Identification and Expression of a New Sulfhydryl Oxidase SOx-3 during the Cell Cycle and the Estrus Cycle in Uterine Cells

Musard, Jean-François; Sallot, Myriam; Dulieu, Philippe; Fraîchard, Annick; Ordener, Catherine; Rémy-Martin, Jean-Paul; Jouvenot, Michèle; Adami, Pascale

doi:10.1006/bbrc.2001.5440

Cited by 35 publications

(39 citation statements)

References 30 publications

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“…Interestingly, QSOX members have been related to fundamental cellular mechanisms such as protein folding (Thorpe et al, 2002), regulation of the cellular redox state, control of cell cycle (Coppock et al, 1993(Coppock et al, , 2000Musard et al, 2001), and apoptosis (Wittke et al, 2003).…”

mentioning

confidence: 99%

Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain

Mairet-Coello

Tury

Fellmann

et al. 2005

J of Comparative Neurology

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The spatiotemporal pattern of distribution of the sulfhydryl oxidase QSOX throughout ontogeny was mapped in rat brain using immunohistochemistry. The enzyme was detected on embryonic day (E) 12 in the dawning mantle layer, but the adult-like pattern was acquired postnatally around day 30 (P30). Throughout ontogenesis, rQSOX was detected in immature and mature neurons, but not in glial cells. The rQSOX developmental pattern can be divided into four periods: on E12 the enzyme was detected in the brainstem, more precisely in motoneurons; later (E16), rQSOX-positive cells were also observed in the forebrain, in the caudoputamen, and the subventricular zone. During late embryogenesis (E18-20), the amount of rQSOX cells considerably increased throughout the brain; they initially appeared in the hippocampus, then in the isocortex. From birth onwards, complex modifications of the rQSOX distribution occurred leading to the adult pattern by P30. Although rQSOX exhibits an overall increasing spatiotemporal pattern of distribution, different expression strategies were distinguished depending on the cell type or brain area. By comparing the rQSOX ontogeny with data on neurogenesis and brain histogenesis, we hypothesize that the enzyme could play a role in guiding migrating cells, their settling, and neuronal maturation, e.g., during outgrowth and synaptogenesis.

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mentioning

confidence: 99%

Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain

Mairet-Coello

Tury

Fellmann

et al. 2005

J of Comparative Neurology

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“…The guinea-pig sulfhydryl oxidase SOx-3 was discovered by looking for estrogen-regulated genes and its levels of expression in the endometrium changed across the estrous cycle. Conversely to rQSOX in rat pituitary, SOx-3 expression in guinea-pig endometrium was lowered during the estrus phase and was supposed to be downregulated by estrogens (Musard et al 2001). Moreover, a screening of estrogen genomic effects has recently demonstrated that the human quiescin Q6 gene is repressed by estrogens in MCF-7 breast cancer cells (Inoue et al 2002).…”

Section: Effect Of Estrogens On Rqsox Expression In the Pituitarymentioning

confidence: 99%

“…QSOX proteins display a highly conserved structure with an N-terminal PDI (protein disulfide isomerase)-like thioredoxin domain and a Cterminal ERV1 (essential for respiration and vegetative growth)-like domain which contains the FAD-binding site and the redox-active CXXC motif (Coppock et al 1998). Among them, the most investigated are the human quiescin Q6, whose mRNA level is increased when lung fibroblasts enter reversible quiescence (Coppock et al 1993(Coppock et al , 1998, sulfhydryl oxidases from chicken egg white (Hoober et al 1996, 1999a, Hoober & Thorpe 1999, guinea-pig endometrial cells (SOx-3, Musard et al 2001), mouse epidermis (Matsuba et al 2002) and human neuroblastoma cells (SOXN, Wittke et al 2003). QSOX proteins catalyze the formation of disulfide bonds in peptides and proteins with reduction of molecular oxygen to hydrogen peroxide (H 2 O 2 ).…”

Section: Introductionmentioning

confidence: 99%

“…Effects of the estrogen status on these enzymes are not well documented yet. The SOx-3 and Q6 genes have been shown to be down-regulated by estrogens respectively in endometrial cells (Musard et al 2001) and MCF-7 breast cancer cells (Inoue et al 2002); but no investigations have been undertaken concerning estrogen effects on rQSOX expression. Estrogens are important physiological regulators of the secretory activity of the anterior pituitary lobe.…”

Section: Introductionmentioning

confidence: 99%

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QSOX sulfhydryl oxidase in rat adenohypophysis: localization and regulation by estrogens

