A 252 bp upstream region of the rat spermatocyte-specific hst70 gene is sufficient to promote expression of the hst70-CAT hybrid gene in testis and brain of transgenic mice

Widłak, Wiesława; Markkula, Merja; Krawczyk, Zdzisłlaw; Kananen, Kirsi; Huhtaniemi, Ilpo

doi:10.1016/0167-4781(95)00135-4

Cited by 22 publications

(61 citation statements)

References 41 publications

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“…The activity of the Hspa2 gene promoter was studied in tissues of adult pHST(897/ 62)-EGFP and pHST(1195/62)-EGFP + INS transgenic mice described earlier (Rupik et al 2006). Both transgenes contained long fragments of Hspa2 promoter that enabled a reporter gene expression speciWc for testes and certain other organs, what was shown previously in transgenic mice with CAT reporter gene (Widlak et al 1994(Widlak et al , 1995. First, we examined EGFP expression in several pHST(897/62)-EGFP transgenic lines and found quite substantial diVerences in EGFP intensity and distribution between such lines (Table 1).…”

Section: Characterization Of Hspa2 Gene Promoter Activity In Hspa2-egmentioning

confidence: 77%

“…SigniWcant level of the gene expression was also observed in brain (Widlak et al 1994(Widlak et al , 1995Murashov and Wolgemuth 1996b;Scieglinska et al 1997). However, in many others somatic tissues Hspa2 transcription was shown to be very low in rodents (Scieglinska et al 1997), but abundant in human (Bonnycastle et al 1994;Roux et al 1994).…”

Section: Introductionmentioning

confidence: 86%

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The expression pattern of the 70-kDa heat shock protein Hspa2 in mouse tissues

Vydra

Winiarski

Rak-Raszewska

et al. 2009

Histochem Cell Biol

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The highest expression level of a 70-kDa heat shock protein family member Hspa2 is detected specifically in meiotic and post-meiotic male germ cells, which is reflected by original name of this protein, i.e., testis-specific Hsp70. However, this chaperon protein could be also detected in certain somatic tissues. Here, the extra-testicular expression pattern of mouse Hspa2 was analyzed. We found expression of Hspa2 in various epithelial cells including lining of bronchioles and oviduct, columnar epithelium of endometrium, epithelial reticular cells of thymus, transitional epithelium of the urinary bladder, or ependymal cells covering walls of the ventricular system of the brain. Surprisingly, Hspa2 was a putative secretory protein in intestine, endometrial glands and subcommissural organ. Hspa2 was detected in central and peripheral nervous system: in neuron's bodies and fiber tracts, in the subventricular zone of the lateral ventricles, in the dentate gyrus of the hippocampus, in enteric ganglia of the gastrointestinal tract. Hspa2 was also expressed in smooth muscles and at low level in immune system (in germinal centers associated with B-lymphocyte production). In addition to somatic tissues listed above, Hspa2 was detected in oocytes arrested at diplotene of the first meiotic division.

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Section: Characterization Of Hspa2 Gene Promoter Activity In Hspa2-egmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 86%

The expression pattern of the 70-kDa heat shock protein Hspa2 in mouse tissues

Vydra

Winiarski

Rak-Raszewska

et al. 2009

Histochem Cell Biol

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“…41,42 The hHSF1DRD gene under the control of the rat Hst70/Hsp70.2 gene promoter (Figure 2a) was used to generate three lines of transgenic mice and the line with highest testis-specific expression of the hHSF1DRD was chosen for further experiments. Though transgenic males proved to be infertile, transgenic females were fertile and did not reveal any specific phenotype.…”

Section: Resultsmentioning

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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“…In the mouse, the product of the HspA2 gene is a molecular chaperone essential for progression of meiosis, and is involved in synaptonemal complexes disassembly, formation of active CDC2/cyclin B1 complex in spermatocytes [Dix et al, 1996;Zhu et al, 1997], as well as in chaperoning transition proteins 1 and 2 in spermatids [Govin et al, 2006]. In a majority of extra-testicular tissues of adult rodents, the HspA2 expression is either very low or fully repressed, and relatively high level of transcripts has been found only in the brain [Widłak et al, 1995;Murashov and Wolgemuth, 1996;Ś ciegliń ska et al, 1997]. Recently, expression of the mouse HspA2 gene during embryogenesis was also reported [Rupik et al, 2006].…”

mentioning

confidence: 99%

The HspA2 protein localizes in nucleoli and centrosomes of heat shocked cancer cells

Ścieglińska

Pigłowski

Mazurek

et al. 2008

J of Cellular Biochemistry

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The human HSPA2 gene, which belongs to the HSP70 family of heat shock genes, is a counterpart of rodent testis-specific HspA2 gene. Rodent genes are expressed mainly in pachytene spermatocytes, while transcripts of human HSPA2 gene have been detected in various normal somatic tissues, albeit translation of the messenger RNA into corresponding protein has not been yet unambiguously demonstrated, except for several cancer cell lines. The aim of our work, a first step in search for HspA2 function in cancer cells, was to establish its intracellular localization at physiological temperature and during heat shock. First, we used qRT-PCR and a highly specific antibody to select cell lines with the highest expression of the HspA2 protein, which turned out to be A549 and NCI-H1299 lines originating from non-small cell lung carcinoma (NSCLC). Significant expression of the HspA2 was also detected by immunohistochemistry in primary NSCLC specimens. Intracellular localization of the HspA2 was studied using both the specific anti-HspA2 polyclonal antibody and transfection of cells with fusion proteins HspA2-EGFP and mRFP-HspA2. We found that, at physiological temperature, the HspA2 was localized primarily in cytoplasm whereas, during heat shock, localization shifted to nucleus and nucleoli. Moreover, we demonstrate that in heat-shocked cells HspA2 accumulated in centrosomes. Our results suggest that the HspA2, like Hsp70 protein, can be involved in protecting nucleoli and centrosomes integrity in cancer cells subjected to heat shock and, possibly, other cellular stressors.

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A 252 bp upstream region of the rat spermatocyte-specific hst70 gene is sufficient to promote expression of the hst70-CAT hybrid gene in testis and brain of transgenic mice

Cited by 22 publications

References 41 publications

The expression pattern of the 70-kDa heat shock protein Hspa2 in mouse tissues

The expression pattern of the 70-kDa heat shock protein Hspa2 in mouse tissues

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

The HspA2 protein localizes in nucleoli and centrosomes of heat shocked cancer cells

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