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| Item Type: | Article |
|---|---|
| Title: | The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction |
| Creators Name: | Haase, H., Pagel, I., Khalina, Y., Zacharzowsky, U., Person, V., Lutsch, G., Petzhold, D., Kott, M., Schaper, J. and Morano, I. |
| Abstract: | Ahnak, a 700 kDa protein, is expressed in a variety of cells and has been implicated in different cell-type-specific functions. In the human heart, we observed an endogenous carboxyl-terminal 72 kDa ahnak fragment that copurified with myofibrillar proteins. Immunocytochemistry combined with confocal microscopy localized this fragment to the intercalated discs and close to the Z-line of cardiomyocytes. No endogenous myofibrillar ahnak fragment was observed in the skeletal muscle. We elucidated the role of the recombinant carboxyl-terminal ahnak fragment (ahnak-C2) in actin filament organization and in the function of muscle fibers. Addition of ahnak-C2 to actin filaments induced filament bundling into paracrystalline-like structures as revealed by electron microscopy. Incubation of demembranated skeletal muscle fibers with ahnak-C2 attenuated the decline in isometric force development upon repeated contraction-relaxation cycles. Our results suggest that the carboxyl-terminal ahnak domain exerts a stabilizing effect on muscle contractility via its interaction with actin of thin filaments. |
| Keywords: | Actins, Amino Acid Sequence, Confocal Microscopy, Electron Microscopy, Indirect Fluorescent Antibody Technique, Membrane Proteins, Molecular Sequence Data, Muscle Contraction, Myocardium, Neoplasm Proteins, Recombinant Fusion Proteins, Skeletal Muscle, Sprague-Dawley Rats, Tertiary Protein Structure, Three-Dimensional Imaging, Animals, Rabbits, Rats |
| Source: | FASEB Journal |
| ISSN: | 0892-6638 |
| Publisher: | Federation of American Societies for Experimental Biology |
| Volume: | 18 |
| Number: | 7 |
| Page Range: | 839-841 |
| Date: | May 2004 |
| Official Publication: | https://doi.org/10.1096/fj.03-0446fje |
| PubMed: | View item in PubMed |
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