Bennett, Pauline M., Baines, Anthony J., Lecomte, Marie-Christine, Maggs, Alison M., Pinder, Jennifer C. (2004) Not just a plasma-membrane protein - in cardiac muscle cell alpha-II spectrin also shows a close association with myofibrils. Journal of Muscle Research and Cell Motility, 25 (2). pp. 119-126. ISSN 0142-4319. (doi:10.1023/B:JURE.0000035892.77399.51) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:8633)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: https://doi.org/10.1023/B:JURE.0000035892.77399.51 |
Abstract
Spectrin and its associated proteins are essential for the integrity of muscle cells and there is increasing evidence for their involvement in signalling pathways as well as having a structural function in mediating stress. Spectrin is a multigene family and it is essential to determine which isoforms are present and their location in the cell. In heart muscle, we have found that one spectrin isoform, alphaII-spectrin, is strongly represented and, using immunofluorescence, we show that it lies within the contractile fibres near the Z-disc as well as on the cardiomyocyte plasma membrane. Electron microscopy of immunogold-labelled cryosections reveals statistically significant clustering of gold particles near the Z-disc, within and close to the edge of myofibrils. betaII-spectrin and ankyrin-R and G are both known to occupy this region. We suggest that alphaIIbetaII spectrin tetramers with ankyrin organise and/or stabilise cardiac muscle cell membrane components relative to the contractile apparatus.
Item Type: | Article |
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DOI/Identification number: | 10.1023/B:JURE.0000035892.77399.51 |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Anthony Baines |
Date Deposited: | 17 Sep 2008 15:15 UTC |
Last Modified: | 05 Nov 2024 09:41 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/8633 (The current URI for this page, for reference purposes) |
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