Tury¹,

Mairet-Coello²,

Poncet³

et al. 2004

Journal of Endocrinology

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The expression of the rat quiescin sulfhydryl oxidase (rQSOX) and its putative regulation by estrogens were investigated in the adenohypophysis. Immunohistochemical observations revealed that rQSOX protein is abundantly expressed throughout the anterior lobe of the pituitary, and can be found in almost all the different cell populations. However, as shown by double immunohistochemistry, the cells displaying the strongest rQSOX labeling belong to a subset of gonadotrophs. Immunoelectron microscopy showed that, in adenohypophyseal cells, the protein is linked to the membranes of the rough endoplasmic reticulum, the Golgi apparatus and to dense-core secretory granules. These results are consistent with the secretion of the protein and its presumed role in the extracellular matrix. According to its sulfhydryl oxidase function, rQSOX could also participate in the intracellular folding of secreted proteins or hormones like LH and FSH and act as an endogenous redox modulator of hormonal secretion. A semiquantitative RT-PCR analysis of rQSOX level across the estrous cycle and the fact that chronic administration of 17 -estradiol to ovariectomized rats led to a sustained up-regulation of rQSOX in the pituitary suggest that rQSOX expression is controlled by sex hormone levels. Further investigations are needed in order to elucidate its precise roles in that gland and the mechanisms of its regulation.

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“…expression of adhesion molecules (von Lukowicz et al 2008), transcriptional regulation of cyclooxygenase-2 (Lin et al 2011), transforming growth factor-b1 (TGF-b1) receptor (Sterling et al 2006), syndecan-4 (Lacal et al 2009), NF-kB (Kauppinen et al 2013), SMAD3 (Huang et al 2011), sex determining region Y-Box-2 (Musard et al 2001) and E-cadherin (McPhee et al 2008), which are essential during embryo implantation (Nakamura et al 2004, San et al 2004, Jha et al 2006, Lin et al 2006, St-Louis et al 2010. Furthermore, cell differentiation, cell proliferation (Lei et al 2009, Kaloglu & Onarlioglu 2010, Macdonald et al 2011, Afshar et al 2012) and the tissue remodelling process also take place in the uterus (Fazleabas & Strakova 2002, Rosario et al 2003, Kaloglu & Onarlioglu 2010, and can be influenced by PARP1 (Pagano et al 2007, Kobayashi 2011.…”

Section: Introductionmentioning

confidence: 99%

PARP1 during embryo implantation and its upregulation by oestradiol in mice

Joshi¹,

Mahfooz²,

Maurya³

et al. 2014

Reproduction

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Pregnancy requires successful implantation of an embryo, which occurs during a restricted period defined as 'receptivity of the endometrium' and is influenced by the ovarian steroids progesterone and oestradiol. The role of poly(ADP-ribose)polymerase-1 (PARP1) in apoptosis is well established. However, it is also involved in cell differentiation, proliferation and tissue remodelling. Previous studies have described the presence of PARP in the uterus, but its exact role in embryo implantation is not yet elucidated. Hence, in this study, we studied the expression of PARP1 in the uterus during embryo implantation and decidualisation, and its regulation by ovarian steroids. Our results show upregulation of the native form of PARP1 (w116 kDa) in the cytosolic and nuclear compartments of implantation and non-implantation sites at day 5 (0500 h), followed by downregulation at day 5 (1000 h), during the embryo implantation period. The transcript level of Parp1 was also augmented during day 5 (0500 h). Inhibition of PARP1 activity by the drug EB-47 decreased the number of embryo implantation sites and blastocysts at day 5 (1000 h). Further, cleavage of native PARP1 was due to the activity of caspase-3 during the peri-implantation stage (day 5 (0500 h)), and is also required for embryo implantation, as inhibition of its activity compromised blastocyst implantation. The native (w116 kDa) and cleaved (w89 kDa) forms of PARP1 were both elevated during decidualisation of the uterus. Furthermore, the expression level of PARP1 in the uterus was found to be under the control of the hormone oestrogen. Our results clearly demonstrate that PARP1 participates in the process of embryo implantation.

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Identification and Expression of a New Sulfhydryl Oxidase SOx-3 during the Cell Cycle and the Estrus Cycle in Uterine Cells

Cited by 35 publications

References 30 publications

Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain

Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain

QSOX sulfhydryl oxidase in rat adenohypophysis: localization and regulation by estrogens

PARP1 during embryo implantation and its upregulation by oestradiol in mice

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