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<div class="pre-content"><div><div class="bk_prnt"><p class="small">NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.</p><p>Molecular Imaging and Contrast Agent Database (MICAD) [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013. </p></div><div class="iconblock clearfix whole_rhythm no_top_margin bk_noprnt"><a class="img_link icnblk_img" title="Table of Contents Page" href="/books/n/micad/"><img class="source-thumb" src="/corehtml/pmc/pmcgifs/bookshelf/thumbs/th-micad-lrg.png" alt="Cover of Molecular Imaging and Contrast Agent Database (MICAD)" height="100px" width="80px" /></a><div class="icnblk_cntnt eight_col"><h2>Molecular Imaging and Contrast Agent Database (MICAD) [Internet].</h2><a data-jig="ncbitoggler" href="#__NBK23068_dtls__">Show details</a><div style="display:none" class="ui-widget" id="__NBK23068_dtls__"><div>Bethesda (MD): <a href="https://www.ncbi.nlm.nih.gov/" ref="pagearea=page-banner&targetsite=external&targetcat=link&targettype=publisher">National Center for Biotechnology Information (US)</a>; 2004-2013.</div></div><div class="half_rhythm"><ul class="inline_list"><li style="margin-right:1em"><a class="bk_cntns" href="/books/n/micad/">Contents</a></li></ul></div><div class="bk_noprnt"><form method="get" action="/books/n/micad/" id="bk_srch"><div class="bk_search"><label for="bk_term" class="offscreen_noflow">Search term</label><input type="text" title="Search this book" id="bk_term" name="term" value="" data-jig="ncbiclearbutton" /> <input type="submit" class="jig-ncbibutton" value="Search this book" submit="false" style="padding: 0.1em 0.4em;" /></div></form></div></div><div class="icnblk_cntnt two_col"><div class="pagination bk_noprnt"><a class="active page_link prev" href="/books/n/micad/AA11C/" title="Previous page in this title">< Prev</a><a class="active page_link next" href="/books/n/micad/MP4B11C/" title="Next page in this title">Next ></a></div></div></div></div></div>
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<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK23068_"><span class="title" itemprop="name">1-[<sup>11</sup>C]Methylpiperidin-4-yl propionate</span></h1><div itemprop="alternativeHeadline" class="subtitle whole_rhythm">[<sup>11</sup>C]PMP</div><p class="contrib-group"><span itemprop="author">Kam Leung</span>, PhD.</p><a data-jig="ncbitoggler" href="#__NBK23068_ai__" style="border:0;text-decoration:none">Author Information and Affiliations</a><div style="display:none" class="ui-widget" id="__NBK23068_ai__"><div class="contrib half_rhythm"><span itemprop="author">Kam Leung</span>, PhD<div class="affiliation small">National for Biotechnology Information, NLM, NIH, Bethesda, MD<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="vog.hin.mln.ibcn@dacim" class="oemail">vog.hin.mln.ibcn@dacim</a></div></div><div class="small">Corresponding author.</div></div></div><p class="small">Created: <span itemprop="datePublished">May 1, 2006</span>; Last Update: <span itemprop="dateModified">February 28, 2012</span>.</p></div><div class="jig-ncbiinpagenav body-content whole_rhythm" data-jigconfig="allHeadingLevels: ['h2'],smoothScroll: false" itemprop="text"><div id="PMP11C.T.nc_chemical_name111cmethylpiper" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK23068/table/PMP11C.T.nc_chemical_name111cmethylpiper/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__PMP11C.T.nc_chemical_name111cmethylpiper_lrgtbl__"><table><tbody><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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||
<b>Chemical name:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">1-[<sup>11</sup>C]Methylpiperidin-4-yl propionate</td><td rowspan="9" colspan="1" style="text-align:center;vertical-align:middle;">
|
||
<a href="https://pubchem.ncbi.nlm.nih.gov/substance/11110529" title="View this structure in PubChem" class="img_link" ref="pagearea=body&targetsite=entrez&targetcat=link&targettype=pubchem"><img src="https://pubchem.ncbi.nlm.nih.gov/image/imgsrv.fcgi?t=l&sid=11110529" alt="image 11110529 in the ncbi pubchem database" /></a>
|
||
