Heat shock proteins and heat adaptation of the whole organism

Moseley, Pope L.

doi:10.1152/jappl.1997.83.5.1413

Cited by 276 publications

(224 citation statements)

References 47 publications

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“…The function of many heat shock factors (HSFs) are to act as chaperones assisting in protein folding thereby avoiding protein aggregation (Lindquist and Craig 1988;Hightower 1991;Moseley 1997) which results in protein homeostasis during cellular response to HS. In all, 20 genes encoding molecular chaperones were upregulated in response to HS (Table 3).…”

Section: Heat Stress Resulted In the Activation Of Heat Shock Factorsmentioning

confidence: 99%

Characterization of genes and pathways that respond to heat stress in Holstein calves through transcriptome analysis

Srikanth

Kwon

Lee

2017

Cell Stress and Chaperones

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This study aimed to investigate the genes and pathways that respond to heat stress in Holstein bull calves exposed to severe ranges of temperature and humidity. A total of ten animals from 4 to 6 months of age were subjected to heat stress at 37°C and 90 % humidity for 12 h. Skin and rectal temperatures were measured before and after heat stress; while no correlation was found between them before heat stress, a moderate correlation was detected after heat stress, confirming rectal temperature to be a better barometer for monitoring heat stress. RNAseq analysis identified 8567 genes to be differentially regulated, out of which 465 genes were significantly upregulated (≥2-fold, P < 0.05) and 49 genes were significantly downregulated (≤2-fold, P < 0.05) in response to heat stress. Significant terms and pathways enriched in response to heat stress included chaperones, cochaperones, cellular response to heat stress, phosphorylation, kinase activation, immune response, apoptosis, Toll-like receptor signaling pathway, Pi3K/AKT activation, protein processing in endoplasmic reticulum, interferon signaling, pathways in cancer, estrogen signaling pathway, and MAPK signaling pathway. The differentially expressed genes were validated by quantitative realtime PCR analysis, which confirmed the tendency of the expression. The genes and pathways identified in this analysis extend our understanding of transcriptional response to heat stress and their likely functioning in adapting the animal to hyperthermic stress. The identified genes could be used as candidate genes for association studies to select and breed animals with improved heat tolerance.

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Section: Heat Stress Resulted In the Activation Of Heat Shock Factorsmentioning

confidence: 99%

Characterization of genes and pathways that respond to heat stress in Holstein calves through transcriptome analysis

Srikanth

Kwon

Lee

2017

Cell Stress and Chaperones

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“…In mammalian cells, there are five major families of HSPs, namely, the HSP100, HSP90, HSP70, HSP60 and small HSP (exemplified by HSP27/HSP25) (reviewed in Gething and Sambrook 10 ). One characteristic feature of heat-shocked somatic cells is the abundant expression of inducible HSP70s (HSP70i) (reviewed in Kregel 11 and Moseley 12 ), which exert antiapoptotic effects that include: (i) inhibition of caspase-3 activation by the apoptosome, 13 and (ii) antagonizing the action of apoptosis-inducing factor (AIF), which is involved in caspase-independent apoptosis. 14 In fact, different HSPs can interfere with both anti-and proapoptotic pathways (reviewed in Beere 8 and Sreedhar and Csermely 9 ).…”

Section: Introductionmentioning

confidence: 99%

Spermatocyte-specific expression of constitutively active heat shock factor 1 induces HSP70i-resistant apoptosis in male germ cells

et al. 2005

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Spermatocytes, the most sensitive male germ cells to heatinduced apoptosis, do not respond to hyperthermia by inducing heat shock proteins (HSPs), including HSP70i, which has been previously shown to confer resistance to apoptosis in somatic cells. To dissect the mechanism of heat-induced apoptosis and to determine if we could protect spermatocytes by expressing HSP70i, we engineered transgenic mice that express in spermatocytes constitutively active heat shock transcription factor (HSF)1. Such HSF1 expression did not lead to transcription of inducible Hsp70 genes, but instead induced caspase-dependent apoptosis that mimicked heat shock-induced death of spermatogenic cells. Both mitochondria-dependent and death receptor-dependent pathways appear to be involved in such HSF1-induced apoptosis: the levels of Bcl-2 family proteins became increased, p53 protein accumulated and expression levels of caspase-8 and deathreceptor-interacting proteins (including Fas-associated death domain protein and TNF receptor associated death domain protein) became elevated. Surprisingly, the constitutive spermatocyte-specific expression of HSP70i in doubletransgenic males did not protect against such HSF1-induced apoptosis.

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“…Hsps are highly conserved throughout evolution in various organisms ranging from yeast cells to mammalian neurons, and can be induced by many forms of stress, including heat and oxidative injury (Becker and Craig, 1994). They can be divided into five different families according to their molecular weights: 25-30 kDa, 60 kDa, 70 kDa, 90 kDa, and 105 kDa (Moseley, 1997).…”

Section: Introduction Hmentioning

confidence: 99%

The Effect of Neonatal Nerve Injury on the Expression of Heat Shock Proteins in Developing Rat Motoneurones

Kalmár¹,

Burnstock

Vrbová

et al. 2002

Journal of Neurotrauma

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The expression of the heat shock proteins hsp27 and hsp70 was examined in the spinal cord and sciatic nerves of developing rats. Using immunohistochemistry, we found that hsp27 is present in many motoneurones at birth. With development, the intensity of staining increases, reaching adult levels by 21 days, when all sciatic motoneurones express hsp27. In the sciatic nerve, hsp27 is strongly expressed throughout postnatal development. In contrast, hsp70 immunoreactivity in motoneurones and the sciatic nerve is weak at birth and does not change with development. The expression of heat shock proteins has been shown to increase in cells under conditions of stress, where they have beneficial effects on cell survival. The effect of neonatal nerve injury on hsp27 and hsp70 expression was also examined in this study. Four days after injury, staining for hsp27 increases in motoneurones, whereas hsp70 does not change. However, there is a significant increase in hsp70 staining in glial cells surrounding the injured motor pool, predominantly in astrocytes. Since neonatal nerve injury induces apoptotic motoneurone death, we also studied the co-expression of hsp27 with markers of apoptosis. No hsp27-positive motoneurones were found to be apoptotic, as assessed by both TUNEL and caspase-3 immunoreactivity. Therefore, it is possible that the upregulation of hsp27 observed in injured motoneurones may play a role in protecting motoneurones from apoptotic cell death following nerve injury.

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Heat shock proteins and heat adaptation of the whole organism

Cited by 276 publications

References 47 publications

Characterization of genes and pathways that respond to heat stress in Holstein calves through transcriptome analysis

Characterization of genes and pathways that respond to heat stress in Holstein calves through transcriptome analysis

Spermatocyte-specific expression of constitutively active heat shock factor 1 induces HSP70i-resistant apoptosis in male germ cells

The Effect of Neonatal Nerve Injury on the Expression of Heat Shock Proteins in Developing Rat Motoneurones

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