Spatial pattern of constitutive and heat shock-induced expression of the small heat shock protein gene family, hsp30, inXenopus laevis tailbud embryos

Lang, Lisa; Miskovic, Dragana; Fernando, Pasan; Heikkila, John J.

doi:10.1002/(sici)1520-6408(1999)25:4<365::aid-dvg10>3.0.co;2-2

Cited by 44 publications

(5 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The differential pattern of Hsp30 gene expression was documented at the level of Hsp30 synthesis (Tam and Heikkila 1995). Recently, using in situ hybridization and immunolocalization studies we detected Hsp30 message and protein in the cement gland of unstressed tailbud embryos (Lang et al 1999). Upon heat shock there was a preferential accumulation of Hsp30 message and protein in selected tissues.…”

Section: Introductionmentioning

confidence: 99%

Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity

Fernando

Heikkila

2000

Cell Stress Chaper

Self Cite

View full text Add to dashboard Cite

Small heat shock proteins protect cells from stress presumably by acting as molecular chaperones. Here we report on the functional characterization of a developmentally regulated, heat-inducible member of the Xenopus small heat shock protein family, Hsp30C. An expression vector containing the open reading frame of the Hsp30C gene was expressed in Escherichia coli. These bacterial cells displayed greater thermoresistance than wild type or plasmid-containing cells. Purified recombinant protein, 30C, was recovered as multimeric complexes which inhibited heat-induced aggregation of either citrate synthase or luciferase as determined by light scattering assays. Additionally, 30C attenuated but did not reverse heat-induced inactivation of enzyme activity. In contrast to an N-terminal deletion mutant, removal of the last 25 amino acids from the C-terminal end of 30C severely impaired its chaperone activity. Furthermore, heat-treated concentrated solutions of the C-terminal mutant formed nonfunctional complexes and precipitated from solution. Immunoblot and gel filtration analysis indicated that 30C binds with and maintains the solubility of luciferase preventing it from forming heat-induced aggregates. Coimmunoprecipitation experiments suggested that the carboxyl region is necessary for 30C to interact with target proteins. These results clearly indicate a molecular chaperone role for Xenopus Hsp30C and provide evidence that its activity requires the carboxyl terminal region.

show abstract

Section: Introductionmentioning

confidence: 99%

Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity

Fernando

Heikkila

2000

Cell Stress Chaper

Self Cite

View full text Add to dashboard Cite

show abstract

“…The expression of human small Hsps are restricted to some specific tissues such as the heart/muscle or lens even in the presence of stresses, while cHsp25 is not expressed in the absence of stress, but is highly expressed after hyperthermia in all the tissues of developing embryos [5]. The expression profile of cHsp25 is similar to those of Xenopus Hsp30 [25] and of minnow Hsp30 [14]. Taken together with the relatedness of the amino acid sequences (Figs.…”

Section: Discussionmentioning

confidence: 64%

Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress*1

KATOH¹

2004

FEBS Letters

View full text Add to dashboard Cite

Protein aggregates are oligomeric complexes of misfolded proteins, and serve as the seeds of inclusion bodies termed aggresomes in the cells. Heat shock proteins (Hsps) prevent misfolding and aggregate formation. Here, we found that only avian Hsp25 dominantly accumulated in the aggresomes induced by proteasome inhibition. Molecular cloning of chicken Hsp25 (cHsp25) revealed that it belongs to the Hsp30 family, which is a subfamily of the a-crystallin/small Hsp gene family. Unexpectedly, overexpression of cHsp25 into HeLa cells promoted inclusion formation whereas overexpression of mouse Hsp27 and its chicken homologue did not. These results suggest that cHsp25 acts differently from other small Hsps on protein aggregates.

show abstract

“…Species-specific sHSP gene expression was increased and expressed exclusively in diapause and dormancy states, such as the dauer stage of C. elegans and cysts of A. franciscana , but was not detected when development continued1011. Thus, HSP25 gene expression was reduced in developmental initiation, but the HSP30CL gene was induced, more similar to the gastrulation stages in Xenopus 7.…”

Section: Discussionmentioning

confidence: 95%

“…These findings indicated that HSP25 and HSP30CL transcripts were not maternally inherited for embryonic development and stress tolerance. Additionally, developmentally constitutive HSP30 homologues in Xenopus were first detected in early and mid-tailbud embryos, after gastrulation, but not soon after ZGA, which in Xenopus occurs at the 128- to 256-cell stage7. It was recently discovered that ZGA starts between EGK stages II and III in chicken3233.…”

Section: Discussionmentioning

confidence: 99%

“…During early gastrulation in Danio rerio , heat shock protein family B (small) member 1 ( hspb1 ) gene is expressed transiently in the developing myotome, lens, and presumptive brain6. Constitutive expression of the hsp30 genes has been detected in the cement gland of early and mid-tailbud Xenopus laevis embryos7. In mouse pre-implantation embryos, Hspb1 mRNA is induced by zygotic genome activation at the two-cell stage, is subsequently decreased at the four-cell stage, and is re-upregulated at the morula stage, with the highest expression in the blastocyst8.…”

mentioning

confidence: 99%

See 1 more Smart Citation

The avian-specific small heat shock protein HSP25 is a constitutive protector against environmental stresses during blastoderm dormancy

Hwang

Kim

et al. 2016

Sci Rep

View full text Add to dashboard Cite

Small heat shock proteins (sHSPs) range in size from 12 to 42 kDa and contain an α-crystalline domain. They have been proposed to play roles in the first line of defence against various stresses in an ATP-independent manner. In birds, a newly oviposited blastoderm can survive several weeks in a dormant state in low-temperature storage suggesting that blastoderm cells are basically tolerant of environmental stress. However, sHSPs in the stress-tolerant blastoderm have yet to be investigated. Thus, we characterised the expression and function of sHSPs in the chicken blastoderm. We found that chicken HSP25 was expressed especially in the blastoderm and was highly upregulated during low-temperature storage. Multiple alignments, phylogenetic trees, and expression in the blastoderms of Japanese quail and zebra finch showed homologues of HSP25 were conserved in other avian species. After knockdown of chicken HSP25, the expression of pluripotency marker genes decreased significantly. Furthermore, loss of function studies demonstrated that chicken HSP25 is associated with anti-apoptotic, anti-oxidant, and pro-autophagic effects in chicken blastoderm cells. Collectively, these results suggest avian HSP25 could play an important role in association with the first line of cellular defences against environmental stress and the protection of future embryonic cells in the avian blastoderm.

show abstract

Spatial pattern of constitutive and heat shock-induced expression of the small heat shock protein gene family, hsp30, inXenopus laevis tailbud embryos

Cited by 44 publications

References 43 publications

Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity

Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity

Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress*1

The avian-specific small heat shock protein HSP25 is a constitutive protector against environmental stresses during blastoderm dormancy

Contact Info

Product

Resources

About