</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Abbreviated name:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">[<sup>11</sup>C]PMP</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Synonym:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">[<sup>11</sup>C]MP4P</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Agent category:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Compound</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Target:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Acetylcholinesterase (AChE)</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Target category:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Enzyme</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Method of detection:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">PET</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Source of signal:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"><sup>11</sup>C</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Activation:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">No</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
|
||
<b>Studies:</b>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">
|
||
<ul class="simple-list"><li class="half_rhythm"><div>
|
||
<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" />
|
||
<i>In vitro</i>
|
||
|
||
</div></li><li class="half_rhythm"><div>
|
||
<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Rodents
|
||
</div></li><li class="half_rhythm"><div>
|
||
<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Non-Human Primates
|
||
</div></li><li class="half_rhythm"><div>
|
||
<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Humans
|
||
</div></li></ul>
|
||
</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Click on the above structure for additional information in <a href="http://pubchem.ncbi.nlm.nih.gov/" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubChem</a>.</td></tr></tbody></table></div></div><div id="PMP11C.Background"><h2 id="_PMP11C_Background_">Background</h2><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=11C%20PMP" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Acetylcholine is an endogenous neurotransmitter at cholinergic synapses and neuroeffector junctions in the peripheral and central nervous systems. It acts on nicotinic and muscarinic receptors to mediate complex functions, such as attention, memory, cognition, and consciousness. Degeneration of cholinergic neurons has been observed in several neurodegenerative disease, such as Alzheimer’s disease (AD) and Parkinson’s disease (PD), but not in vascular dementia. Acetylcholinesterase (AChE) is the enzyme that terminates cholinergic actions through the rapid hydrolysis of acetylcholine to choline and acetate. AChE is localized on both cholinergic and cholinoceptive neurons in the brain with the highest activity in the striatum, followed by the cerebellum, thalamus, and cerebral cortex (<a class="bk_pop" href="#PMP11C.REF.1">1</a>). AChE has been a target for radioligand development as well as drug development because its levels decrease in AD (<a class="bk_pop" href="#PMP11C.REF.1" data-bk-pop-others="PMP11C.REF.2">1, 2</a>).</p><p>For measurements of AChE activity, various labeled esters of 1-methy-4-hydroxypiperidine have been designed and evaluated as acetylcholine substrate analogs (<a class="bk_pop" href="#PMP11C.REF.3">3</a>). Two of them, <i>N</i>-[<sup>11</sup>C]methylpiperidin-4-yl acetate (<a href="/books/n/micad/MP4A11C/">[<sup>11</sup>C]MP4A</a>) and 1-[<sup>11</sup>C]methylpiperidin-4-yl propionate ([11C]PMP), were chosen for further development as radioligands for use in positron emission tomography (PET). Each has a tertiary amine structure that makes it lipophilic; thus, it readily crosses the blood-brain barrier (BBB). [<sup>11</sup>C]PMP is specifically hydrolyzed by AChE (86-95% specificity) and yields a hydrophilic metabolite, <i>N</i>-[<sup>11</sup>C]methylpiperidinol ([<sup>11</sup>C]MP4OH), which is trapped in the brain because it cannot cross the BBB. The hydrolysis rate of MP4P is 3- to 4-fold slower than that of MP4A in rat and human brain homogenates (<a class="bk_pop" href="#PMP11C.REF.1">1</a>), thus allowing more precise estimates of AChE activity in regions of moderate to high AChE levels. [<sup>11</sup>C]PMP is being developed as a PET agent for the non-invasive study of brain AChE activity in patients with AD and PD.</p><div id="PMP11C.Related_Resource_Links"><h3>Related Resource Links</h3><ul><li class="half_rhythm"><div>Chapters in MICAD (<a href="/sites/entrez?db=Books&cmd=Search&term=acetylcholinesterase++AND+micad%5bbook%5d&doptcmdl=TOCView&log%24=booksrch&bname=micad" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">AChE</a>)</div></li><li class="half_rhythm"><div>Gene information in NCBI (<a href="/sites/entrez?Db=gene&Cmd=retrieve&dopt=full_report&list_uids=43&log$=genesensor5&logdbfrom=protein" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">AChE</a>).