This basic science study demonstrates the specific binding and spatial relationship of alpha-actinin to actin bundles in fibroblasts.
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Does not inform clinical practice; leaves open alpha-actinin's role in cardiac cytoskeletal function pending targeted validation.
Rhodamine-labelled alpha-actinin was specifically bound to actin containing filament bundles of demembranated fibroblasts, and was particularly associated with their termini. Optimal binding of rhodamine-alpha-actinin occurred at pH 6.0 - 6.2 and could be abolished by the addition of unlabeled alpha-actinin or myosin subfragment 1. The spatial relationships between the decorating alpha-actinin and several actin associated proteins was determined by double fluorescence microscopy.
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B Geiger (1981) studied this question.
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