http://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&feed=atom&action=historyTeam:Tuebingen/Project/Receptor - Revision history2024-03-29T05:14:22ZRevision history for this page on the wikiMediaWiki 1.16.5http://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=282913&oldid=prevSvenB at 20:21, 3 October 20132013-10-03T20:21:40Z<p></p>
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</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=282905&oldid=prevSvenB at 20:21, 3 October 20132013-10-03T20:21:20Z<p></p>
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</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=280535&oldid=prevSvenB at 18:18, 3 October 20132013-10-03T18:18:59Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>The mPRs themselves are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we created by PCR of yeast DNA. The DNA-sequence of our Padh1 is identical to <a href="http://parts.igem.org/wiki/index.php?title=Part%3ABBa_J63005">BBa_J63005</a><del class="diffchange diffchange-inline">. However, BBa_J63005 is currently unavailable thus we had to create this part ourselves</del>.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>The mPRs themselves are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we created by PCR of yeast DNA. The DNA-sequence of our Padh1 is identical to <a href="http://parts.igem.org/wiki/index.php?title=Part%3ABBa_J63005">BBa_J63005</a>.</p></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=280451&oldid=prevSvenB at 18:13, 3 October 20132013-10-03T18:13:57Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>The mPRs themselves are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we created by PCR of yeast DNA. The DNA-sequence of our Padh1 is identical to <a href="http://parts.igem.org/wiki/index.php?title=Part%3ABBa_J63005">BBa_J63005</a>.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>The mPRs themselves are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we created by PCR of yeast DNA. The DNA-sequence of our Padh1 is identical to <a href="http://parts.igem.org/wiki/index.php?title=Part%3ABBa_J63005">BBa_J63005</a><ins class="diffchange diffchange-inline">. However, BBa_J63005 is currently unavailable thus we had to create this part ourselves</ins>.</p></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=280415&oldid=prevSvenB at 18:11, 3 October 20132013-10-03T18:11:32Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Kupchak et al. (2007) showed that yeast PAQR proteins repress a gene called FET3 in <i>S. cerevisiae</i>. Knowing this, Smith et al. (2008) used the expression of FET3 as a reporter for their study of human mPRs (which were heterologically expressed in yeast) and were able to show that these mPRs, too, repress FET3. Since both yeast and human PAQR proteins reliably repress FET3 we are confident that PAQR proteins from other species will interact with the FET3 promoter, too. In fact, Zhu et al. (2003) obtained evidence that teleost fishes (like <i>Danio rerio</i>) employ mPRs for the induction of oocyte meiotic maturation. Amphibians (like <i>Xenopus laevis</i>) use high-affinity mPRs for the induction of the same process (Liu and Patiño, 1993).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Kupchak et al. (2007) showed that yeast PAQR proteins repress a gene called FET3 in <i>S. cerevisiae</i>. Knowing this, Smith et al. (2008) used the expression of FET3 as a reporter for their study of human mPRs (which were heterologically expressed in yeast) and were able to show that these mPRs, too, repress FET3. Since both yeast and human PAQR proteins reliably repress FET3 we are confident that PAQR proteins from other species will interact with the FET3 promoter, too. In fact, Zhu et al. (2003) obtained evidence that teleost fishes (like <i>Danio rerio</i>) employ mPRs for the induction of oocyte meiotic maturation. Amphibians (like <i>Xenopus laevis</i>) use high-affinity mPRs for the induction of the same process (Liu and Patiño, 1993).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”<del class="diffchange diffchange-inline">. The mPRs are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we retrieved from the Registry</del>. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter<ins class="diffchange diffchange-inline">.</p> </ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> </div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins class="diffchange diffchange-inline"><p>The mPRs themselves are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we created by PCR of yeast DNA. The DNA-sequence of our Padh1 is identical to <a href="http://parts.igem.org/wiki/index.php?title=Part%3ABBa_J63005">BBa_J63005</a></ins>.</p></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=279335&oldid=prevSvenB at 17:06, 3 October 20132013-10-03T17:06:25Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Kupchak et al. (2007) showed that yeast PAQR proteins repress a gene called FET3 in <i>S. cerevisiae</i>. Knowing this, Smith et al. (2008) used the expression of FET3 as a reporter for their study of human mPRs (which were heterologically expressed in yeast) and were able to show that these mPRs, too, repress FET3. Since both yeast and human PAQR proteins reliably repress FET3 we are confident that PAQR proteins from other species will interact with the FET3 promoter, too. In fact, Zhu et al. (2003) obtained evidence that teleost fishes (like <i>Danio rerio</i>) employ mPRs for the induction of oocyte meiotic maturation. Amphibians (like <i>Xenopus laevis</i>) use high-affinity mPRs for the induction of the same process (Liu and Patiño, 1993).