Linked Life Data

12967630

Source:http://linkedlifedata.com/resource/pubmed/id/12967630

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2003-9-11
pubmed:abstractText
The Ca(2+)-independent, voltage-gated transient outward current (I(to)) displays a marked increase during development of cardiomyocytes. However, the molecular mechanism remained unclear. In rat adult ventricular myocytes, I(to) can be divided into a fast (I(to,f)) and a slow (I(to,s)) component by recovery process from inactivation. Voltage-gated K(+) channel-interacting proteins 2 (KChIP2) has recently been shown to modify membrane expressions and current densities of I(to,f). Here we examined the developmental change of I(to) and the putative molecular correlates of I(to,f) (Kv4.2 and Kv4.3) and KChIP2 in rat ventricular myocytes. Even in rat embryonic day 12 (E12) myocytes, we detected I(to). However, I(to) in E12 was solely composed of I(to,s). In postnatal day 10 (P10), we recorded much increased I(to) composed of two components (I(to,f) and I(to,s)), and I(to,f) was dominant. Thus, the developmental increase of I(to) from E12 to P10 can be explained by the dramatic appearance of I(to,f). Real-time RT-PCR revealed that Kv4.2 and Kv4.3 mRNA levels were slightly changed. By contrast, KChIP2 mRNA level increased from E12 to P10 by 731-fold. Therefore, the huge increase of KChIP2 expression was likely to be the cause of the great increase of I(to,f). In order to confirm that KChIP2 is crucial to induce I(to,f), we used adenoviral gene transfer technique. When KChIP2 was over-expressed in E12 myocytes, a great amplitude of I(to,f) appeared. Immunocytochemical experiments also demonstrated that KChIP2 enhanced the trafficking of Kv4.2 channels to cell surface. These results indicate that KChIP2 plays an important role in the generation of functional I(to,f) channels during development.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2828
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1073-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12967630-Adenoviridae, pubmed-meshheading:12967630-Aging, pubmed-meshheading:12967630-Animals, pubmed-meshheading:12967630-Animals, Newborn, pubmed-meshheading:12967630-Calcium-Binding Proteins, pubmed-meshheading:12967630-Cells, Cultured, pubmed-meshheading:12967630-Fetus, pubmed-meshheading:12967630-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:12967630-Heart Ventricles, pubmed-meshheading:12967630-Ion Channel Gating, pubmed-meshheading:12967630-Kv Channel-Interacting Proteins, pubmed-meshheading:12967630-Myocardium, pubmed-meshheading:12967630-Patch-Clamp Techniques, pubmed-meshheading:12967630-Polymerase Chain Reaction, pubmed-meshheading:12967630-Potassium Channels, pubmed-meshheading:12967630-Potassium Channels, Voltage-Gated, pubmed-meshheading:12967630-RNA, Messenger, pubmed-meshheading:12967630-Rats, pubmed-meshheading:12967630-Rats, Wistar, pubmed-meshheading:12967630-Shal Potassium Channels, pubmed-meshheading:12967630-Time Factors
pubmed:year
2003
pubmed:articleTitle
Contribution of KChIP2 to the developmental increase in transient outward current of rat cardiomyocytes.
pubmed:affiliation
Department of Cellular Physiology and Signal Transduction, Sapporo Medical University School of Medicine, South 1 West 17, Chuo-ku, Sapporo 060 8556, Japan. tkobaya@sapmed.ac.jp
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't