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A Novel Highly Specific and Potent Inhibitor of Calmodulin-Dependent Protein Kinase II

Ishida, A., Kameshita, I., Okuno, S., Kitani, T., Fujisawa, H.·1995·Biochemical and Biophysical Research Communications
DOI 10.1006/bbrc.1995.2040
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Abstract

A novel synthetic peptide AIP (autocamtide-2-related inhibitory peptide), a nonphosphorylatable analog of autocamtide-2, was found to be a highly specific and potent inhibitor of calmodulin-dependent protein kinase II (CaM-kinase II). It was 50 and 500 times more potent than CaMK-(281-302Ala286) and KN-93, respectively, under the assay conditions used. The inhibition was unaffected by the presence or absence of Ca2+/calmodulin, and it was competitive with autocamtide-2 and noncompetitive with syntide-2. AIP (1 microM) completely inhibited CaM-kinase II activity, but did not affect cyclic AMP-dependent protein kinase, protein kinase C, calmodulin-dependent protein kinase IV, and unidentified protein kinases occurring in a rat brain extract. These results indicate that AIP is a useful tool for studying the physiological roles of CaM-kinase II.

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  • CaMKII inhibition with AIP blocks cLTP-induced SNX17 recruitment to synapses, whereas PKA inhibition with KT5720 and ERK inhibition with U0126 do not.

    “We found that autocamtide-2-related inhibitory peptide (AIP), a selective and potent inhibitor of CaMKII (Ishida et al., 1995), blocked SNX17 recruitment to synapses upon cLTP stimulation. However, both KT5720 and U0126, which inhibit PKA- and ERK- dependent signaling pathways, respectively, failed to block cLTP-dependent SNX17 recruitment (Fig. 4 E).”

    From Recruitment of the SNX17-Retriever recycling pathway regulates synaptic function and plasticity (2023) · cites this paper as Ishida et al., 1995

  • AIP is a selective and potent inhibitor of CaMKII.

    “autocamtide-2-related inhibitory peptide (AIP), a selective and potent inhibitor of CaMKII (Ishida et al., 1995)”

    From Recruitment of the SNX17-Retriever recycling pathway regulates synaptic function and plasticity (2023) · cites this paper as Ishida et al., 1995

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Metadata

Authors
Ishida, A., Kameshita, I., Okuno, S., Kitani, T., & Fujisawa, H.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
1995-07
Volume
212
Issue
3
Pages
806-812
ISSN
0006-291X
DOI
10.1006/bbrc.1995.2040
Cited by
252
References
0
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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