Expression of HSP86 in male germ cells.

Lee, Se Jin

doi:10.1128/mcb.10.6.3239

Cited by 53 publications

(43 citation statements)

References 20 publications

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“…This finding suggests that HSP90 is involved in the pre-meiotic development of spermatogenic cells. In agreement with our immunocytochemical results, Lee (1990) and Gruppi et al (1991) detected high levels of HSP90 transcripts in mouse meiotic prophase spermatogenic cells by Northern blot analysis and in situ hybridization using specific probes to human HSP89 (a and f3). Since they showed that mouse HSP86 gene transcripts identical to the a-isoform are expressed more abundantly than the P-isofom, we suggest that the protein that we detect in spermatogonia is most likely the HSP90a isoform of rat.…”

Section: Discussionsupporting

confidence: 93%

“…HSP90 appears to repress the activities of these cytosolic factors and potentially influences gene expression of the cell. In mammalian testis, it has been reported that murine HSP86 mRNA is highly expressed in mouse testis, especially in pre-meiotic spermatogenic cells (Lee, 1990;Gruppi et al, 1991). This finding is of particular interest with respect to studies on germ cell devel-opment, because mammalian germ cells differentiate in response to steroid hormones and are present within a tissue not only affected by but involved in the synthesis of steroid hormones.…”

Section: ~67-76 1995)mentioning

confidence: 99%

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Immunocytochemical observation of the 90 KD heat shock protein (HSP90): high expression in primordial and pre-meiotic germ cells of male and female rat gonads.

Ohsako¹,

Bunick²,

Hayashi³

1995

J Histochem Cytochem.

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We used immunocytochemistry to detect the 90 ~0 major heat shock protein (HSW), a potential regulator of gene expression, during male and female rat gonad development. In the Day 13.0 post-coital (dpc) fetal gonad, strong immunoreactivity to anti-HSP90 antibody was shown in the cytoplasm of primordial germ cells (PGCs). Other somatic cells in the gonad showed only faint reactivity. During testicular development, strong immunostaining was observed in the cytoplasm of embryonic germ cells and in spermatogonia and spermatocytes of the pre-pubertal testis. In adult testis reactivity of spermatogonia and pachytene spermatocytes was strong but reactivity of post-meiotic spermatogenic cells, i.e., secondary spermatocytes and spermatids, was ex-

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Section: Discussionsupporting

confidence: 93%

Section: ~67-76 1995)mentioning

confidence: 99%

Immunocytochemical observation of the 90 KD heat shock protein (HSP90): high expression in primordial and pre-meiotic germ cells of male and female rat gonads.

Ohsako¹,

Bunick²,

Hayashi³

1995

J Histochem Cytochem.

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“…It was hypothesized previously that RNAs could be localized in cells by a mechanism involving a combination of generalized degradation and local protection (19 (25,52), is expressed in germ cells (8,20,38) as might be a human Hsp85 gene (34), suggesting that members of the Hsp9O gene family might serve similar functions in germ cells of diverse animal species (33).…”

Section: Discussionmentioning

confidence: 99%

Dynamic Hsp83 RNA localization during Drosophila oogenesis and embryogenesis.

Parkhurst¹,

Halsell²,

Lipshitz³

1993

Mol. Cell. Biol.

116

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Hsp83 is the Drosophila homolog of the mammalian Hsp9O family of regulatory molecular chaperones. We show that maternally synthesized Hsp83 transcripts are localized to the posterior pole of the early Drosophila embryo by a novel mechanism involving a combination of generalized RNA degradation and local protection at the posterior. This protection ofHsp83 RNA occurs in wild-type embryos and embryos produced by females carrying the maternal effect mutations nanos and pumilio, which eliminate components of the posterior polar plasm without disrupting polar granule integrity. In contrast, Hsp83 RNA is not protected at the posterior pole of embryos produced by females carrying maternal mutations that disrupt the posterior polar plasm and the polar granules-cappuccino, oskar, spire, staufen, tudor, valois, and vasa. Mislocalization of oskar RNA to the anterior pole, which has been shown to result in induction of germ cells at the anterior, leads to anterior protection of maternal Hsp83 RNA. These results suggest that Hsp83 RNA is a component of the posterior polar plasm that might be associated with polar granules. In addition, we show that zygotic expression of Hsp83 commences in the anterior third of the embryo at the syncytial blastoderm stage and is regulated by the anterior morphogen, bicoid. We consider the possible developmental significance of this complex control of Hsp83 transcript distribution.Cytoplasmically localized determinants, in the form of localized maternal RNAs and proteins, play a key role in providing positional cues in the oocyte and early embryo of Drosophila melanogaster. To date, two RNAs localized to the anterior pole of both the oocyte and the early embryo have been described: bicoid RNA, which encodes the anterior determinant (12,13,58,59), and RNA encoding a

