publications

References 48 publications

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Postsynaptic Calcineurin Activity Downregulates Synaptic Transmission by Weakening Intracellular Ca²⁺Signaling Mechanisms in Hippocampal CA1 Neurons

Calmodulin‐dependent multifunctional protein kinase

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Changes in the subcellular distribution of calmodulin-kinase II during brain development

Cited by 91 publications

References 48 publications

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Postsynaptic Calcineurin Activity Downregulates Synaptic Transmission by Weakening Intracellular Ca2+Signaling Mechanisms in Hippocampal CA1 Neurons

Calmodulin‐dependent multifunctional protein kinase

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Postsynaptic Calcineurin Activity Downregulates Synaptic Transmission by Weakening Intracellular Ca²⁺Signaling Mechanisms in Hippocampal CA1 Neurons