</div></li><li class="half_rhythm"><div>Articles in Online Mendelian Inheritance in Man (OMIM) (<a href="http://omim.org/entry/100740" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">AChE</a>)</div></li><li class="half_rhythm"><div>Clinical trials (<a href="http://www.clinicaltrials.gov/ct2/results?term=acetylcholinesterase" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">AChE</a>)</div></li><li class="half_rhythm"><div>Drug information in FDA (<a href="http://google-test.fda.gov/search?q=Acetylcholinesterase+inhibitor&client=FDAgov&site=FDAgov&lr=&proxystylesheet=FDAgov&output=xml_no_dtd&getfields=*&x=15&y=12" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">AChE</a>)</div></li></ul></div></div><div id="PMP11C.Synthesis"><h2 id="_PMP11C_Synthesis_">Synthesis</h2><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=11C%20PMP%20and%20synthesis" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Snyder et al. (<a class="bk_pop" href="#PMP11C.REF.4">4</a>) reported synthesis of [<sup>11</sup>C]PMP by direct N-methylation of 4-piperidinyl propionate with [<sup>11</sup>C]methyl trifluoromethanesulfonate at room temperature in dimethylformamide, with a radiochemical yield of 57% (end of synthesis) after high-performance liquid chromatography purification. Radiochemical purities were >99% with a specific activity of 41 GBq/mmol (1,500 Ci/mmol) and a total synthesis time of ~35 min.</p></div><div id="PMP11C.In_Vitro_Studies_Testing_in_Cells"><h2 id="_PMP11C_In_Vitro_Studies_Testing_in_Cells_">In Vitro Studies: Testing in Cells and Tissues</h2><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=%2811C%20PMP%29%20and%20in%20vitro" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Shinotoh et al. (<a class="bk_pop" href="#PMP11C.REF.1">1</a>) reported that PMP was rapidly hydrolyzed to MP4OH and propanoic acid by rat and human brain homogenates with 95 and 86% specificity for AChE, respectively. The hydrolysis rate in human cerebral cortex (0.042 fraction/min/g/ml) is about 10% that in rat cerebral cortex (0.39 fraction/min/g/ml).</p></div><div id="PMP11C.Animal_Studies"><h2 id="_PMP11C_Animal_Studies_">Animal Studies</h2><div id="PMP11C.Rodents"><h3>Rodents</h3><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=11C%20PMP%20and%20rodentia" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Kilbourn et al. (<a class="bk_pop" href="#PMP11C.REF.5">5</a>) reported that 2 min after injection in mice, [<sup>11</sup>C]PMP showed rapid accumulation in the brain and a regional retention of radioactivity in the striatum (12.9 ± 0.86% of injected dose (ID)/g), cortex (10.9 ± 1.31% ID/g), hippocampus (10.5 ± 1.33% ID/g), thalamus (9.53 ± 1.1% ID/g), hypothalamus (8.67 ± 1.48% ID/g), and cerebellum (7.01 ± 0.97% ID/g), reflecting known levels of AChE activity in the rodent brain. More than 95% of radioactivity in the brain was the hydrolytic metabolite, [<sup>11</sup>C]MP4OH. There was a gradual washout in all regions with time (up to 30 min). At 10 min after injection, the striatum/cerebellum, cortex/cerebellum, and striatum/cortex ratios were 3.06 ± 0.31, 1.1.79 ± 0.15, and 1.71 ± 0.19, respectively. On the other hand, for [<sup>11</sup>C]MP4A, the striatum/cerebellum, cortex/cerebellum, and striatum/cortex ratios were 1.81 ± 0.20, 1.64 ± 0.12, and 1.09 ± 0.08, respectively. Therefore, [<sup>11</sup>C]PMP seems to be better for discrimination among regions of high, intermediate, and low AChE activity. Retention of [<sup>11</sup>C]PMP radioactivity in all regions was reduced by pretreatment with 3 mg/kg diisopropylfluorophosphate (DFP), a specific irreversible AChE inhibitor. DFP pretreatment also significantly increased the proportions of intact ester in both blood and brain. Using PET scans, Shao et al. (<a class="bk_pop" href="#PMP11C.REF.6">6</a>) estimated [<sup>11</sup>C]PMP hydrolysis rate constant (<i>k</i><sub>3</sub>) values for the striatum and cortex to be 0.1009/min and 0.0453/min, respectively.</p></div><div id="PMP11C.Other_NonPrimate_Mammals"><h3>Other Non-Primate Mammals</h3><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=11C%20PMP%20and%20%28pig%20or%20dog%20or%20sheep%20or%20rabbit%29" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publication is currently available.