RNA polymerase II interacts with the Hspa1b promoter in mouse epididymal spermatozoa

Wilkerson, Donald C.; Sarge, Kevin D.

doi:10.1530/rep-09-0015

Cited by 16 publications

(13 citation statements)

References 70 publications

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“…HSPA1B belongs to HSP70 family and it is one of the most extensively studied heat inducible HSPs (Kampinga et al 2009, Stetler et al 2010, Scieglinska et al 2011. Recent studies have demonstrated that HSF1, HSF2, SP1, and RNA polymerase II are bound to the Hspa1b promoter in the mature spermatozoa of mice, allowing the rapid expression of this cytoprotective gene if the cells encounter stress (Xing et al 2005, Wilkerson et al 2008, Wilkerson & Sarge 2009. In this study, we elucidate the novel post-transcriptional regulation of HSPA1B by miR-15a, extend our knowledge of stress-induced heat-shock response pathway.…”

Section: Discussionmentioning

confidence: 99%

Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele

Mou

et al. 2014

Reproduction

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Hyperthermia and oxidative stresses are the two central elements contributing to varicocele-related sperm damage. Growing evidence indicates that microRNAs (miRNAs) are involved in the regulation of the heat and oxidative stress responses. In this study, we analyzed the expressions of several stress-related miRNAs in the sperm and found that the expression of miR-15a was significantly decreased in patients with varicocele compared with the control. Furthermore, miR-15a repressed the expression of HSPA1B, which is a typical stressinduced chaperone protein, through directly binding its 3 0 -UTR. The expressions of miR-15a and HSPA1B exhibited an inverse correlation in sperm. Our results provide a valuable insight into the varicocele-related sperm impairment and male infertility, and may help to develop potential therapeutic targets and novel biomarkers for male infertility.

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Section: Discussionmentioning

confidence: 99%

Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele

Mou

et al. 2014

Reproduction

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“…HSFs are transcription factors that bind specific cis-acting sequences upstream of the heat shock gene promoters called heat shock elements (HSE), which consist of multiple adjacent inverted arrays of the 5′-nGAAn-3′ binding site [39-41]. Intermingled to HSE elements there are conventional AT-rich (TATA) and GC-rich (SP1) start sites, CCAAT boxes and AP1/AP2 control elements, suggesting that heat shock genes may be both induced in response to stress and expressed under non-stress conditions [42-44]. TBP (TATA-binding protein) and GAGA are transcription factors that bind HSP gene promoters under physiological conditions, while heat shock factors, like HSF1, regulate HSP expression in response to stressful insults [45-47].…”

Section: Hsf1 and Modulation Of The Heat Shock Responsementioning

confidence: 99%

Inducible Hsp70 in the Regulation of Cancer Cell Survival: Analysis of Chaperone Induction, Expression and Activity

Zorzi

Bonvini

2011

Cancers

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Understanding the mechanisms that control stress is central to realize how cells respond to environmental and physiological insults. All the more important is to reveal how tumour cells withstand their harsher growth conditions and cope with drug-induced apoptosis, since resistance to chemotherapy is the foremost complication when curing cancer. Intensive research on tumour biology over the past number of years has provided significant insights into the molecular events that occur during oncogenesis, and resistance to anti-cancer drugs has been shown to often rely on stress response and expression of inducible heat shock proteins (HSPs). However, with respect to the mechanisms guarding cancer cells against proteotoxic stresses and the modulatory effects that allow their survival, much remains to be defined. Heat shock proteins are molecules responsible for folding newly synthesized polypeptides under physiological conditions and misfolded proteins under stress, but their role in maintaining the transformed phenotype often goes beyond their conventional chaperone activity. Expression of inducible HSPs is known to correlate with limited sensitivity to apoptosis induced by diverse cytotoxic agents and dismal prognosis of several tumour types, however whether cancer cells survive because of the constitutive expression of heat shock proteins or the ability to induce them when adapting to the hostile microenvironment remains to be elucidated. Clear is that tumours appear nowadays more “addicted” to heat shock proteins than previously envisaged, and targeting HSPs represents a powerful approach and a future challenge for sensitizing tumours to therapy. This review will focus on the anti-apoptotic role of heat shock 70kDa protein (Hsp70), and how regulatory factors that control inducible Hsp70 synthesis, expression and activity may be relevant for response to stress and survival of cancer cells.

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“…This protein is present under normal and stress conditions (Christians et al, 1997). Previous studies carried out in early embryonic and gametic stages have shown that the expression of HSP genes affects follicular development, embryonic survival, and pregnancy maintenance (Britt, 1992;Sağırkaya et al, 2006;Wilkerson & Sarge, 2009). The expression of HSP genes is related to thermal stress.…”

Section: Introductionmentioning

confidence: 99%

Genetic diversity of the 3ꞌ and 5ꞌ untranslated regions of the <i>HSP70.1</i> gene between native Turkish and Holstein Friesian cattle breeds

et al. 2017

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Heat stress proteins are important factors in protecting cells against environmental stress. The HSP70.1 gene is one of the most important members of the heat stress protein family, which is essential for life, production and reproduction. In this study, partial regions of HSP70.1 (3ꞌ and 5ꞌ untranslated regions (UTRs)) were sequenced in six cattle breeds. Blood samples of five native breeds, namely Yerli Kara (YK), Boz ırk (BI), Yerli Güney Sarısı (YGS), Güney Doğu Anadolu Kırmızısı (GAK) and Doğu Anadolu Kırmızısı (DAK) were collected from their native regions and blood samples of the Holstein Friesian (Siyah Alaca (SA)) breed were collected from each of these regions. Totals of 249 and 206 animals were analysed for the HSP70.1-3ꞌ and 5ꞌ UTR regions, respectively. In the 3ꞌ UTR region, 13 single nucleotide polymorphisms (SNPs) and one indel were found, whereas this region was found to be monomorphic among animals of the Holstein Friesian breed. In the 5ꞌ UTR region, 43 SNPs and three indels were revealed in all of the investigated breeds. On the other hand, a new C983T nucleotide substitution was identified in this region, and is thought to disrupt the Sp1-hsp70 promoter binding site. The 5ꞌ UTR region was also more variable in the Turkish native breeds than in the Holstein Friesian. This study is the first to investigate the 3ꞌ and 5ꞌ UTRs of the HSP70.1 gene in Turkish native breeds. The genetic structure of these gene regions in Turkish native cattle breeds was found to be quite different from those of other cattle breeds that had been studied in the past.

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RNA polymerase II interacts with the Hspa1b promoter in mouse epididymal spermatozoa

Cited by 16 publications

References 70 publications

Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele

Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele

Inducible Hsp70 in the Regulation of Cancer Cell Survival: Analysis of Chaperone Induction, Expression and Activity

Genetic diversity of the 3ꞌ and 5ꞌ untranslated regions of the <i>HSP70.1</i> gene between native Turkish and Holstein Friesian cattle breeds

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