Molecular and functional characterization of HdHSP20: A biomarker of environmental stresses in disk abalone Haliotis discus discus

Wan, Qiang; Whang, Ilson; Lee, Jehee

doi:10.1016/j.fsi.2012.03.034

Cited by 38 publications

(29 citation statements)

References 75 publications

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“…PmHSP20 was detected in different healthy P. martensii organisms with highest expression in the hepatopancreas and lowest in the adductor muscle, hemocyte, gill, and foot (Figure 4). The expression pattern of PmHSP20 in tissues was somewhat similar to previously reported HSP20 expression patterns in the disk abalone (Wan et al, 2012), but different to those previously reported in shrimp (Huang et al, 2008), bloody clam, and razor clam (Bao et al, 2011;Zhang et al, 2013). It has been speculated that different species-or-origin or various tissue functions result in the different expression of sHSPs in tissues.…”

Section: Discussionsupporting

confidence: 70%

“…Specifically, it has been implicated in the immediate response to pathological events, the extracellular regulation of platelet functions (Gusev et al, 2005), and in cardioprotection (Islamovic et al, 2007). Consistent with this, the ability of HSP20 to strengthen the endurance of fishery animals to disease is becoming clear (Wan et al, 2012).…”

Section: Introductionmentioning

confidence: 84%

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Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Lei¹,

Wu²,

Liang³

et al. 2016

Genet. Mol. Res.

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ABSTRACT. Small heat shock proteins (HSPs) are molecular chaperones with ATP-independent properties. They are involved in a variety of physiological and stress processes. In this study, the full-length HSP 20 (HSP20) from Pinctada martensii, designated as PmHSP20, was obtained from hemocytes using rapid amplification of cDNA ends technology. The PmHSP20 cDNA was 952 bp in length, containing an open reading frame of 534 bp that encoded 177-amino acid residues, with an isoelectric point of 5.86 and molecular weight of 20.24 kDa. The sequence of this deduced polypeptide contained typical structure and function domains conserved in the HSP20 family, providing evidence that PmHSP20 belongs to the HSP20 family. The PmHSP20 mRNA expression levels were detected in various tissues of P. martensii and in hemocytes after challenges with the bacteria Vibrio harveyi and lipopolysaccharide (LPS) using quantitative realtime polymerase chain reaction amplification. The results indicated that PmHSP20 is constitutively expressed in all tissues tested and might be involved in the immune response. The upregulation of PmHSP20 after V. harveyi and LPS challenge suggests that PmHSP20 plays an important role in anti-bacterial immunity. Studies on PmHSP20 are a valuable resource to further explore the immune system in pearl oysters and might enhance our knowledge of molluscan innate immunity.

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Section: Discussionsupporting

confidence: 70%

Section: Introductionmentioning

confidence: 84%

Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Lei¹,

Wu²,

Liang³

et al. 2016

Genet. Mol. Res.

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“…In plants, yeast, and most invertebrates, the sHSP genes are encoded by intronless genes. In Halocynthia , three introns interrupt the coding sequence [1], whereas the structure usually described in mammalian (human and rodent), amphibian ( Xenopus tropicalis ), fish ( Danio rerio ), arthropods ( Ixodes scapularis ) or molluscs ( Haliotis discus discus ) includes the presence of 3 exons separated by two introns [14].…”

Section: Resultsmentioning

confidence: 99%

“…In abalone Haliotis discus discus mRNA level of HdHSP20 was up-regulate after exposure to thermal shock, extreme salinities, heavy metals and the microbial infections [14]. Similarly, in scallop Argopecten irradians , AiHSP22 mRNA showed over expression in response to heavy metal exposure [15].…”

Section: Introductionmentioning

confidence: 97%

Characterization of Small HSPs from Anemonia viridis Reveals Insights into Molecular Evolution of Alpha Crystallin Genes among Cnidarians

