English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Molecular and functional differences between heart mKv1.7 channel isoforms

Finol-Urdaneta, R. K., Strüver, N., & Terlau, H. (2006). Molecular and functional differences between heart mKv1.7 channel isoforms. Journal of General Physiology, 128(1), 133-145.

Item is

Files

show Files
hide Files
:
Finol_06.pdf (Any fulltext), 4MB
 
File Permalink:
-
Name:
Finol_06.pdf
Description:
-
Visibility:
Restricted (UNKNOWN id 315; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
eDoc_access: MPG
License:
-

Locators

show

Creators

show
hide
 Creators:
Finol-Urdaneta, Rocio Karin1, Author              
Strüver, Nina1, Author              
Terlau, Heinrich1, Author              
Affiliations:
1Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173655              

Content

show
hide
Free keywords: SHAKER POTASSIUM CHANNEL; K+ CHANNELS; METHIONINE OXIDATION; HYDROGEN-PEROXIDE; SMOOTH-MUSCLE; GENE FAMILY; INACTIVATION; MODULATION; EXPRESSION; STOICHIOMETRY
 Abstract: Ion channels are membrane-spanning proteins that allow ions to permeate at high rates. The kinetic characteristics of the channels present in a cell determine the cell signaling profile and therefore cell function in many different physiological processes. We found that Kv1.7 channels from mouse heart muscle have two putative translation initiation start sites that generate two channel isoforms with different functional characteristics, mKv1.7L (489 aa) and a shorter mKv1.7S (457 aa). The electrophysiological analysis of mKv1.7L and mKv1.7S channels revealed that the two channel isoforms have different inactivation kinetics. The channel resulting from the longer protein (L) inactivates faster than the shorter channels (S). Our data supports the hypothesis that mKv1.7L channels inactivate predominantly due to an N-type related mechanism, which is impaired in the mKv1.7S form. Furthermore, only the longer version mKv1.7L is regulated by the cell redox state, whereas the shorter form mKv1.7S is not. Thus, expression starting at each translation initiation site results in significant functional divergence. Our data suggest that the redox modulation of mKv1.7L may occur through a site in the cytoplasmic N-terminal domain that seems to encompass a metal coordination motif resembling those found in many redox-sensitive proteins. The mRNA expression profile and redox modulation of mKv1.7 kinetics identify these channels as molecular entities of potential importance in cellular redox-stress states such as hypoxia.

Details

show
hide
Language(s): eng - English
 Dates: 2006-07
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 292166
ISI: 000238574000011
ISI: 000238574000011
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of General Physiology
  Alternative Title : J.Gen. Physiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 128 (1) Sequence Number: - Start / End Page: 133 - 145 Identifier: ISSN: 0022-1295