3.8 Article

Cell adhesion in zebrafish myogenesis: Distribution of intermediate filaments, microfilaments, intracellular adhesion structures and extracellular matrix

期刊

CELL MOTILITY AND THE CYTOSKELETON
卷 65, 期 10, 页码 801-815

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WILEY-LISS
DOI: 10.1002/cm.20301

关键词

Danio rerio; septogenesis; cytoskeleton; desmin; vinculin; actin

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  1. Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq),

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To overcome the limitations of in vitro studies, we have been studying myogenesis in situ in zebrafish embryos, at a sub-cellular level. While in previous work we focused on myofibrillogenesis and some aspects of adhesion structures, here we describe in more detail cell adhesion structures and interactions among cytoskeletal components, membrane and extracellular matrix during zebrafish muscle development. We studied the intermediate filaments, and we describe the full range of desmin distribution in zebrafish development, from perinuclear to striated, until its deposition around the intersomite septa of older somites. This adhesion structure, positige for desmin and actin, has not been previously observed in myogenesis in vitro. We also show that actin in initially located in the intersomite septum region whereas it is confined to the myofibrils later on. While actin localization changes during development, the adhesion complex proteins vinculin, paxillin, talin, dystrophin, laminin and fibronectin always appear exclusively proteins accumulates before the intracellular ones. Contrary to the adhesion proteins, that are continuously distributed, desmin and sarcomeric actin form triangular aggregates among the septa and the cytoskeleton. We studied the cytoskeletal linker plectin as well, and we show that it has a distribution similar to desmin and not to actin. We conclude that the in situ adhesion structures differ from their in vitro counterparts, and that the actual zebrafish embryo myogenesis is quite different than that which occurs in in vitro systems. Cell Motil. Cytoskeleton 65: 801-815, 2008. (C) 2008 Wiley-Liss, Inc.

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