</p></div><div id="PMP11C.NonHuman_Primates"><h3>Non-Human Primates</h3><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=11C%20PMP%20and%20%28primate%20not%20human%29" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Kilbourn et al. (<a class="bk_pop" href="#PMP11C.REF.5">5</a>) performed [<sup>11</sup>C]PMP PET studies in one monkey and found rapid accumulation in the brain within minutes after injection. About 15% and 50% of the initial high uptake in the striatum and cortex, respectively, was washed out in the initial 15 min and then remained constant with a maximal striatum/cortex ratio of 2.25, compared with 1.8 with [<sup>11</sup>C]MP4A.</p></div></div><div id="PMP11C.Human_Studies"><h2 id="_PMP11C_Human_Studies_">Human Studies</h2><p>[<a href="/entrez/query.fcgi?cmd=PureSearch&db=pubmed&details_term=11C%20PMP%20and%20human" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Kinetic analysis of [<sup>11</sup>C]PMP for measurement of cerebral AChE activity has been performed with and without arterial blood sampling (<a class="bk_pop" href="#PMP11C.REF.7" data-bk-pop-others="PMP11C.REF.8">7, 8</a>). A three-compartment model with three parameters was used to measure AChE hydrolysis of the tracer (<i>k</i><sub>3</sub>), the transport rate constant of the tracer from the blood to the brain through the BBB (<i>K</i><sub>1</sub>), and the transport rate constant of the tracer from the brain to the blood through the BBB (<i>k</i><sub>2</sub>). Kuhl et al. (<a class="bk_pop" href="#PMP11C.REF.9">9</a>) studied 26 healthy controls and 14 patients with AD who had no dementia; the authors used [<sup>11</sup>C]PMP PET, 2-[<sup>18</sup>F]fluoro-2-deoxy-D-glucose (<a href="/books/n/micad/FDG/">FDG</a>), and 5-[<sup>123</sup>I]iodobenzovesamicol ([<sup>123</sup>I]IBVM) for AChE activity, glucose metabolism, and vesicular acetylcholine transporter activity, respectively. The highest uptake was in the striatum, followed by the cerebellum, pons, thalamus, occipital cortex, temporal cortex, and frontal cortex. The estimated AChE distribution in the brain of the control subjects agreed with the AChE distribution at biopsies reported by others (<a class="bk_pop" href="#PMP11C.REF.10" data-bk-pop-others="PMP11C.REF.11">10, 11</a>). There was a 30% reduction of AChE activity in the cerebral cortex of the AD patients compared with the controls. Treatment with physostigmine (an AChE inhibitor) produced little effect on the [<sup>11</sup>C]PMP <i>K</i><sub>1</sub> in the controls. In contrast, there were significant decreases in the [<sup>11</sup>C]PMP <i>k</i><sub>3</sub> of all brain regions. There was a 15% decrease in cortical [<sup>11</sup>C]PMP <i>K</i><sub>1</sub> in elderly controls compared with young controls. However, there was no correlation of [<sup>11</sup>C]PMP <i>k</i><sub>3</sub> values with age and gender. In 11 AD patients, [<sup>11</sup>C]PMP <i>k</i><sub>3</sub> correlated significantly with [<sup>123</sup>I]IBVM binding, but neither the [<sup>11</sup>C]PMP <i>k</i><sub>3</sub> nor [<sup>123</sup>I]IBVM binding correlated with FDG uptake. After treatment with donepezil (an AChE inhibitor), cerebral cortical [<sup>11</sup>C]PMP <i>k</i><sub>3</sub> inhibition in AD brain averaged 27% in 6 patients (<a class="bk_pop" href="#PMP11C.REF.12">12</a>).</p><p>Marshall et al. (<a class="bk_pop" href="#PMP11C.REF.13">13</a>) studied the relationship between the severity of white matter hyperintensity (WMH) and cortical AChE activity in 11 patients with parkinsonian dementia (PDem) and 14 control subjects. [<sup>11</sup>C]PMP <i>k</i><sub>3</sub> values were significantly reduced (–20%; <i>P</i>< 0.001) in the cortex of PDem patients (0.0185 ± 0.0019/min) compared with the controls (0.0231 ± 0.0026/min). PDem subjects had higher mean severity of WMH (+20.1%) compared with control subjects (<i>P</i> < 0.05). However, there was no significant correlation of cortical [<sup>11</sup>C]PMP AChE activity with WMH severity. Bohnen et al. (<a class="bk_pop" href="#PMP11C.REF.14">14</a>) found that [<sup>11</sup>C]PMP AChE activity was significantly reduced (–11%; <i>P</i> < 0.05) in the cortex in patients with mild to moderate AD (0.0201 ± 0.0018/min; <i>n</i> = 15) compared with 12 normal controls (0.0226 ± 0.0023/min). Cortical [<sup>11</sup>C]PMP AChE activity was more robustly associated with functions of attention and working memory (<i>P</i> = 0.01) than with performance on primary memory tests in AD.</p><p>Internal dosimetry data for [<sup>11</sup>C]PMP in humans are not yet available in the literature</p></div><div id="PMP11C.References"><h2 id="_PMP11C_References_">References</h2><dl class="temp-labeled-list"><dt>1.</dt><dd><div class="bk_ref" id="PMP11C.REF.1">Shinotoh H., Fukushi K., Nagatsuka S., Irie T.
