Boussouf, S.E. and Maytum, R. and Jaquet, K. and Geeves, M.A. (2007) Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments. Journal of Muscle Research and Cell Motility, 28 (1). pp. 49-58. ISSN 0142-4319 .
|The full text of this publication is not available from this repository. (Contact us about this Publication)|
We have expressed alpha & beta isoforms of mammalian striated muscle tropomyosin (Tm) and alpha-Tm carrying the D175N or E180G cardiomyopathy mutations. In each case the Tm carries an Ala-Ser N-terminal extension to mimic the acetylation of the native Tm. We show that these Ala-Ser modified proteins are good analogues of the native Tm in the assays used here. We go on to use an in vitro kinetic approach to define the assembly of actin filaments with the Tm isoforms with either a cardiac or a skeletal muscle troponin (cTn, skTn). With skTn the calcium sensitivity of the actin filament is the same for alpha & beta-Tm and there is little change with the mutant Tms. For cTn switching from alpha to beta-Tm causes an increase of calcium sensitivity of 0.2 pCa units. D175N is very similar to the wild type alpha-Tm and E180G shows a small increase in calcium sensitivity of about 0.1 pCa unit. The formation of the switched-off blocked-state of the actin filament is independent of the Tm isoform but does differ for cardiac versus skeletal Tn. The in vitro assays developed here provide a novel, simple and efficient method for assaying the behaviour of expressed thin filament proteins.
|Uncontrolled keywords:||actin; Ca-regulation; skeletal muscle; cardiac muscle; cardiomyopathies|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Suzanne Duffy|
|Date Deposited:||19 Mar 2008 10:23|
|Last Modified:||14 Jan 2010 14:07|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/2499 (The current URI for this page, for reference purposes)|
- Depositors only (login required):