Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine
The elongation factor-2 (eEF-2) is selectively phosphorylated by the eEF-2 kinase (calmodulin-dependent kinase III). This phosphorylation can be inhibited by calmodulin antagonists, such as CGS 9343B (IC 5o = 4 μM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylat...
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| Veröffentlicht in: | FEBS letters 1994-01, Vol.338 (1), p.85-88 |
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| creator | Gschwendt, Michael Kittstein, Walter Marks, Friedrich |
| description | The elongation factor-2 (eEF-2) is selectively phosphorylated by the eEF-2 kinase (calmodulin-dependent kinase III). This phosphorylation can be inhibited by calmodulin antagonists, such as CGS 9343B (IC
5o = 4 μM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC
50 of 5.3 μM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC
50> 50 μM) and thus can be differentiated from most other protein kinases that are suppressed by staurosporine in the nM range. |
| doi_str_mv | 10.1016/0014-5793(94)80121-5 |
| format | Article |
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50 of 5.3 μM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC
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5o = 4 μM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC
50 of 5.3 μM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC
50> 50 μM) and thus can be differentiated from most other protein kinases that are suppressed by staurosporine in the nM range.</description><subject>Acetophenones - pharmacology</subject><subject>Alkaloids - pharmacology</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Benzopyrans - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Calmodulin-dependent kinase III</subject><subject>CaM, calmodulin</subject><subject>eEP-2, elongation factor-2</subject><subject>Elongation factor-2</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Mice</subject><subject>Phosphorylation</subject><subject>PKC, protein kinase C</subject><subject>Protein kinase inhibitor</subject><subject>Protein Kinase Inhibitors</subject><subject>Staurosporine</subject><subject>Transferases</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNktGOEyEUhonRrHX1DTThwhi9GAUGGNgLE920arKJN3pNKHNw0SlUmHbTx_CNZdqxl-oV4fzf-eHwg9BTSl5TQuUbQihvRKfbl5q_UoQy2oh7aEFV1zYtl-o-WpyRh-hRKd9J3SuqL9CFaklHJVugX8shxW92DClib92YcsPwjxBtgSsM3oMbwx5wiLdhHY7U-oDHW8Ax7WHA25xGCHHu-IOljGt9HCBXycYeZxjs7FMglmq0D2P1SXc29wWX0e5yKttUeXiMHng7FHgyr5fo62r55fpjc_P5w6frdzeN45yKxlIg3HnFvGTCKa17xSko2XvPiVsDlV5o2WsupRNMCEed9aAdqXK3rk9yiV6cfOsMP3dQRrMJxcEw2AhpV0wnW8EY7f4JUqmJ6qSsID-Brg5TMnizzWFj88FQYqbIzJSHmfIwmptjZEbUtmez_269gf7cNGdU9eezbouzg882ulDOWKuZoFRVbHXC7sIAh_862qyW79kkTHXNj9XpPm9PRlBffx8gm-ICRAd9yPU7mD6Fvw_0G6PYySY</recordid><startdate>19940124</startdate><enddate>19940124</enddate><creator>Gschwendt, Michael</creator><creator>Kittstein, Walter</creator><creator>Marks, Friedrich</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19940124</creationdate><title>Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine</title><author>Gschwendt, Michael ; Kittstein, Walter ; Marks, Friedrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4415-a1e04cf82f625c899d841e86dff40cbe16f596d9466c5255c1cafe9c0f407b793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Acetophenones - pharmacology</topic><topic>Alkaloids - pharmacology</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Benzopyrans - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Calmodulin-dependent kinase III</topic><topic>CaM, calmodulin</topic><topic>eEP-2, elongation factor-2</topic><topic>Elongation factor-2</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Mice</topic><topic>Phosphorylation</topic><topic>PKC, protein kinase C</topic><topic>Protein kinase inhibitor</topic><topic>Protein Kinase Inhibitors</topic><topic>Staurosporine</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gschwendt, Michael</creatorcontrib><creatorcontrib>Kittstein, Walter</creatorcontrib><creatorcontrib>Marks, Friedrich</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gschwendt, Michael</au><au>Kittstein, Walter</au><au>Marks, Friedrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1994-01-24</date><risdate>1994</risdate><volume>338</volume><issue>1</issue><spage>85</spage><epage>88</epage><pages>85-88</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The elongation factor-2 (eEF-2) is selectively phosphorylated by the eEF-2 kinase (calmodulin-dependent kinase III). This phosphorylation can be inhibited by calmodulin antagonists, such as CGS 9343B (IC
5o = 4 μM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC
50 of 5.3 μM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC
50> 50 μM) and thus can be differentiated from most other protein kinases that are suppressed by staurosporine in the nM range.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>8307162</pmid><doi>10.1016/0014-5793(94)80121-5</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1994-01, Vol.338 (1), p.85-88 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via ScienceDirect (Elsevier); Alma/SFX Local Collection |
| subjects | Acetophenones - pharmacology Alkaloids - pharmacology Analytical, structural and metabolic biochemistry Animals Benzopyrans - pharmacology Biological and medical sciences Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors Calcium-Calmodulin-Dependent Protein Kinases - metabolism Calmodulin-dependent kinase III CaM, calmodulin eEP-2, elongation factor-2 Elongation factor-2 Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Mice Phosphorylation PKC, protein kinase C Protein kinase inhibitor Protein Kinase Inhibitors Staurosporine Transferases |
| title | Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine |
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