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Kupchak et al. (2007) showed that yeast PAQR proteins repress a gene called FET3 in <i>S. cerevisiae</i>. Knowing this, Smith et al. (2008) used the expression of FET3 as a reporter for their study of human mPRs (which were heterologically expressed in yeast) and were able to show that these mPRs, too, repress FET3. Since both yeast and human PAQR proteins reliably repress FET3 we are confident that PAQR proteins from other species will interact with the FET3 promoter, too. In fact, Zhu et al. (2003) obtained evidence that teleost fishes (like <i>Danio rerio</i>) employ mPRs for the induction of oocyte meiotic maturation. Amphibians (like <i>Xenopus laevis</i>) use high-affinity mPRs for the induction of the same process (Liu and Patiño, 1993).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>For our measurement system we decided to use membrane progestin receptors (mPR) of <i>Xenopus laevis</i> and <i>Danio rerio</i> as progestin detectors / “sniffers”<ins class="diffchange diffchange-inline">. The mPRs are regulated by the constitutive promoter of the ADH1 gene (Padh1), which we retrieved from the Registry</ins>. In the end when our system is ready for use we will analyze the properties of both mPRs (denoted mPR Xl and mPR Dr) and decide which one suits our needs best. Once progestin binds to the mPR the FET3 gene promoter (Pfet3) will be repressed by an endogenous signaling molecule from the PAQR-pathway of our chassis (<i>S. cerevisiae</i>). As a result the expression of downstream genes of Pfet3 will stop. In order to receive a positive feedback when progestin is detected we need to invert the receptor signal – therefore we have combined Pfet3 with a repressor that represses the promoter of our reporter.</p> </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Additional information: <br></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=277742&oldid=prevSvenB at 15:25, 3 October 20132013-10-03T15:25:51Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Secondly, currently unknown compound that can bind to the progestin receptor may have progestin-like effects in fish (see the relation between bisphenol A and estrogen receptors (Takayanagi et al., 2006, Gould et al., 1998, Okada et al., 2008) as an example for such reactions).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Secondly, currently unknown compound that can bind to the progestin receptor may have progestin-like effects in fish (see the relation between bisphenol A and estrogen receptors (Takayanagi et al., 2006, Gould et al., 1998, Okada et al., 2008) as an example for such reactions).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>We are using progesterone membrane receptors (mPR) that mediate nongenomic progesterone responses and belong to the progestin <del class="diffchange diffchange-inline">an </del>AdipoQ-Receptor (PAQR) family (Tang et al., 2005) as “progestin sniffers” for our measurement system. mPR seems to have G-protein coupled receptor (GPCR) characteristics though there are no other GPCRs in the PAQR family (Tang et al., 2005, Zhu et al., 2003).</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>We are using progesterone membrane receptors (mPR) that mediate nongenomic progesterone responses and belong to the progestin <ins class="diffchange diffchange-inline">and </ins>AdipoQ-Receptor (PAQR) family (Tang et al., 2005) as “progestin sniffers” for our measurement system. mPR seems to have G-protein coupled receptor (GPCR) characteristics though there are no other GPCRs in the PAQR family (Tang et al., 2005, Zhu et al., 2003).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Smith et al. (2008) were able to show that human mPRs can sense progesterone and structurally similar compounds like 17alpha-Hydroxyprogesterone at physiologically relevant concentrations, therefore we believe that other compounds that are related to progesterone can bind to mPRs as well. In their study on female <i>Xenopus laevis</i> Liu and Patiño (1993) found such a correlation between structural similarity and binding affinity.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Smith et al. (2008) were able to show that human mPRs can sense progesterone and structurally similar compounds like 17alpha-Hydroxyprogesterone at physiologically relevant concentrations, therefore we believe that other compounds that are related to progesterone can bind to mPRs as well. In their study on female <i>Xenopus laevis</i> Liu and Patiño (1993) found such a correlation between structural similarity and binding affinity.