et al. 2014

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Gene family encoding small Heat-Shock Proteins (sHSPs containing α-crystallin domain) are found both in prokaryotic and eukaryotic organisms; however, there is limited knowledge of their evolution. In this study, two small HSP genes termed AvHSP28.6 and AvHSP27, both organized in one intron and two exons, were characterised in the Mediterranean snakelocks anemone Anemonia viridis. The release of the genome sequence of Hydra magnipapillata and Nematostella vectensis enabled a comprehensive study of the molecular evolution of α-crystallin gene family among cnidarians. Most of the H. magnipapillata sHSP genes share the same gene organization described for AvHSP28.6 and AvHSP27, differing from the sHSP genes of N. vectensis which mainly show an intronless architecture. The different genomic organization of sHSPs, the phylogenetic analyses based on protein sequences, and the relationships among Cnidarians, suggest that the A.viridis sHSPs represent the common ancestor from which H. magnipapillata genes directly evolved through segmental genome duplication. Additionally retroposition events may be considered responsible for the divergence of sHSP genes of N. vectensis from A. viridis. Analyses of transcriptional expression profile showed that AvHSP28.6 was constitutively expressed among different tissues from both ectodermal and endodermal layers of the adult sea anemones, under normal physiological conditions and also under different stress condition. Specifically, we profiled the transcriptional activation of AvHSP28.6 after challenges with different abiotic/biotic stresses showing induction by extreme temperatures, heavy metals exposure and immune stimulation. Conversely, no AvHSP27 transcript was detected in such dissected tissues, in adult whole body cDNA library or under stress conditions. Hence, the involvement of AvHSP28.6 gene in the sea anemone defensome is strongly suggested.

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“…Upon heat shock, HSPs are activated by a change in their oligomerization state and through phosphorylation; subsequently, they bind to denaturing proteins and prevent their aggregation (Haslbeck et al, 2005;Zeng et al, 2015). Previous reports on various aquaculture species of oysters suggested a rapid induction in the expression level of HSPs when the animals were subjected to thermal stress (Dong et al, 2006;Ueda and Boettcher, 2009;Huang et al, 2011;Cho and Jeong, 2012;Wan et al, 2012;Wu et al, 2012;Li et al, 2016). In the present study, it was found that 10 paralogs of both HSP70 and HSP40 were simultaneously up-regulated under thermal stress.…”

Section: Involvement Of Chaperones Heat Shock and Ubiquitin Proteinsmentioning

confidence: 99%

Characterization and Identification of Differentially Expressed Genes Involved in Thermal Adaptation of the Hong Kong Oyster Crassostrea hongkongensis by Digital Gene Expression Profiling

Zhang

Mao

et al. 2017

Front. Mar. Sci.

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Thermal exposure of sessile marine animals inhabiting estuarine intertidal regions is a serious concern with respect to their physiological processes. Organisms living in this region can be exposed to high temperature (>40 • C) during the low tide, which may affect the survival of these organisms. The Hong Kong oyster, Crassostrea hongkongensis, distributed along the coast waters of the South China Sea, is one of the dominant sessile inhabitants of marine intertidal region which undergoes large seasonal temperature fluctuations (up to 10-20 • C during diurnal cycles) every year. To cope with acute thermal stress, it has developed several adaptation mechanisms, e.g., the firmly shut of the shells. However, the genetic basis of these mechanisms remain largely unclear. To better understand how acute thermal exposure affects the biology of the oyster, two cDNA libraries obtained from the gill of oysters exposed to 37 • C thermal stress and ambient temperature were sequenced using the Digital Gene Expression (DGE) tag profiling strategy. In total, 5.9 and 6.2 million reads were obtained from thermal stress and control libraries, respectively, with approximately 74.25 and 75.02% of the reads mapping to the Crassostrea hongkongensis reference sequence. A total of 605 differentially expressed transcripts could be detected in the thermal stress group as compared to the control group, of which 378 are up-regulated and 227 are down-regulated. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis indicated that these Differentially Expressed Genes (DEGs) were enriched with a broad spectrum of biological processes and pathways, including those associated with chaperones, antioxidants, immunity, apoptosis and cytoskeletal reorganization. Among these significantly enriched pathways, protein processing in the endoplasmic reticulum was the most affected metabolic pathway, which plays an important role in the unfolded protein response (UPR) and ER-associated degradation (ERAD) processes. Our results demonstrate the complex multi-modal cellular response to thermal stress in C. hongkongensis.

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Molecular and functional characterization of HdHSP20: A biomarker of environmental stresses in disk abalone Haliotis discus discus

Cited by 38 publications

References 75 publications

Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Characterization of Small HSPs from Anemonia viridis Reveals Insights into Molecular Evolution of Alpha Crystallin Genes among Cnidarians

Characterization and Identification of Differentially Expressed Genes Involved in Thermal Adaptation of the Hong Kong Oyster Crassostrea hongkongensis by Digital Gene Expression Profiling

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