Linked Life Data

7602512

Source:http://linkedlifedata.com/resource/pubmed/id/7602512

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-8-10
pubmed:abstractText
1. This study used the whole-cell patch clamp technique to investigate the action of a 28-mer 'inactivation peptide' based on part of the N-terminal sequence of the human Kv3.4 K+ channel (hKv3.4 peptide) on the cloned mouse brain K+ channel mKv1.1 expressed in Chinese hamster ovary (CHO) cells, and compared this with the inactivation produced by Shaker B inactivation peptide (ShB peptide). 2. Inclusion of the hKv3.4 peptide in the patch electrode (320 microM) transformed non-inactivating mKv1.1 into a rapidly inactivating current. The voltage dependence of time constants of decay and steady-state inactivation induced by hKv3.4 peptide were characteristic of an 'A-type' K+ current. 3. The hKv3.4 peptide had no effect on the voltage dependence of activation of mKv1.1, with a mid-point of activation of -8 mV, and a slope factor of 15 mV. Steady-state inactivation curves had a mid-point of inactivation of -36 mV and a slope factor of -7 mV; the time constant of recovery from inactivation at -90 mV was 1.3 s. 4. The chemical modification reagents N-bromoacetamide (NBA, 100 microM) and chloramine-T (CL-T, 500 microM) had no effect on the fast inactivation of mKv1.1 induced by ShB peptide. In contrast, the inactivation caused by hKv3.4 peptide was removed by brief exposure to NBA and CL-T. 5. Chemical modification resulted in a hyperpolarizing shift of -8 mV (CL-T) and -11 mV (NBA) in the voltage dependence of activation of mKv1.1 in the presence of hKv3.4 peptide. 6. Chemical modification was critically dependent on the presence of a cysteine residue at position 6, and not position 24, of hKv3.4 peptide. 7. NBA and CL-T caused only a slight inhibition of unmodified mKv1.1 current with no significant effect on the voltage dependence of mKv1.1 activation, and also had no effect on channel deactivation at -90 mV. 8. Chemical modification experiments were consistent with a selective action on the hKv3.4 peptide itself, specifically at the cysteine residue at position 6.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1174512, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1378392, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1497892, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1497893, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1593614, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1840526, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1881453, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1908562, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1920536, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-1922383, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2122519, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2122520, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2169042, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2311579, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2318832, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2413161, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2454678, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-2552083, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-591912, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-6321714, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-6324912, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-650167, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-7932213, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-8006813, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-8133245, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-8183366, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-8185946, http://linkedlifedata.com/resource/pubmed/commentcorrection/7602512-8358568
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-3751
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
484 ( Pt 1)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-13
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Inactivation of the cloned potassium channel mouse Kv1.1 by the human Kv3.4 'ball' peptide and its chemical modification.
pubmed:affiliation
Electrophysiology Laboratory, Wyeth Research, Taplow, Berkshire, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't