A non‐selective cation current activated via the multifunctional Ca(2+)‐calmodulin‐dependent protein kinase in human epithelial cells.

Braun, Andrew P.; Schulman, Howard

doi:10.1113/jphysiol.1995.sp020944

Cited by 78 publications

(68 citation statements)

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“…2 Therefore, it is possible that the KN-93-induced G 2 phase arrest of HeLa cells may also result from the inhibition of CaM kinase I activity. To exclude a role for either CaM kinase I or IV at the G 2 /M phase transition, we microinjected AC3-I, a specific peptide inhibitor of CaM kinase II (65), into a synchronized population of HeLa cells. Upon microinjection in G 2 phase cells, AC3-I, but not AC3-C, blocked entry into M phase.…”

Section: Discussionmentioning

confidence: 99%

Calcium/Calmodulin-dependent Phosphorylation and Activation of Human Cdc25-C at the G2/M Phase Transition in HeLa Cells

Patel

Holt

Philipova³

et al. 1999

Journal of Biological Chemistry

127

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Section: Discussionmentioning

confidence: 99%

Calcium/Calmodulin-dependent Phosphorylation and Activation of Human Cdc25-C at the G2/M Phase Transition in HeLa Cells

Patel

Holt

Philipova³

et al. 1999

Journal of Biological Chemistry

127

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“…These inhibitors act on the catalytic domain of C aMkinase (Ocorr and Schulman, 1991;Ishida and Fujisawa, 1995). The IC 50 values for C aM K II(273-302) and C aM K II(AC3) inhibitory peptides are 1 M (Malinow et al, 1989) and 3 M (Braun and Schulman, 1995) (assay performed by Dr. Angus Nairn, Rockefeller University, New York, N Y), respectively. These inhibitors also can affect PKC but at much higher concentrations (IC 50 Ͼ200 and ϳ500 M, respectively) (Malinow et al, 1989;Braun and Schulman, 1995) (but see Hvalby et al, 1994).…”

Section: Methodsmentioning

confidence: 99%

“…The IC 50 values for C aM K II(273-302) and C aM K II(AC3) inhibitory peptides are 1 M (Malinow et al, 1989) and 3 M (Braun and Schulman, 1995) (assay performed by Dr. Angus Nairn, Rockefeller University, New York, N Y), respectively. These inhibitors also can affect PKC but at much higher concentrations (IC 50 Ͼ200 and ϳ500 M, respectively) (Malinow et al, 1989;Braun and Schulman, 1995) (but see Hvalby et al, 1994). For the C aM K II(AC3)-protected peptide inhibitor, IC 50 was found to be ϳ5 M (assay performed by Dr. Angus Nairn).…”

Section: Methodsmentioning

confidence: 99%

“…Three specific inhibitors of C aM-kinase were used: AC3-derived peptide inhibitor (K K AL H RQEAVDAL) (Braun and Schulman, 1995) (synthesized at the University of Michigan Protein and C arboxyhydrate Structure Facility, Ann Arbor, M I), C aMkinase (AC3)-protected peptide inhibitor (Ac-K K AL H RQEAVDAL-NH 2 ) (synthesized at QCB, Hopkinton, M A), and pseudosubstrate peptide inhibitor corresponding to residues 273-302 of the rat ␣-C aMkinase H RSTVASCMHRQETVDCLKKFNARRKLKGA (Malinow et al, 1989) (a gift of Dr. H. Schulman, Stanford University, Stanford, CA). A rhodamine-conjugated AC3 peptide also was used in some experiments (University of Michigan Protein and C arboxyhydrate Structure Facility).…”

Section: Methodsmentioning

confidence: 99%

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Postsynaptic Inhibitors of Calcium/Calmodulin-Dependent Protein Kinase Type II Block Induction But Not Maintenance of Pairing-Induced Long-Term Potentiation

