Hsp27 is persistently expressed in zebrafish skeletal and cardiac muscle tissues but dispensable for their morphogenesis

Tucker, Nathan R.; Ustyugov, A. A.; Bryantsev, Anton L.; Konkel, Michael E.; Shelden, Eric A.

doi:10.1007/s12192-009-0105-1

Cited by 23 publications

(19 citation statements)

References 69 publications

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“…A third possibility is that αA-crystallin serves functions that overlap with other proteins, such as αB-crystallin or other small heat shock protein expressed in the zebrafish lens like Hsp27 and MKBP (Elicker and Hutson, 2007; Marvin et al, 2008). Interestingly, knockdown of Hsp27, which is constitutively expressed in zebrafish cardiac and skeletal muscle, also produces no developmental abnormalities (Tucker et al, 2009). Redundancy between α-crystallins was suggested as an explanation for the lack of significant phenotypes in the individual knockout of mouse αA- and αB-crystallin (Boyle et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Loss of the small heat shock protein αA-crystallin does not lead to detectable defects in early zebrafish lens development

Posner

Skiba

Brown

et al. 2013

Experimental Eye Research

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Alpha crystallins are small heat shock proteins essential to normal ocular lens function. They also help maintain homeostasis in many non-ocular vertebrate tissues and their expression levels change in multiple diseases of the nervous and cardiovascular system and during cancer. The specific roles that α-crystallins may play in eye development are unclear. Studies with knockout mice suggested that only one of the two mammalian α-crystallins is required for normal early lens development. However, studies in two fish species suggested that reduction of αA-crystallin alone could inhibit normal fiber cell differentiation, cause cataract and contribute to lens degeneration. In this study we used synthetic antisense morpholino oligomers to suppress the expression of zebrafish αA-crystallin to directly test the hypothesis that, unlike mammals, the zebrafish requires αA-crystallin for normal early lens development. Despite the reduction of zebrafish αA-crystallin protein to undetectable levels by western analysis through 4 days of development we found no changes in fiber cell differentiation, lens morphology or transparency. In contrast, suppression of AQP0a expression, previously shown to cause lens cataract, produced irregularly shaped lenses, delay in fiber cell differentiation and lens opacities detectable by confocal microscopy. The normal development observed in αA-crystallin deficient zebrafish embryos may reflect similarly non-essential roles for this protein in the early stages of both zebrafish and mammalian lens development. This finding has ramifications for a growing number of researchers taking advantage of the zebrafish's transparent external embryos to study vertebrate eye development. Our demonstration that lens cataracts can be visualized in three-dimensions by confocal microscopy in a living zebrafish provides a new tool for studying the causes, development and prevention of lens opacities.

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Section: Discussionmentioning

confidence: 99%

Loss of the small heat shock protein αA-crystallin does not lead to detectable defects in early zebrafish lens development

Posner

Skiba

Brown

et al. 2013

Experimental Eye Research

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“…hspb12 is found only in birds and fish and is most closely related to hspb7 ; however there is little homology between the two proteins outside the conserved α-crystallin domain (Elicker and Hutson, 2007). Remarkably, although hspb1 is dispensable for normal heart development in zebrafish (Tucker et al, 2009), reduction of hspb1 in Xenopus causes cardia bifida (Brown et al, 2007). …”

Section: Introductionmentioning

confidence: 99%

Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish

Lahvic

Marin

et al. 2013

Developmental Biology

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Small heat shock proteins (sHsps) regulate cellular functions not only under stress, but also during normal development, when they are expressed in organ-specific patterns. Here we demonstrate that two small heat shock proteins expressed in embryonic zebrafish heart, hspb7 and hspb12, have roles in the development of left-right asymmetry. In zebrafish, laterality is determined by the motility of cilia in Kupffer’s vesicle (KV), where hspb7 is expressed; knockdown of hspb7 causes laterality defects by disrupting the motility of these cilia. In embryos with reduced hspb7, the axonemes of KV cilia have a 9+0 structure, while control embyros have a predominately 9+2 structure. Reduction of either hspb7 or hspb12 alters the expression pattern of genes that propagate the signals that establish left-right asymmetry: the nodal-related gene southpaw (spaw) in the lateral plate mesoderm, and its downstream targets pitx2, lefty1 and lefty2. Partial depletion of hspb7 causes concordant heart, brain and visceral laterality defects, indicating that loss of KV cilia motility leads causes coordinated but randomized laterality. Reducing hspb12 leads to similar alterations in the expression of downstream laterality genes, but at a lower penetrance. Simultaneous reduction of hspb7 and hspb12 randomizes heart, brain and visceral laterality, suggesting that these two genes have partially redundant functions in the establishment of left-right asymmetry. In addition, both hspb7 and hspb12 are expressed in the precardiac mesoderm and in the yolk syncytial layer, which supports the migration and fusion of mesodermal cardiac precursors. In embryos in which the reduction of hspb7 or hspb12 was limited to the yolk, migration defects predominated, suggesting that the yolk expression of these genes rather than heart expression is responsible for the migration defects.

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“…Retinal sections were blocked in 20% goat serum, and then one of the following monoclonal antibodies was used: anti-HuC/D (1:200) from Molecular Probes (Eugene, OR); Zpr-1 (1:200) and Zrf-1(1:200) from the Zebrafish International Resource Center (University of Oregon, Eugene, OR); rat anti-BrdU (1:20) purchased from Chemicon (Temecula, CA) and anti-zebrafish Hsp27 (1:250) provided by Dr. Eric Shelden (Washington State University) (Tucker et al, 2009). For BrdU staining, sections were washed in a 1:1 solution of 4N HCl:PBST (phosphate-buffered saline + 0.05% Triton X-100) for 30 minutes.…”

Section: Methodsmentioning

confidence: 99%

Retinal proliferation response in the buphthalmic zebrafish, bugeye

Lama-Sherpa

Hunter

Frey

et al. 2011

Experimental Eye Research

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The zebrafish retina regenerates in response to acute retinal lesions, replacing damaged neurons with new neurons. In this study we test the hypothesis that chronic stress to inner retinal neurons also triggers a retinal regeneration response in the bugeye zebrafish. Mutations in the lrp2 gene in zebrafish are associated with a progressive eye phenotype (bugeye) that models several risk factors for human glaucoma including buphthalmos (enlarged eyes), elevated intraocular pressure (IOP), and upregulation of genes related to retinal ganglion cell pathology. The retinas of adult bugeye zebrafish showed high rates of ongoing proliferation which resulted in the production of a small number of new retinal neurons, particularly photoreceptors. A marker of mechanical cell stress, Hsp27, was strongly expressed in inner retinal neurons and glia of bugeye retinas. The more enlarged eyes of individual bugeye zebrafish showed disrupted retinal lamination, and a persistent reduced density of neurons in the ganglion cell layer (GCL), although total numbers of GCL neurons were higher than in control eyes. Despite the presence of a proliferative response to damage, the adult bugeye zebrafish remained behaviorally blind. These findings suggest the existence of an unsuccessful regenerative response to a persistent pathological condition in the bugeye zebrafish.

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Hsp27 is persistently expressed in zebrafish skeletal and cardiac muscle tissues but dispensable for their morphogenesis

Cited by 23 publications

References 69 publications

Loss of the small heat shock protein αA-crystallin does not lead to detectable defects in early zebrafish lens development

Loss of the small heat shock protein αA-crystallin does not lead to detectable defects in early zebrafish lens development

Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish

Retinal proliferation response in the buphthalmic zebrafish, bugeye

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