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The spectrin-associated cytoskeleton in mammalian heart.

Baines, Anthony J., Pinder, Jennifer C. (2005) The spectrin-associated cytoskeleton in mammalian heart. Frontiers in Bioscience, 10 . pp. 3020-33. ISSN 1093-9946. (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:8630)

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.


The membrane-associated cytoskeleton of the cardiac muscle cell is emerging as an important element in the maintenance of normal cell functioning. Recently it was shown that when proteins (betaII-spectrin, muscle Lim-only protein, ankyrin-B, ankyrin-G) of this system are defective or deficient, cardiac malfunction ensues. It is well-established that the spectrin cytoskeleton is associated with the plasma membrane, but it was only lately demonstrated that its components also lie on internal cell membranes. This is particularly apparent in muscle cells of the heart which contain specialised intracellular membrane compartments particular to this cell type such as the sarcoplasmic reticulum and T-tubules. Cardiomyocytes are subjected to constant mechanical stress. Since their mechanics are controlled through coordination of calcium fluxes mediated via cell membrane-based assemblies, it is imperative that these essential elements withstand the displacement forces of contraction. Cardiomyocyte spectrin locates the multifunctional spectrin/actin-binding and membrane-binding component, protein 4.1, and they act together on the plasma membrane as well as on internal membranes. We have found that cardiac protein 4.1 links to the calcium handling apparatus whilst spectrins connect with the sarcomeric contractile elements of the cell. Overall this assembly fulfils roles in stabilising cardiomyocyte cell membranes and in coordinating the macromolecular protein accumulations which regulate and accomplish cardiac molecular crosstalk, whilst at the same time enabling the muscle cells to resist extreme forces of contraction.

Item Type: Article
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Anthony Baines
Date Deposited: 05 Sep 2008 13:27 UTC
Last Modified: 16 Nov 2021 09:46 UTC
Resource URI: (The current URI for this page, for reference purposes)
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