</p></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=272782&oldid=prevSvenB at 01:25, 3 October 20132013-10-03T01:25:02Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>Since we want to measure progestin concentrations (e.g. Kolodziej et al., 2003, also see Motivation) that have an effect on fish but usually do not harm humans (European Agency for the Evaluation of Medicinal Products, 1999) we decided to not use human progestin receptors (for a human cell derived measurement system see for example van der Linden et al., 2008) but rather the progestin receptors of fish for our progestin measurement system. This has some advantages:</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>Since we want to measure progestin concentrations (e.g. Kolodziej et al., 2003, also see <ins class="diffchange diffchange-inline"><a href="https://2013.igem.org/Team:Tuebingen/Project/</ins>Motivation<ins class="diffchange diffchange-inline">">Motivation</a></ins>) that have an effect on fish but usually do not harm humans (European Agency for the Evaluation of Medicinal Products, 1999) we decided to not use human progestin receptors (for a human cell derived measurement system see for example van der Linden et al., 2008) but rather the progestin receptors of fish for our progestin measurement system. This has some advantages:</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Firstly, any progestin concentration that can cause a reporter signal in our system might also affect fish in some way. In fact, we use exactly the progestin receptors that induce the oocyte meiotic maturation in fish and amphibia we mentioned in our project motivation (Zhu et al., 2003).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Firstly, any progestin concentration that can cause a reporter signal in our system might also affect fish in some way. In fact, we use exactly the progestin receptors that induce the oocyte meiotic maturation in fish and amphibia we mentioned in our project motivation (Zhu et al., 2003).</p></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Smith et al. (2008) were able to show that human mPRs can sense progesterone and structurally similar compounds like 17alpha-Hydroxyprogesterone at physiologically relevant concentrations, therefore we believe that other compounds that are related to progesterone can bind to mPRs as well. In their study on female <i>Xenopus laevis</i> Liu and Patiño (1993) found such a correlation between structural similarity and binding affinity.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Smith et al. (2008) were able to show that human mPRs can sense progesterone and structurally similar compounds like 17alpha-Hydroxyprogesterone at physiologically relevant concentrations, therefore we believe that other compounds that are related to progesterone can bind to mPRs as well. In their study on female <i>Xenopus laevis</i> Liu and Patiño (1993) found such a correlation between structural similarity and binding affinity.</p></div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>We chose <i>Saccharomyces cerevisiae</i> as chassis for our biological system due to the fact that yeast possesses endogenous receptors of the PAQR family (Lyons et al., 2004) thus the apparatus for the operation of receptors of that family should be available in these organisms. In fact, Kupchak et al. (2007) showed that many PAQR proteins are able to “activate similar intracellular signaling cascades, suggesting a conserved mechanism for signal transduction”. Also, <i>S. cerevisiae</i> does not use progesterone in its own metabolism and does not possess any progesterone receptors thus should not interfere with our measurement system (Smith et al., 2008). Furthermore <i>S. cerevisiae</i> is a rather well understood eukaryote organism and offers acceptable reproduction rates. We did not consider <del class="diffchange diffchange-inline">E. </del>coli since “it is not known if PAQR receptors function the same in this organism as they do in eukaryotes” (Smith et al., 2008). All in all, <i>S. cerevisiae</i> is an ideal chassis organism for our measurement system.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>We chose <i>Saccharomyces cerevisiae</i> as chassis for our biological system due to the fact that yeast possesses endogenous receptors of the PAQR family (Lyons et al., 2004) thus the apparatus for the operation of receptors of that family should be available in these organisms. In fact, Kupchak et al. (2007) showed that many PAQR proteins are able to “activate similar intracellular signaling cascades, suggesting a conserved mechanism for signal transduction”. Also, <i>S. cerevisiae</i> does not use progesterone in its own metabolism and does not possess any progesterone receptors thus should not interfere with our measurement system (Smith et al., 2008). Furthermore <i>S. cerevisiae</i> is a rather well understood eukaryote organism and offers acceptable reproduction rates. We did not consider <ins class="diffchange diffchange-inline"><i>Escherichia </ins>coli<ins class="diffchange diffchange-inline"></i> </ins>since “it is not known if PAQR receptors function the same in this organism as they do in eukaryotes” (Smith et al., 2008). All in all, <i>S. cerevisiae</i> is an ideal chassis organism for our measurement system.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Kupchak et al. (2007) showed that yeast PAQR proteins repress a gene called FET3 in <i>S. cerevisiae</i>. Knowing this, Smith et al. (2008) used the expression of FET3 as a reporter for their study of human mPRs (which were heterologically expressed in yeast) and were able to show that these mPRs, too, repress FET3. Since both yeast and human PAQR proteins reliably repress FET3 we are confident that PAQR proteins from other species will interact with the FET3 promoter, too. In fact, Zhu et al. (2003) obtained evidence that teleost fishes (like <i>Danio rerio</i>) employ mPRs for the induction of oocyte meiotic maturation. Amphibians (like <i>Xenopus laevis</i>) use high-affinity mPRs for the induction of the same process (Liu and Patiño, 1993).