scholarly journals Ploidy Manipulation of Zebrafish Embryos with Heat Shock 2 Treatment

10.3791/54492 ◽  
2016 ◽  
Author(s):  
Destiny L. Baars ◽  
Kendra A. Takle ◽  
Jonathon Heier ◽  
Francisco Pelegri
Keyword(s):  
Heat Shock ◽  
Zebrafish Embryos ◽  
Ploidy Manipulation

scholarly journals Heat-shock protein 90 1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos

2008 ◽  
Vol 105 (2) ◽  
pp. 554-559 ◽  
Author(s):  
S. J. Du ◽  
H. Li ◽  
Y. Bian ◽  
Y. Zhong
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Skeletal Muscles ◽  
Heat Shock Protein 90 ◽  
Zebrafish Embryos

scholarly journals Heat shock stimulation of a tilapia heat shock protein 70 promoter is mediated by a distal element

2001 ◽  
Vol 356 (2) ◽  
pp. 353-359 ◽  
Author(s):  
Alfredo MOLINA ◽  
Emmanuel Di MARTINO ◽  
Joseph A. MARTIAL ◽  
Marc MULLER
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Transient Expression ◽  
Heat Shock Response ◽  
Heat Shock Protein 70 ◽  
Zebrafish Embryos ◽  
Epithelioma Papulosum Cyprini ◽  
Hsp70 Promoter ◽  
Shock Response ◽  
Constitutive Factor

We reported previously that a tilapia (Oreochromis mossambicus) heat shock protein 70 (HSP70) promoter is able to confer heat shock response on a reporter gene after transient expression both in cell culture and in microinjected zebrafish embryos. Here we present the first functional analysis of a fish HSP70 promoter, the tiHSP70 promoter. Using transient expression experiments in carp EPC (epithelioma papulosum cyprini) cells and in microinjected zebrafish embryos, we show that a distal heat shock response element (HSE1) at approx. −800 is predominantly responsible for the heat shock response of the tiHSP70 promoter. This element specifically binds an inducible transcription factor, most probably heat shock factor, and a constitutive factor. The constitutive complex is not observed with the non-functional, proximal HSE3 sequence, suggesting that both factors are required for the heat shock response mediated by HSE1.

scholarly journals Characterization of Hspb8 in Zebrafish

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1562
Author(s):  
Magda Dubińska-Magiera ◽  
Joanna Niedbalska-Tarnowska ◽  
Marta Migocka-Patrzałek ◽  
Ewelina Posyniak ◽  
Małgorzata Daczewska
Keyword(s):  
Heat Shock ◽  
Small Heat Shock Protein ◽  
Zebrafish Embryos ◽  
Gene Encoding ◽  
Tissue Integrity ◽  
Pathological Conditions ◽  
Muscle Ultrastructure ◽  
Specific Localization ◽  
Potential Use

Hspb8 is a member of the small heat shock protein (sHSP) family. Its expression is known to be upregulated under heat shock. This protein interacts with different partners and can, therefore, be involved in various processes relevant to tissue integrity and functioning. In humans, mutations in the gene encoding Hspb8 can lead to the development of various diseases such as myopathies and neuropathies. In our study, we aimed to perform an in-depth characterization of zebrafish Hspb8 during zebrafish development. We applied techniques such as RT-qPCR, Western blot, immunofluorescence, co-immunoprecipitation, LC-MS, and morpholino-mediated knockdown. We broadened the knowledge regarding zebrafish hspb8 expression during development under normal and heat shock conditions as well as its tissue- and subcellular-specific localization. A co-IP analysis allowed us to conclude that zebrafish Hspb8 can interact with proteins such as Bag3 and Hsc70, which are crucial for formation of an autophagy-inducing complex. We also demonstrated that hspb8 morpholino-mediated knockdown has an impact on zebrafish embryos’ morphology, muscle ultrastructure, and motility behavior. Our research provides a valuable resource for the potential use of the zebrafish as a model for studying pathological conditions associated with hspb8 disorders.

scholarly journals Smyd1b is required for skeletal and cardiac muscle function in zebrafish

2013 ◽  
Vol 24 (22) ◽  
pp. 3511-3521 ◽  
Author(s):  
Huiqing Li ◽  
Yongwang Zhong ◽  
Zengfeng Wang ◽  
Jie Gao ◽  
Jin Xu ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Analysis ◽  
Heat Shock Protein 90 ◽  
Thick Filament ◽  
Protein Accumulation ◽  
Zebrafish Embryos ◽  
Reverse Transcription Pcr ◽  
Filament Assembly ◽  
Cardiac Muscles