|
||
<em>Acetylcholinesterase imaging: its use in therapy evaluation and drug design.</em>
|
||
<span><span class="ref-journal">Curr Pharm Des. </span>2004;<span class="ref-vol">10</span>(13):1505–17.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15134572" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15134572</span></a>]</div></dd><dt>2.</dt><dd><div class="bk_ref" id="PMP11C.REF.2">Herholz K.
|
||
<em>PET studies in dementia.</em>
|
||
<span><span class="ref-journal">Ann Nucl Med. </span>2003;<span class="ref-vol">17</span>(2):79–89.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12790355" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12790355</span></a>]</div></dd><dt>3.</dt><dd><div class="bk_ref" id="PMP11C.REF.3">Irie T., Fukushi K., Akimoto Y., Tamagami H., Nozaki T.
|
||
<em>Design and evaluation of radioactive acetylcholine analogs for mapping brain acetylcholinesterase (AchE) in vivo.</em>
|
||
<span><span class="ref-journal">Nucl Med Biol. </span>1994;<span class="ref-vol">21</span>(6):801–8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/9234329" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 9234329</span></a>]</div></dd><dt>4.</dt><dd><div class="bk_ref" id="PMP11C.REF.4">Snyder S.E., Tluczek L., Jewett D.M., Nguyen T.B., Kuhl D.E., Kilbourn M.R.
|
||
<em>Synthesis of 1-[11C]methylpiperidin-4-yl propionate ([11C]PMP) for in vivo measurements of acetylcholinesterase activity.</em>
|
||
<span><span class="ref-journal">Nucl Med Biol. </span>1998;<span class="ref-vol">25</span>(8):751–4.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/9863562" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 9863562</span></a>]</div></dd><dt>5.</dt><dd><div class="bk_ref" id="PMP11C.REF.5">Kilbourn M.R., Snyder S.E., Sherman P.S., Kuhl D.E.
|
||
<em>In vivo studies of acetylcholinesterase activity using a labeled substrate, N-[11C]methylpiperdin-4-yl propionate ([11C]PMP).</em>
|
||
<span><span class="ref-journal">Synapse. </span>1996;<span class="ref-vol">22</span>(2):123–31.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/8787128" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8787128</span></a>]</div></dd><dt>6.</dt><dd><div class="bk_ref" id="PMP11C.REF.6">Shao X., Koeppe R.A., Butch E.R., Kilbourn M.R., Snyder S.E.
|
||
<em>Evaluation of 18F-labeled acetylcholinesterase substrates as PET radiotracers.</em>
|
||
<span><span class="ref-journal">Bioorg Med Chem. </span>2005;<span class="ref-vol">13</span>(3):869–75.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15653352" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15653352</span></a>]</div></dd><dt>7.</dt><dd><div class="bk_ref" id="PMP11C.REF.7">Koeppe R.A., Frey K.A., Snyder S.E., Meyer P., Kilbourn M.R., Kuhl D.E.
|
||
<em>Kinetic modeling of N-[11C]methylpiperidin-4-yl propionate: alternatives for analysis of an irreversible positron emission tomography trace for measurement of acetylcholinesterase activity in human brain.</em>
|
||
<span><span class="ref-journal">J Cereb Blood Flow Metab. </span>1999;<span class="ref-vol">19</span>(10):1150–63.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/10532640" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 10532640</span></a>]</div></dd><dt>8.</dt><dd><div class="bk_ref" id="PMP11C.REF.8">Sato K., Fukushi K., Shinotoh H., Nagatsuka S., Tanaka N., Aotsuka A., Ota T., Shiraishi T., Tanada S., Iyo M., Irie T.
