Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum

Meyer, Christiane; Schmid, Roland; Schmieding, Kerstin; Falkenstein, Elisabeth; Wehling, Martin

doi:10.1016/s0039-128x(97)00143-8

Cited by 46 publications

(33 citation statements)

References 25 publications

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“…This is consistent with PGRMC1 western blots obtained from lysates of other organs and cell types such as porcine liver (Meyer et al 1998); human and rat granulosa and luteal cells (Engmann et al 2006; mouse and human smooth muscle, uterus, and placenta (Zhang et al 2008). This study also shows that PGRMC1 is present at the GV-and MII-stage oocytes and is associated with male and female pronucleus formation of the zygote and is highly expressed in blastocysts.…”

Section: Discussionsupporting

confidence: 86%

Progesterone receptor membrane component 1 expression and putative function in bovine oocyte maturation, fertilization, and early embryonic development

Luciano¹,

Lodde²,

Franciosi³

et al. 2010

Reproduction

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Although the mRNA that encodes progesterone receptor membrane component 1 (PGRMC1) is present in mammalian oocytes, nothing is known about either PGRMC1's expression pattern or function in oocytes during maturation, fertilization, and subsequent embryonic development. As PGRMC1 associates with the mitotic spindle in somatic cells, we hypothesized that PGRMC1 is involved in oocyte maturation (meiosis). Western blot analysis confirmed the presence of PGRMC1 in bovine oocytes. This study also shows that PGRMC1 is present at the germinal vesicle (GV)-and MII-stage oocytes and is associated with male and female pronucleus formation of the zygote and is highly expressed in blastocysts. A more detailed examination of PGRMC1 localization using confocal imaging demonstrated that in GV-stage oocytes, PGRMC1 was concentrated throughout the GV but did not localize to the chromatin. With the resumption of meiosis in vitro, PGRMC1 concentrated in the centromeric region of metaphase I chromosomes, while in the anaphase I/telophase I stages the majority of PGRMC1 concentrated between the separating chromosomes. At the metaphase II stage, PGRMC1 re-associated with the centromeric region of the chromosomes. A colocalization study demonstrated that PGRMC1 associated with the phosphorylated form of aurora kinase B, which localizes to the centromeres at metaphase. Finally, PGRMC1 antibody injection significantly lowered the percentage of oocytes that matured and reached the metaphase II stage after 24 h of culture. The majority of the PGRMC1 antibodyinjected oocytes arrested in the prometaphase I stage of meiosis. Furthermore, in most of the PGRMC1 antibody-injected oocytes, the chromosomes were disorganized and scattered. Taken together, these data demonstrate that PGRMC1 is expressed in bovine oocytes and its localization changes at specific stages of oocyte maturation. These observations suggest an important role for PGRMC1 in oocyte maturation, which may be specifically related to the mechanism by which chromosomes segregate.

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Section: Discussionsupporting

confidence: 86%

Progesterone receptor membrane component 1 expression and putative function in bovine oocyte maturation, fertilization, and early embryonic development

Luciano¹,

Lodde²,

Franciosi³

et al. 2010

Reproduction

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“…Some examples of such nongenomic progesterone action include facilitation of female mouse sexual behavior (Frye & Vongher 1999), oocyte maturation in Xenopus (Masui & Markert 1971), and spotted sea trout (Zhu et al 2003b), as well as the acrosome reaction in sperm (Meizel & Turner 1991). Putative mPRs have been identified in tissues such as human sperm (Luconi et al 1998, rat brain (Krebs et al 2000), rat granulosa cells (Peluso et al 2004), porcine liver (Meyer et al 1996), human liver, kidney, and placenta (Meyer et al 1998). Members of the mPR family described in this study have previously been identified in fish oocytes (Zhu et al 2003b), fish sperm (Thomas et al 2005b), various human tissues (Zhu et al 2003a, Chapman et al 2006, Karteris et al 2006, Dressing & Thomas 2007, Nutu et al 2007, rat corpus luteum (Cai & Stocco 2005), and sheep ovary (Ashley et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Expression of membrane progesterone receptors on human T lymphocytes and Jurkat cells and activation of G-proteins by progesterone

Dosiou¹,

Hamilton²,

Pang³

et al. 2007

Journal of Endocrinology

172

131

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“…Also there are several other proteins which are postulated to be potential mPRs detected by different antibodies. Most importantly, Meyer et al (1998) and Falkenstein et al (1999) reported that 28 and 56 kDa proteins, which do not share the classic hormone-binding domain with the genomic progesterone receptor, are detected by the ProgPep antibody raised against the N-terminus of porcine liver mPR. Interestingly, as reported for mAb C-262 by Sabeur et al (1996), ProgRek, raised against the recombinant porcine liver mPR expressed in E. coli fused with an N-terminal His-tag, inhibited the progesterone-induced Ca 2+ increase (Falkenstein et al 1999).…”

Section: Discussionmentioning

confidence: 99%

Identification of a 71 kDa protein as a putative non-genomic membrane progesterone receptor in boar spermatozoa

Jang¹,

Yi²

2005

Journal of Endocrinology

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A putative non-genomic progesterone receptor was identified by Western blot analysis from the membrane fraction but not the cytosolic fraction of boar spermatozoa using monoclonal antibody (mAb) C-262. When the membrane and the cytosolic fractions of boar liver, kidney, uterus and spermatozoa were analyzed with mAb C-262, protein bands with molecular masses of 86 and 120 kDa were detected from the cytosolic fraction of the uterus, whereas a 71 kDa protein was detected from the membrane fraction of spermatozoa. Apparently, while the 86 and 120 kDa proteins from the uterus correspond to the genomic progesterone receptor isoforms A and B in boar, the 71 kDa protein of the sperm membrane fraction seems to be a novel membrane-associated progesterone receptor. Ligand blot assay of the membrane and the cytosolic fractions of boar spermatozoa performed with peroxidaseconjugated progesterone revealed that only the 71 kDa membrane protein binds specifically to progesterone, reinforcing the results obtained from the Western blot analysis. Also ligand blot assays performed in the presence of mAb C-262 demonstrated that mAb C-262 inhibited progesterone binding to the 71 kDa protein in a dosedependent manner. Ligand blot assays performed in the presence of free progesterone, RU486 or estrogen revealed that binding of peroxidase-conjugated progesterone to the 71 kDa protein was inhibited by free progesterone and RU486 in a dose-dependent manner but not by estrogen, which further confirms that progesterone binds to the 71 kDa protein specifically. Furthermore, the progesterone-induced acrosome reaction was inhibited by mAb C-262 in a dose-dependent manner. These results strongly imply that spermatozoa possess a progesterone receptor in a membrane-bound form and can be influenced by progesterone via non-genomic progesterone receptor.

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Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum

Cited by 46 publications

References 25 publications

Progesterone receptor membrane component 1 expression and putative function in bovine oocyte maturation, fertilization, and early embryonic development

Progesterone receptor membrane component 1 expression and putative function in bovine oocyte maturation, fertilization, and early embryonic development

Expression of membrane progesterone receptors on human T lymphocytes and Jurkat cells and activation of G-proteins by progesterone

Identification of a 71 kDa protein as a putative non-genomic membrane progesterone receptor in boar spermatozoa

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