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KChIP2 - Study of Ca2+ binding sites
2003 (English)Independent thesis Advanced level (professional degree), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

Recent research has identified a b-subunit to the voltage-gated potassium-ion channel hKv4.3, the Kv interacting protein 2 - KChIP2. This subunit acts as a functional modifier of hKv4.3 both by acting as a chaperone and by altering channel kinetics amplifying the fast transient outward current, Ito1 about 2- to 3-fold. KChIP2 is a calcium-binding protein able to bind 3-4 calcium ions in distinct sites called EF-hands. Calcium binding has modulatory effect on the KChIP2-hKv4.3 functional complex. This project aimed to study the role of individual EF-hands and importance of calcium binding by site-directed mutagenesis. The four EF-hands were rendered non-functional by site-directed mutagenesis. The functional effect of single, double, triple and quadruple mutants on the KChIP2-hKv4.3 complex was studied using the Xenopus laevis oocytes expression system and the voltage clamp technique. Four different parameters were measured: peak current at +40mV, peak current at +10mV, recovery from inactivation and inactivation time constants. The results showed that KChIP2 interacts with hKv4.3 modifying its electrophysiological characteristics as described in literature and that those functional properties of KChIP2 are calcium ion-dependent. EF-hand 1 either does not bind calcium in KChIP2 wild type protein or else calcium-binding of this EF-hand is not important for hKv4.3 modulation. This was expected since the sequence of EF-hand 1 is divergent from the EF-hand consensus sequence.

Place, publisher, year, edition, pages
2003.
Keyword [en]
Technology, KChIP2
Keyword [sv]
Teknik
Identifiers
URN: urn:nbn:se:ltu:diva-54805ISRN: LTU-EX--03/174--SELocal ID: bbb3c0b0-38ec-4792-8585-3f40edd5eb91OAI: oai:DiVA.org:ltu-54805DiVA: diva2:1028187
Subject / course
Student thesis, at least 30 credits
Educational program
Chemical Engineering, master's level
Examiners
Note
Validerat; 20101217 (root)Available from: 2016-10-04 Created: 2016-10-04Bibliographically approved

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