|
||
<em>Evaluation of simplified kinetic analyses for measurement of brain acetylcholinesterase activity using N-[11C]Methylpiperidin-4-yl propionate and positron emission tomography.</em>
|
||
<span><span class="ref-journal">J Cereb Blood Flow Metab. </span>2004;<span class="ref-vol">24</span>(6):600–11.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15181367" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15181367</span></a>]</div></dd><dt>9.</dt><dd><div class="bk_ref" id="PMP11C.REF.9">Kuhl D.E., Koeppe R.A., Minoshima S., Snyder S.E., Ficaro E.P., Foster N.L., Frey K.A., Kilbourn M.R.
|
||
<em>In vivo mapping of cerebral acetylcholinesterase activity in aging and Alzheimer's disease.</em>
|
||
<span><span class="ref-journal">Neurology. </span>1999;<span class="ref-vol">52</span>(4):691–9.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/10078712" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 10078712</span></a>]</div></dd><dt>10.</dt><dd><div class="bk_ref" id="PMP11C.REF.10">Atack J.R., Perry E.K., Bonham J.R., Candy J.M., Perry R.H.
|
||
<em>Molecular forms of acetylcholinesterase and butyrylcholinesterase in the aged human central nervous system.</em>
|
||
<span><span class="ref-journal">J Neurochem. </span>1986;<span class="ref-vol">47</span>(1):263–77.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/3711902" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 3711902</span></a>]</div></dd><dt>11.</dt><dd><div class="bk_ref" id="PMP11C.REF.11">Reinikainen K.J., Riekkinen P.J., Paljarvi L., Soininen H., Helkala E.L., Jolkkonen J., Laakso M.
|
||
<em>Cholinergic deficit in Alzheimer's disease: a study based on CSF and autopsy data.</em>
|
||
<span><span class="ref-journal">Neurochem Res. </span>1988;<span class="ref-vol">13</span>(2):135–46.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/3362291" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 3362291</span></a>]</div></dd><dt>12.</dt><dd><div class="bk_ref" id="PMP11C.REF.12">Kuhl D.E., Minoshima S., Frey K.A., Foster N.L., Kilbourn M.R., Koeppe R.A.
|
||
<em>Limited donepezil inhibition of acetylcholinesterase measured with positron emission tomography in living Alzheimer cerebral cortex.</em>
|
||
<span><span class="ref-journal">Ann Neurol. </span>2000;<span class="ref-vol">48</span>(3):391–5.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/10976649" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 10976649</span></a>]</div></dd><dt>13.</dt><dd><div class="bk_ref" id="PMP11C.REF.13">Marshall G.A., Shchelchkov E., Kaufer D.I., Ivanco L.S., Bohnen N.I.
|
||
<em>White matter hyperintensities and cortical acetylcholinesterase activity in parkinsonian dementia.</em>
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<span><span class="ref-journal">Acta Neurol Scand. </span>2006;<span class="ref-vol">113</span>(2):87–91.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16411968" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16411968</span></a>]</div></dd><dt>14.</dt><dd><div class="bk_ref" id="PMP11C.REF.14">Bohnen N.I., Kaufer D.I., Hendrickson R., Ivanco L.S., Lopresti B., Davis J.G., Constantine G., Mathis C.A., Moore R.Y., DeKosky S.T.