Smyd1b is a member of the Smyd family that is specifically expressed in skeletal and cardiac muscles. Smyd1b plays a key role in thick filament assembly during myofibrillogenesis in skeletal muscles of zebrafish embryos. To better characterize Smyd1b function and its mechanism of action in myofibrillogenesis, we analyzed the effects of smyd1b knockdown on myofibrillogenesis in skeletal and cardiac muscles of zebrafish embryos. The results show that knockdown of smyd1b causes significant disruption of myofibril organization in both skeletal and cardiac muscles of zebrafish embryos. Microarray and quantitative reverse transcription-PCR analyses show that knockdown of smyd1b up-regulates heat shock protein 90 (hsp90) and unc45b gene expression. Biochemical analysis reveals that Smyd1b can be coimmunoprecipitated with heat shock protein 90 α-1 and Unc45b, two myosin chaperones expressed in muscle cells. Consistent with its potential function in myosin folding and assembly, knockdown of smyd1b significantly reduces myosin protein accumulation without affecting mRNA expression. This likely results from increased myosin degradation involving unc45b overexpression. Together these data support the idea that Smyd1b may work together with myosin chaperones to control myosin folding, degradation, and assembly into sarcomeres during myofibrillogenesis.

scholarly journals Focal gene misexpression in zebrafish embryos induced by local heat shock using a modified soldering iron

2007 ◽  
Vol 236 (11) ◽  
pp. 3071-3076 ◽  
Author(s):  
Melissa E. Hardy ◽  
Louis V. Ross ◽  
Chi-Bin Chien
Keyword(s):  
Heat Shock ◽  
Local Heat ◽  
Zebrafish Embryos ◽  
Soldering Iron

Heat shock genes and the heat shock response in zebrafish embryos

1997 ◽  
Vol 75 (5) ◽  
pp. 487-497 ◽  
Author(s):  
Patrick H Krone ◽  
Zsolt Lele ◽  
Jennifer B Sass
Keyword(s):  
Heat Shock ◽  
Embryonic Development ◽  
Expression Patterns ◽  
Gene Families ◽  
Zebrafish Embryos ◽  
Heat Shock Genes ◽  
Specific Expression ◽  
Temporal Regulation ◽  
Wide Range ◽  
Genes Encoding

Heat shock genes exhibit complex patterns of spatial and temporal regulation during embryonic development in a wide range of organisms. Our laboratory has initiated an analysis of heat shock protein gene expression in the zebrafish, a model system that is now utilized extensively for the examination of early embryonic development of vertebrates. We have cloned members of the zebrafish hsp47, hsp70,\i and hsp90 gene families and shown them to be closely related to their counterparts in higher vertebrates. Whole mount in situ hybridization and Northern blot analyses have revealed that these genes are regulated in distinct spatial, temporal, and stress-specific manners. Furthermore, the tissue-specific expression patterns of the hsp47 and hsp90 alpha genes correlate closely with the expression of genes encoding known chaperone targets of Hsp47 and Hsp90 in other systems. The data raise a number of interesting questions regarding the function and regulation of these heat shock genes in zebrafish embryos during normal development and following exposure to environmental stress.

Fish kidney cell line in response to heat shock

1992 ◽  
Vol 50 (1) ◽  
pp. 704-705
Author(s):  
Li-Chu Tung ◽  
Yung-Reui Chen ◽  
Shiu-Nan Chen ◽  
Guang-Hsiung Kuo
Keyword(s):  
Heat Shock ◽  
Cell Line ◽  
Fetal Calf Serum ◽  
Calf Serum ◽  
Uranyl Acetate ◽  
Ultrastructural Changes ◽  
Heat Shock Treatment ◽  
Acanthopagrus Schlegeli ◽  
Cacodylate Buffer ◽  
Fish Kidney

In the present study, the ultrastructural changes of BPK cells, a fibroblast-like cell line, derived from the kidney of juvenile black porgy Acanthopagrus schlegeli, under heat shock treatment are described.The BPK cells were maintained in L-15 medium supplemented with 10% fetal calf serum and 0.15 M NaCl at 28|C2. The heating was carried out in precalibrated water baths. Monolayers of cells, grown on coverslips in parafilm-sealed petri dishes were submerged under water for 30 min at 40|C treatments. Cells were fixed in 2.5% glutaraldehyde in 0.1 M cacodylate buffer supplemented with 6.6% sucrose, postfixed in 1% OsO4 and flat embedded in Spurr’s resin. Silver section were cut parallel to the substratum, stained with uranyl acetate and Reynold’s lead citrate, and examined in a Hitachi H-600 electron microscope at 75 KV.

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