Induction of <i>HSP70</i> Gene Expression by the Antiproliferative Prostaglandin PGA<sub>2</sub>: A Growth-Dependent Response Mediated by Activation of Heat Shock Transcription Factor

Holbrook, Nikki J.; Carlson, Sara G.; Choi, Augustine M.K.; Fargnoli, Joseph

doi:10.1128/mcb.12.4.1528-1534.1992

Cited by 17 publications

(3 citation statements)

References 29 publications

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“…Chaperones may help diagnose many disorders, for example, tumors [ 94 , 95 ], heart diseases [ 96 ], rheumatologic disorders [ 97 ], and infectious or neurodegenerative disorders [ 98 ]. Hsp70 levels increase as a result of the accumulation of physical and chemical agents or stressors during life.…”

Section: Chaperones As Diagnostic Markersmentioning

confidence: 99%

“…Hsp70 levels increase as a result of the accumulation of physical and chemical agents or stressors during life. When stress agents occur, there is a promotion of genes coding Hsp70, and increased production is a cell’s response [ 96 ]. The proteins created should enhance cell resistance to stressors and recovery from injury.…”

Section: Chaperones As Diagnostic Markersmentioning

confidence: 99%

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Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Batko,

Antosz,

Miśków

et al. 2024

IJMS

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The review describes correlations between impaired functioning of chaperones and co-chaperones in Alzheimer’s disease (AD) pathogenesis. The study aims to highlight significant lines of research in this field. Chaperones like Hsp90 or Hsp70 are critical agents in regulating cell homeostasis. Due to some conditions, like aging, their activity is damaged, resulting in β-amyloid and tau aggregation. This leads to the development of neurocognitive impairment. Dysregulation of co-chaperones is one of the causes of this condition. Disorders in the functioning of molecules like PP5, Cdc37, CacyBP/SIPTRAP1, CHIP protein, FKBP52, or STIP1 play a key role in AD pathogenesis. PP5, Cdc37, CacyBP/SIPTRAP1, and FKBP52 are Hsp90 co-chaperones. CHIP protein is a co-chaperone that switches Hsp70/Hsp90 complexes, and STIP1 binds to Hsp70. Recognition of precise processes allows for the invention of effective treatment methods. Potential drugs may either reduce tau levels or inhibit tau accumulation and aggregation. Some substances neuroprotect from Aβ toxicity. Further studies on chaperones and co-chaperones are required to understand the fundamental tenets of this topic more entirely and improve the prevention and treatment of AD.

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Section: Chaperones As Diagnostic Markersmentioning

confidence: 99%

Section: Chaperones As Diagnostic Markersmentioning

confidence: 99%

Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Batko,

Antosz,

Miśków

et al. 2024

IJMS

View full text Add to dashboard Cite

show abstract

“…During the progression of apoptosis, PGA2 has been shown to induce stress proteins such as GADD153, p21, c-Myc and HSP-70 which play important roles in many models of apoptosis [1,[5][6][7]. So, many reports have been focused on the role of these stress proteins in PGA2-induced cell death.…”

Section: Introductionmentioning

confidence: 99%

Prostaglandin A₂-induced Apoptosis is Not Inhibited by Heme Oygenase-1 in U2OS Cells

Ko¹,

Lee²,

Ahn³

et al. 2008

Journal of Life Science

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Prostaglandin A2 (PGA2), one of cyclopentenone PGs, induced both apoptosis and heme oxygenase (HO)-1 expression in U2OS cells. PGA2-induced apoptosis was not perturbed by either over-expression or knock-down of HO-1, whereas H2O2-induced cell death was inversely modulated by the expression level of HO-1. In addition, N-acetyl-L-cysteine (NAC), a thiol antioxidant, blocked both apoptosis and HO-1 expression induced by PGA2. But, non-thiol antioxidants like butylated hydorxyanisole (BHA) and ascorbic acid did not block either apoptosis or HO-1-induction. Taken together, these results suggest that PGA2 induces both apoptosis and HO-1 expression, which are critically related to the thiol-reactivity of PGA2, but not oxidative stress, and HO-1 expression may be independent or functionally located downstream of apoptosis by PGA2 without contribution to apoptosis progression.

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Selective postmortem degradation of inducible heat shock protein 70 (hsp70) mRNAs in rat Brain

1994

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1. Altered mRNA levels in postmortem brain tissue from persons with Alzheimer's disease (AD) or other neurological diseases are usually presumed to be characteristic of the disease state, even though both agonal state (the physiological state immediately premortem) and postmortem interval (PMI) (the time between death and harvesting the tissue) have the potential to affect levels of mRNAs measured in postmortem tissue. Although the possible effect of postmortem interval on mRNA levels has been more carefully evaluated than that of agonal state, many studies assume that all mRNAs have similar rates of degradation postmortem. 2. To determine the postmortem stability of inducible heat shock protein 70 (hsp70) mRNAs, themselves unstable in vivo at normal body temperature, rats were heat shocked in order to induce synthesis of the hsp70 mRNAs. hsp70 mRNA levels in cerebellum and cortex were then compared to those of their heat shock cognate 70 (hsc70) mRNAs, as well as to levels of 18S rRNAs, at 0 and at 24 hr postmortem. 3. Quantiation of northern blots after hybridization with an hsp70 mRNA-specific oligo probe indicated a massive loss of hsp70 mRNA signal in RNAs isolated from 24-hr postmortem brains; quantitation by slot-blot hybridization was 5- to 15-fold more efficient. Even using the latter technique, hsp70 mRNA levels were reduced by 59% in 24-hr-postmortem cerebellum and by 78% in cortex compared to mRNA levels in the same region of 0-hr-postmortem brain. There was little reduction postmortem in levels of the hsp70 mRNAs or of 18S rRNAs in either brain region. 4. In situ hybridization analysis indicated that hsp70 mRNAs were less abundant in all major classes of cerebellar cells after 24 hr postmortem and mRNAs had degraded severalfold more rapidly in neurons than in glia. There was no corresponding loss of intracellular 18S rRNA in any cell type. 5. We conclude from these results that the effect of postmortem interval on mRNA degradation must be carefully evaluated when analyzing levels of inducible hsp70 mRNAs, and perhaps other short-lived mRNAs, in human brain.

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Induction of HSP70 Gene Expression by the Antiproliferative Prostaglandin PGA₂: A Growth-Dependent Response Mediated by Activation of Heat Shock Transcription Factor

Cited by 17 publications

References 29 publications

Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Prostaglandin A₂-induced Apoptosis is Not Inhibited by Heme Oygenase-1 in U2OS Cells

Selective postmortem degradation of inducible heat shock protein 70 (hsp70) mRNAs in rat Brain

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Induction of HSP70 Gene Expression by the Antiproliferative Prostaglandin PGA2: A Growth-Dependent Response Mediated by Activation of Heat Shock Transcription Factor

Cited by 17 publications

References 29 publications

Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease

Prostaglandin A2-induced Apoptosis is Not Inhibited by Heme Oygenase-1 in U2OS Cells

Selective postmortem degradation of inducible heat shock protein 70 (hsp70) mRNAs in rat Brain

Contact Info

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Induction of HSP70 Gene Expression by the Antiproliferative Prostaglandin PGA₂: A Growth-Dependent Response Mediated by Activation of Heat Shock Transcription Factor

Prostaglandin A₂-induced Apoptosis is Not Inhibited by Heme Oygenase-1 in U2OS Cells