|
||
<em>Cognitive correlates of alterations in acetylcholinesterase in Alzheimer's disease.</em>
|
||
<span><span class="ref-journal">Neurosci Lett. </span>2005;<span class="ref-vol">380</span>(1-2):127–32.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15854764" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15854764</span></a>]</div></dd></dl></div><div id="bk_toc_contnr"></div></div></div>
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<div xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"></div><div class="portlet"><div class="portlet_head"><div class="portlet_title"><h3><span>Views</span></h3></div><a name="Shutter" sid="1" href="#" class="portlet_shutter" title="Show/hide content" remembercollapsed="true" pgsec_name="PDF_download" id="Shutter"></a></div><div class="portlet_content"><ul xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" class="simple-list"><li><a href="/books/NBK23068/?report=reader">PubReader</a></li><li><a href="/books/NBK23068/?report=printable">Print View</a></li><li><a data-jig="ncbidialog" href="#_ncbi_dlg_citbx_NBK23068" data-jigconfig="width:400,modal:true">Cite this Page</a><div id="_ncbi_dlg_citbx_NBK23068" style="display:none" title="Cite this Page"><div class="bk_tt">Leung K. 1-[11C]Methylpiperidin-4-yl propionate. 2006 May 1 [Updated 2012 Feb 28]. In: Molecular Imaging and Contrast Agent Database (MICAD) [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013. <span class="bk_cite_avail"></span></div></div></li><li><a href="/books/NBK23068/pdf/Bookshelf_NBK23068.pdf">PDF version of this page</a> (140K)</li><li><a href="/books/n/micad/toc/bin/micad.csv">MICAD summary (CSV file)</a></li></ul></div></div><div class="portlet"><div class="portlet_head"><div class="portlet_title"><h3><span>In this page</span></h3></div><a name="Shutter" sid="1" href="#" class="portlet_shutter" title="Show/hide content" remembercollapsed="true" pgsec_name="page-toc" id="Shutter"></a></div><div class="portlet_content"><ul xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" class="simple-list"><li><a href="#PMP11C.Background" ref="log$=inpage&link_id=inpage">Background</a></li><li><a href="#PMP11C.Synthesis" ref="log$=inpage&link_id=inpage">Synthesis</a></li><li><a href="#PMP11C.In_Vitro_Studies_Testing_in_Cells" ref="log$=inpage&link_id=inpage">In Vitro Studies: Testing in Cells and Tissues</a></li><li><a href="#PMP11C.Animal_Studies" ref="log$=inpage&link_id=inpage">Animal Studies</a></li><li><a href="#PMP11C.Human_Studies" ref="log$=inpage&link_id=inpage">Human Studies</a></li><li><a href="#PMP11C.References" ref="log$=inpage&link_id=inpage">References</a></li></ul></div></div><div class="portlet"><div class="portlet_head"><div class="portlet_title"><h3><span>Search MICAD</span></h3></div><a name="Shutter" sid="1" href="#" class="portlet_shutter" title="Show/hide content" remembercollapsed="true" pgsec_name="source-application" id="Shutter"></a></div><div class="portlet_content"><form xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" name="frmSearch" method="get" action="/books/NBK5330/" id="frmSearch"><script type="text/javascript" src="/corehtml/pmc//js/bookshelf/micad.js">/**/</script><label class="offscreen_noflow" for="txtfield">Search term</label><input id="txtfield" type="text" name="f1_term" size="22" onKeyPress="KeyPress('micad',event,'/books/NBK5330/','')" /><button name="f1_search" type="submit">Go</button><button onclick="this.form.reset();" type="reset">Clear</button><p><b>Limit my Search:</b></p><div class="clearfix"><label for="detection">Method of detection:</label><div class="right"><select name="detection" id="detection" style="width:200px"><option value="" selected="selected">Any</option><option value="(MRI OR "Magnetic resonance imaging" OR MRS)">MRI</option><option value="Multimodal">Multimodal imaging</option><option value="Optical">Optical imaging</option><option value="PET">PET</option><option value="Photoacoustic">Photoacoustic imaging</option><option value="(SPECT OR planar)">SPECT</option><option value="Ultrasound">Ultrasound</option><option value="(x-ray OR ct)">X-ray, CT</option></select></div></div><div class="clearfix"><label for="signal">Source of signal/contrast:</label><div class="right"><select name="signal" id="signal" style="width:200px"><option value="" selected="selected">Any</option><optgroup label="MRI agents"><option value="(Copper OR Cu)">Copper</option><option value="(Europium OR Eu3+)">Europium</option><option value="(Fluorine OR 19F)">Fluorine</option><option value="(Gadolinium OR Gd3+)">Gadolinium</option><option value=""Hyperpolarized 13C"">Hyperpolarized 13C</option><option value=""Iron oxide"">Iron oxide</option><option value=""Nitroxide radicals"">Nitroxide radicals</option><option value="(Oxygen OR 17O)">Oxygen</option><option value="Thulium">Thulium</option></optgroup><optgroup label="Multimodal agents"><option value="((Gadolinium OR Gd3+) AND Optical)">Gadolinium and optical</option><option value="((Gadolinium OR Gd3+) AND (Gold OR Au))">Gadolinium and Gold</option><option value="("Iron oxide" AND (64Cu OR 124I OR 111In))">Iron oxide and
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