Cytoskeletal and cellular adhesion proteins in zebrafish (Danio rerio) myogenesis

Costa, Márcio Henrique Sá Netto; Escaleira, Roberta C.; Manasfi, Muhamed; Souza, Lays; Mermelstein, Cláudia

doi:10.1590/s0100-879x2003000800019

Cited by 14 publications

(17 citation statements)

References 13 publications

(11 reference statements)

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“…The subcellular localization of Fxr1p in striated muscle tissue was in granular structures at the sarcolemma, which appear to be costameres as the granular Fxr1p staining overlaps with that of vinculin and dystrophin, both are components of the costameric protein network (Morris and Fulton, 1994;Costa et al, 2003). This is in agreement with previous reports in mice that also described Fxr1p staining in granular structures in costameres (Dube et al, 2000;Mientjes et al, 2004).…”

Section: Discussionsupporting

confidence: 90%

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Characterization ofFxr1inDanio rerio; a simple vertebrate model to study costamere development

Engels

Padje

Blonden

et al. 2004

Journal of Experimental Biology

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SUMMARY The X-linked FMR1 gene, which is involved in the fragile X syndrome, forms a small gene family with its two autosomal homologs, FXR1 and FXR2. Mouse models for the FXR genes have been generated and proved to be valuable in elucidating the function of these genes, particularly in adult mice. Unfortunately, Fxr1 knockout mice die shortly after birth, necessitating an animal model that allows the study of the role of Fxr1p, the gene product of Fxr1, in early embryonic development. For gene function studies during early embryonic development the use of zebrafish as a model organism is highly advantageous. In this paper the suitability of the zebrafish as a model organism to study Fxr1p function during early development is explored. As a first step, we present here the initial characterization of Fxr1p in zebrafish. Fxr1p is present in all the cells from zebrafish embryos from the 2/4-cell stage onward; however, during late development a more tissue-specific distribution is found, with the highest expression in developing muscle. In adult zebrafish, Fxr1p is localized at the myoseptum and in costamere-like granules in skeletal muscle. In the testis, Fxr1p is localized in immature spermatogenic cells and in brain tissue Fxr1p displays a predominantly nuclear staining in neurons throughout the brain. Finally, the different tissue-specific isoforms of Fxr1p are characterized. Since the functional domains and the expression pattern of Fxr1p in zebrafish are comparable to those in higher vertebrates such as mouse and human, we conclude that the zebrafish is a highly suitable model for functional studies of Fxr1p.

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Section: Discussionsupporting

confidence: 90%

“…Both proteins are components of the myoseptum and provide a connection between the extracellular matrix (ECM) and the intracellular cytoskeleton Costa et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Characterization ofFxr1inDanio rerio; a simple vertebrate model to study costamere development

Engels

Padje

Blonden

et al. 2004

Journal of Experimental Biology

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“…29 The following antibodies were used at the indicated dilutions: anti-sarcomeric ␣-actinin (clone EA53; Sigma) at 1:1000 and F59 30 at 1:10. The heart was dissected using forceps.…”

Section: Antibody Staining and Histologymentioning

confidence: 99%

Depletion of Zebrafish Titin Reduces Cardiac Contractility by Disrupting the Assembly of Z-Discs and A-Bands

Seeley

Huang

Chen

et al. 2007

Circulation Research

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Abstract-The genetic study of titin has been notoriously difficult because of its size and complicated alternative splicing routes. Here, we have used zebrafish as an animal model to investigate the functions of individual titin isoforms. We identified 2 titin orthologs in zebrafish, ttna and ttnb, and annotated the full-length genomic sequences for both genes. We found that ttna, but not ttnb, is required for sarcomere assembly in the heart as well as the subsequent establishment of cardiac contractility. In fact, ttna is the earliest sarcomeric mRNA that is expressed in the heart, which makes it an early molecular marker for cardiomyocyte differentiation. Surprisingly, ttna is required for later steps of sarcomere assembly, including the assembly of Z-discs and A-bands, but not for early steps such as the assembly of Z-bodies and nonstriated myosin filaments. Reduction of individual titin isoforms in vivo using morpholino-modified antisense oligonucleotides indicated that (1) both N2B exon-containing and N2A exon-containing isoforms of ttna are required for sarcomere assembly in the heart; (2) N2A exon-containing isoforms of both ttna and ttnb are required for sarcomere assembly in the somites; and (3) the N2B exon-containing isoforms of ttnb are expressed later than other titin isoforms and are probably involved in modulating their expression; however, these isoforms of ttnb are not required for sarcomere assembly. Collectively, our results reveal distinct functions of different titin isoforms and suggest that various phenotypes in "titinopathies" may be attributable to the disruption of different titin isoforms. (Circ Res. 2007;100:238-245.)

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“…Some papers address somitogenesis in general and septogenesis particularly [Stickney et al, 2000], but without studying its constituent proteins and structures at the sub-cellular level. We already described some of the structural and sub-cellular aspects of adhesion proteins such as vinculin and dystrophin in the zebrafish embryo [Costa et al, 2003]. Here we broaden this study by analyzing several sarcomeric and adhesion proteins and their extracellular matrix counterparts.…”

Section: Introductionmentioning

confidence: 96%

“…However, even in this so called ''in vivo cell biology'', as in most of the studies on zebrafish/embryonic myogenesis, the subcellular structures have not been described, in the way they have been analyzed in cell cultures. We previously followed the changes in distribution of some components of the muscle cytoskeleton: intermediate filaments and myofibrils [Costa et al, 2002], and some of the cytoskeletal attachments to the membrane [Costa et al, 2003]. Here we broaden our analysis of the cytoskeleton, the matrix and their attachments, by focusing on the adhesion structures and probing the distribution of key proteins in myogenesis.…”

Section: Introductionmentioning

confidence: 99%

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

Costa

Escaleira

Jazenko

et al. 2008

Cell Motil. Cytoskeleton

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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 works 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, positive for desmin and actin, has not been previously observed in myogenesis in vitro. We also show that actin is 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 at the intersomite septa, and appear to be co-distributed, even though the extracellular 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.

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Cytoskeletal and cellular adhesion proteins in zebrafish (Danio rerio) myogenesis

Cited by 14 publications

References 13 publications

Characterization ofFxr1inDanio rerio; a simple vertebrate model to study costamere development

Characterization ofFxr1inDanio rerio; a simple vertebrate model to study costamere development

Depletion of Zebrafish Titin Reduces Cardiac Contractility by Disrupting the Assembly of Z-Discs and A-Bands

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

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