1997

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The role of postsynaptic kinases in the induction and maintenance of long-term potentiation (LTP) was studied in the CA1 region of the rat hippocampal slice. A peptide inhibitor for the catalytic domain of calcium/calmodulin-dependent protein kinase type II (CaM-kinase) was applied through a perfused patch pipette. The inhibitor completely blocked both the shortterm potentiation and LTP induced by a pairing protocol. This indicates that the kinase or kinases affected by the peptide are downstream from depolarization in the LTP cascade. The ability to block LTP required that measures be taken to interfere with degradation of the peptide kinase inhibitor by endogenous proteases; either addition of protease inhibitors or modifications of the peptide itself greatly enhanced the effectiveness of the peptide. Protease inhibitors by themselves or control peptide did not block LTP induction. To study the effect of kinase inhibitor on LTP maintenance, we induced LTP in one pathway. Subsequent introduction of the kinase inhibitor blocked the induction of LTP in a second pathway, but it did not affect maintenance of LTP in the first. The implications for the role of kinases in LTP maintenance are discussed. Key words: long-term potentiation; calcium/calmodulindependent kinase; peptide inhibitors; hippocampal slices; whole-cell recording; intracellular perfusion; protease inhibitors; fluorescent imagingLong-term potentiation (LTP) in the CA1 region of the hippocampus is the best-studied example of the activity-dependent synaptic modifications that may underlie learning and memory (Bliss and Collingridge, 1993;Malenka and Nicoll, 1993) There is now considerable biochemical, physiological, and genetic evidence for the involvement of protein kinases in LTP induction (Colley and Routtenberg, 1993;Suzuki, 1994;Roberson et al., 1996). Some experiments have shown specifically that blocking different postsynaptic kinases is sufficient to block LTP induction (Malenka et al., 1989;Malinow et al., 1989;O'Dell et al., 1991;Wang and Feng, 1992;Hvalby et al., 1994;Blitzer et al., 1995;Feng, 1995;Wang and Kelly, 1996). Furthermore, introduction of protein kinase C (C -kinase) or calcium /calmodulin-dependent protein kinase type II (C aM-kinase) (Hu et al., 1987; McGladeMcCulloh et al., 1993;L ledo et al., 1995) or their activators (Wang and Kelly, 1995) into the postsynaptic cell results in synaptic potentiation that may occlude tetanus-induced LTP (Wang and Kelly, 1995).Although there is general agreement that postsynaptic kinases are involved in LTP induction, their exact role remains unclear. LTP is initiated by C a 2ϩ entry through the NMDA channels (Bliss and Collingridge, 1993), an entry that requires depolarization (Mayer et al., 1984;Nowak et al., 1984). The depolarization may be provided by dendritic action potentials (Jaffe et al., 1992;Magee and Johnston, 1997) and the EPSP, both of which depend on voltage-dependent channels Sakmann, 1994, 1995;Andreasen and Lambert, 1995), which themselves may be regulated by phosphorylation ...

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“…These mice were deficient in LTP and hippocampus-dependent spatial learning tasks [15]. CA1 hippocampal synapses have served as a model system by which to understand synaptic plasticity.…”

Section: Function Of Camk II In Learning-memorymentioning

confidence: 99%

Function of the CaMK II on LTP of Exercise Learning

Xie¹,

Xu²,

Li³

et al. 2013

IJAPM

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Abstract-This Ca2+ /calmodulin-dependent kinase II (CaMKII) is an abundant synaptic signaling molecule that is essential for memory formation and the induction of synaptic potentiation. Additionally, CaMKII plays a prominent role in synaptic tagging and metaplasticity. The kinase becomes active in the presence of calcium and has the potential to switch to an autonomous mode of activity upon auto-phosphorylation. Since CaMKII can be autonomously active and required for the formation of memory, CaMKII is central to the mechanism of hippocampal, N-methyl-d-Aspartate NMDA receptor dependent long-term potentiation of synaptic transmission (LTP). However, the exact reason increased activity and how this is worked it is still matter of debate and the exact time window of increased activity and how this is terminated, There is now overwhelming evident that the expression and significance of CaMKII mRNA in hippocampus of rats whose spatial learning and memory function were enhanced by Regular Aerobic Exercise. Thus, regulation of Exercise of the expression of endogenous CaMKII may constitute important role on CaMKII signaling on LTP during memory formation.

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A non‐selective cation current activated via the multifunctional Ca(2+)‐calmodulin‐dependent protein kinase in human epithelial cells.

Abstract: 1. Activation of macroscopic membrane currents by intracellular calcium ([Ca2+]

Cited by 78 publications

References 50 publications

Calcium/Calmodulin-dependent Phosphorylation and Activation of Human Cdc25-C at the G2/M Phase Transition in HeLa Cells

Calcium/Calmodulin-dependent Phosphorylation and Activation of Human Cdc25-C at the G2/M Phase Transition in HeLa Cells

Postsynaptic Inhibitors of Calcium/Calmodulin-Dependent Protein Kinase Type II Block Induction But Not Maintenance of Pairing-Induced Long-Term Potentiation

Function of the CaMK II on LTP of Exercise Learning

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