RGD Reference Report - The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction. - Rat Genome Database

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The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction.

Authors: Haase, H  Pagel, I  Khalina, Y  Zacharzowsky, U  Person, V  Lutsch, G  Petzhold, D  Kott, M  Schaper, J  Morano, I 
Citation: Haase H, etal., FASEB J 2004 May;18(7):839-41. Epub 2004 Mar 04.
RGD ID: 1304304
Pubmed: PMID:15001564   (View Abstract at PubMed)
DOI: DOI:10.1096/fj.03-0446fje   (Journal Full-text)

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.

Objects referenced in this article
Gene Ahnak AHNAK nucleoprotein Rattus norvegicus

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