Identification of cDNA for the HSPA2, HSPA5 and HSPA8 orthologs of the heat shock protein 70 family from guinea fowl (<i>Numida meleagris</i>)

Iwamoto, Shigehisa; Koike, Y.; Hosomichi, Kazuyoshi; Hara, Hiromi; Yoshida, Yutaka; Ogawa, Hiroshi; Hanzawa, Kei

doi:10.1111/j.1740-0929.2005.00299.x

Cited by 3 publications

(4 citation statements)

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“…Moreover, the dN/dS ratios between these highly related quail and chicken genes are less than 0.1, suggesting that intense negative selection eliminates disadvantageous mutations and has preserved the amino acid sequence of the quail HSP70 over time. CjHSPA8 has 10 amino acid substitutions relative to GgHSC70 , which is the same as what was found for the guinea fowl gene NmHSPA8 (Iwamoto et al . 2005).…”

Section: Discussionsupporting

confidence: 82%

“…Complete cDNA sequences for CjHSPA2 , CjHSPA5 and CjHSPA8 were amplified using the rapid amplification of cDNA ends (RACE) method (SMART RACE cDNA Amplification Kit; BD Biosciences Clontech, Palo Alta, CA, USA) in accordance to a previous report (Sricharoen et al . 1998; Iwamoto et al . 2005).…”

Section: Methodsmentioning

confidence: 99%

“…GgHSP70 and GgHSC70 have not previously been annotated in the chicken genome map (NCBI 2000). Our previous report suggests that the guinea fowl genes NmHSPA2 and NmHSPA8 and the chicken genes GgHSP70 and GgHSC70 are orthologous to HSPA2 and HSPA8 orthologous genes (Iwamoto et al . 2005).…”

Section: Introductionmentioning

confidence: 99%

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Identification of heat shock protein 70 genes HSPA2, HSPA5 and HSPA8 from the Japanese quail, Coturnix japonica

Iwamoto

Sato

Hosomichi

et al. 2008

Animal Science Journal

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We have identified three members of the heat shock protein (HSP) 70 family from the Japanese quail, Coturnix japonica. The coding regions of the genes, CjHSPA2, CjHSPA5 and CjHSPA8, exhibit more than 96% similarity to related genes in the chicken, GgHSP70, GgHSPA5 and GgHSC70. The putative proteins encoded by the quail genes contain motifs considered essential for HSP70 family members. In addition, the predicted proteins are more similar to HSPA2, HSPA5, and HSPA8 proteins from vertebrates than they are to other members of the HSP70 family. As is true for orthologs from chicken and mammals, the quail genomic loci consist of a single exon (CjHSPA2) or eight exons (CjHSPA5 and CjHSPA8). The promoter regions of the genes also contain conserved motifs and are similar in structure to promoter regions of related genes in other species. Furthermore, gene order in the regions surrounding the quail HSP70 has been preserved, providing evidence that the genomic regions are orthologous to HSP70-containing regions in the chicken genome. One of the quail HSP70-related genes, CjHSPA2, exhibited a robust response to heat shock treatment and transcription of CjHSPA8 mRNA was weakly induced by heat treatment. Taken together, the data suggest that CjHSPA2, CjHSPA5 and CjHSPA8 encode orthologs of HSPA2, HSPA5 and HSPA8 with the notable difference that CjHSPA2 and CjHSPA8 are heat shock-inducible genes, whereas HSPA2 and HSPA8 are constitutively expressed in a heat shock-independent manner.

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Section: Discussionsupporting

confidence: 82%

Section: Methodsmentioning

confidence: 99%

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Identification of heat shock protein 70 genes HSPA2, HSPA5 and HSPA8 from the Japanese quail, Coturnix japonica

Iwamoto

Sato

Hosomichi

et al. 2008

Animal Science Journal

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“…Thus, we conclude that acclimatization leads to a complete change in response to HS. The HSPA8 gene (up-regulated in all contrast) is a member of the HSP70 family of molecular chaperones and is known to play an important role in directing correct folding of newly synthesized proteins and in the destruction of non-reversibly denatured proteins (Hartl, 1996; Iwamoto et al, 2005). HSPA8 has been found to be up-regulated under HS in chickens (Sun et al, 2015b; Wang et al, 2015) and could serve as a good biomarker.…”

Section: Discussionmentioning

confidence: 99%

Cardiac and Skeletal Muscle Transcriptome Response to Heat Stress in Kenyan Chicken Ecotypes Adapted to Low and High Altitudes Reveal Differences in Thermal Tolerance and Stress Response

et al. 2019

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Heat stress (HS) negatively affects chicken performance. Agricultural expansion will happen in regions that experience high ambient temperatures, where fast-growing commercial chickens are vulnerable. Indigenous chickens of such regions, due to generations of exposure to environmental challenges, might have higher thermal tolerance. In this study, two indigenous chicken ecotypes, from the hot and humid Mombasa (lowland) and the colder Naivasha (highland) regions, were used to investigate the effects of acute (5 h, 35°C) and chronic (3 days of 35°C for 8 h/day) HS on the cardiac and skeletal muscle, through RNA sequencing. The rectal temperature gain and the number of differentially expressed genes (DEGs) [False Discovery Rate (FDR) < 0.05] were two times higher in the acute stage than in the chronic stage in both ecotypes, suggesting that cyclic exposure to HS can lead to adaptation. A tissue- and stage-specific difference in response to HS was observed, with peroxisome proliferator-activated-receptor (PPAR) signaling and mitogen-activate protein kinase (MAPK) signaling pathways, enriched in heart and skeletal muscle, respectively, and the p53 pathway enriched only in the acute stage in both tissues. The acute and chronic stage DEGs were integrated by a region-specific gene coexpression network (GCN), and genes with the highest number of connections (hub genes) were identified. The hub genes in the lowland network were CCNB2, Crb2, CHST9, SESN1, and NR4A3, while COMMD4, TTC32, H1F0, ACYP1, and RPS28 were the hub genes in the highland network. Pathway analysis of genes in the GCN showed that p53 and PPAR signaling pathways were enriched in both low and highland networks, while MAPK signaling and protein processing in endoplasmic reticulum were enriched only in the gene network of highland chickens. This shows that to dissipate the accumulated heat, to reduce heat induced apoptosis, and to promote DNA damage repair, the ecotypes activated or suppressed different genes, indicating the differences in thermal tolerance and HS response mechanisms between the ecotypes. This study provides information on the HS response of chickens, adapted to two different agro climatic environments, extending our understanding of the mechanisms of HS response and the effect of adaptation in counteracting HS.

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Review: The role of heat shock proteins in chicken: Insights into stress adaptation and health

Abare,

Rahayu,

Tugiyanti

2023

Research in Veterinary Science

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Identification of cDNA for the HSPA2, HSPA5 and HSPA8 orthologs of the heat shock protein 70 family from guinea fowl (Numida meleagris)

Cited by 3 publications

References 13 publications

Identification of heat shock protein 70 genes HSPA2, HSPA5 and HSPA8 from the Japanese quail, Coturnix japonica

Identification of heat shock protein 70 genes HSPA2, HSPA5 and HSPA8 from the Japanese quail, Coturnix japonica

Cardiac and Skeletal Muscle Transcriptome Response to Heat Stress in Kenyan Chicken Ecotypes Adapted to Low and High Altitudes Reveal Differences in Thermal Tolerance and Stress Response

Review: The role of heat shock proteins in chicken: Insights into stress adaptation and health

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