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Kupchak et al. (2007) showed that yeast PAQR proteins repress a gene called FET3 in <i>S. cerevisiae</i>. Knowing this, Smith et al. (2008) used the expression of FET3 as a reporter for their study of human mPRs (which were heterologically expressed in yeast) and were able to show that these mPRs, too, repress FET3. Since both yeast and human PAQR proteins reliably repress FET3 we are confident that PAQR proteins from other species will interact with the FET3 promoter, too. In fact, Zhu et al. (2003) obtained evidence that teleost fishes (like <i>Danio rerio</i>) employ mPRs for the induction of oocyte meiotic maturation. Amphibians (like <i>Xenopus laevis</i>) use high-affinity mPRs for the induction of the same process (Liu and Patiño, 1993).</p></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=272780&oldid=prevSvenB at 01:23, 3 October 20132013-10-03T01:23:45Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Secondly, currently unknown compound that can bind to the progestin receptor may have progestin-like effects in fish (see the relation between bisphenol A and estrogen receptors (Takayanagi et al., 2006, Gould et al., 1998, Okada et al., 2008) as an example for such reactions).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Secondly, currently unknown compound that can bind to the progestin receptor may have progestin-like effects in fish (see the relation between bisphenol A and estrogen receptors (Takayanagi et al., 2006, Gould et al., 1998, Okada et al., 2008) as an example for such reactions).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>We are using progesterone membrane receptors (mPR) that mediate nongenomic progesterone responses and belong to the progestin an AdipoQ-Receptor (PAQR) family (Tang et al., 2005) as “progestin sniffers” for our measurement system. mPR seems to have G-protein coupled receptor (GPCR) characteristics though there are no other GPCRs <del class="diffchange diffchange-inline">In </del>the PAQR family (Tang et al., 2005, Zhu et al., 2003)</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>We are using progesterone membrane receptors (mPR) that mediate nongenomic progesterone responses and belong to the progestin an AdipoQ-Receptor (PAQR) family (Tang et al., 2005) as “progestin sniffers” for our measurement system. mPR seems to have G-protein coupled receptor (GPCR) characteristics though there are no other GPCRs <ins class="diffchange diffchange-inline">in </ins>the PAQR family (Tang et al., 2005, Zhu et al., 2003)<ins class="diffchange diffchange-inline">.</ins></p></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Smith et al. (2008) were able to show that human mPRs can sense progesterone and structurally similar compounds like 17alpha-Hydroxyprogesterone at physiologically relevant concentrations, therefore we believe that other compounds that are related to progesterone can bind to mPRs as well. In their study on female <i>Xenopus laevis</i> Liu and Patiño (1993) found such a correlation between structural similarity and binding affinity.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Smith et al. (2008) were able to show that human mPRs can sense progesterone and structurally similar compounds like 17alpha-Hydroxyprogesterone at physiologically relevant concentrations, therefore we believe that other compounds that are related to progesterone can bind to mPRs as well. In their study on female <i>Xenopus laevis</i> Liu and Patiño (1993) found such a correlation between structural similarity and binding affinity.</p></div></td></tr>
</table>SvenBhttp://2013.igem.org/wiki/index.php?title=Team:Tuebingen/Project/Receptor&diff=272732&oldid=prevSvenB at 00:55, 3 October 20132013-10-03T00:55:46Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>ASKWITH, C., EIDE, D., VAN HO, A., BERNARD, P. S., LI, L., DAVIS-KAPLAN, S., SIPE, D. M. & KAPLAN, J. 1994. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell, 76, 403-410.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>ASKWITH, C., EIDE, D., VAN HO, A., BERNARD, P. S., LI, L., DAVIS-KAPLAN, S., SIPE, D. M. & KAPLAN, J. 1994. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell, 76, 403-410.</p></div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><p>EUROPEAN AGENCY FOR THE EVALUATION OF MEDICINAL PRODUCTS. 1999. Progesterone - Summary Report [Online]. London. Available: http://www.ema.europa.eu/docs/en_GB/document_library/Maximum_Residue_Limits_-_Report/2011/07/WC500108427.pdf.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><p>EUROPEAN AGENCY FOR THE EVALUATION OF MEDICINAL PRODUCTS. 1999. Progesterone - Summary Report [Online]. London. Available: <ins class="diffchange diffchange-inline"><a href="</ins>http://www.ema.europa.eu/docs/en_GB/document_library/Maximum_Residue_Limits_-_Report/2011/07/WC500108427.pdf<ins class="diffchange diffchange-inline">">http://www.ema.europa.eu/docs/en_GB/document_library/Maximum_Residue_Limits_-_Report/2011/07/WC500108427.pdf</a></ins>.</p></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>GOULD, J. C., LEONARD, L. S., MANESS, S. C., WAGNER, B. L., CONNER, K., ZACHAREWSKI, T., SAFE, S., MCDONNELL, D. P. & </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>GOULD, J. C., LEONARD, L. S., MANESS, S. C., WAGNER, B. L., CONNER, K., ZACHAREWSKI, T., SAFE, S., MCDONNELL, D. P. & </div></td></tr>
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