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“…Although there is no direct evidence that IME2 and the rat mak1 kinase genes are functional homologs, one (HSP84) of the two members of the murine HSP90 genes is specifically expressed in male meiotic germ cells (36), suggesting that the relationship of these meiotic regulatory kinases to these target promoters may indeed be phylogenetically conserved. Meiotic induction of rodent HSP84 may furthermore involve HSF because HSF2 accumulates in sperm cells and is able to constitutively bind to HSEs of testis-specific HSP70 genes (57).…”

mentioning

confidence: 99%

“…HSP82 is an intensively studied heat shock gene that relies primarily on a single heat shock element (HSE) adjacent to the promoter to drive vegetative and heatinduced transcription (18,19,35,46,72). It is likely that Hsp82p has a phylogenetically conserved function during meiosis or early oogenesis because its homologs are similarly expressed in other fungi (9), the fruit fly (12), and mammals (22,36).…”

mentioning

confidence: 99%

A Bipartite Operator Interacts with a Heat Shock Element To Mediate Early Meiotic Induction of Saccharomyces cerevisiae HSP82

Szent-Györgyi

1995

Molecular and Cellular Biology

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Although key genetic regulators of early meiotic transcription in Saccharomyces cerevisiae have been well characterized, the activation of meiotic genes is still poorly understood in terms of cis-acting DNA elements and their associated factors. I report here that induction of HSP82 is regulated by the early meiotic IME1-IME2 transcriptional cascade. Vegetative repression and meiotic induction depend on interactions of the promoterproximal heat shock element (HSE) with a nearby bipartite repression element, composed of the ubiquitous early meiotic motif, URS1 (upstream repression sequence 1), and a novel ancillary repression element. The ancillary repression element is required for efficient vegetative repression, is spatially separable from URS1, and continues to facilitate repression during sporulation. In contrast, URS1 also functions as a vegetative repression element but is converted early in meiosis into an HSE-dependent activation element. An early step in this transformation may be the antagonism of URS1-mediated repression by IME1. The HSE also nonspecifically supports a second major mode of meiotic activation that does not require URS1 but does require expression of IME2 and concurrent starvation. Interestingly, increased rather than decreased URS1-mediated vegetative transcription can be artificially achieved by introducing rare point mutations into URS1 or by deleting the UME6 gene. These lesions offer insight into mechanisms of URS-dependent repression and activation. Experiments suggest that URS1-bound factors functionally modulate heat shock factor during vegetative transcription and early meiotic induction but not during heat shock. The loss of repression and activation observed when the IME2 activation element, T 4 C, is substituted for the HSE suggests specific requirements for URS1-upstream activation sequence interactions.

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Expression of HSP86 in male germ cells.

Cited by 53 publications

References 20 publications

Immunocytochemical observation of the 90 KD heat shock protein (HSP90): high expression in primordial and pre-meiotic germ cells of male and female rat gonads.

Immunocytochemical observation of the 90 KD heat shock protein (HSP90): high expression in primordial and pre-meiotic germ cells of male and female rat gonads.

Dynamic Hsp83 RNA localization during Drosophila oogenesis and embryogenesis.

A Bipartite Operator Interacts with a Heat Shock Element To Mediate Early Meiotic Induction of Saccharomyces cerevisiae HSP82

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