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<script type="text/javascript" src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.boots.min.js"> </script><title>TA138-conjugated 111In nanoparticles - Molecular Imaging and Contrast Agent Database (MICAD) - NCBI Bookshelf</title>
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<meta name="citation_title" content="TA138-conjugated 111In nanoparticles">
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<meta name="citation_date" content="2007/11/13">
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<meta name="citation_author" content="Arvind Chopra">
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<meta name="og:description" content="Integrins are a broad family of glycoprotein, transmembrane cell surface receptors that are formed by the association of an α and a β subunit. These receptors are involved in cell-matrix interactions and also play a role in cell signaling and migration (1, 2). Because of their role in cell migration, the αvβ3 integrin (that binds proteins such as vitronectin, fibronectin, thrombospondin, collagen, osteopontin, etc.) is a target of interest for the investigation of cancer metastasis and angiogenesis (3). Normally this receptor is expressed at low levels on epithelial and mature endothelial cells, but the expression is significantly upregulated during wound repair, cancer metastasis, and in neoplastic tumor vasculature (4-6). However, the exact role of αvβ3 integrin in angiogenesis is unclear because the inhibition of this receptor inhibits tumor angiogenesis, but knockout mice lacking the β3 integrins were shown to develop larger than normal and extremely vascularized tumors (7, 8).">
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yet</button><a id="jr-fip-next" class="wsprkl btn" title="Jump to next match">▶</a></nav></nav></div><div id="jr-epub-interstitial" class="hidden"></div><div id="jr-content"><article data-type="main"><div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><div class="fm-sec"><h1 id="_NBK23093_"><span class="title" itemprop="name">TA138-conjugated <sup>111</sup>In nanoparticles</span></h1><div itemprop="alternativeHeadline" class="subtitle whole_rhythm">α<sub>v</sub>β<sub>3</sub>-targeted <sup>111</sup>In/NP</div><p class="contribs">Chopra A.</p><p class="fm-aai"><a href="#_NBK23093_pubdet_">Publication Details</a></p></div></div><div class="jig-ncbiinpagenav body-content whole_rhythm" data-jigconfig="allHeadingLevels: ['h2'],smoothScroll: false" itemprop="text"><div class="iconblock whole_rhythm clearfix ten_col table-wrap" id="figIntegrinNP111InT1"><a href="/books/NBK23093/table/IntegrinNP111In.T1/?report=objectonly" target="object" title="Table" class="img_link icnblk_img" rid-ob="figobIntegrinNP111InT1"><img class="small-thumb" src="/corehtml/pmc/css/bookshelf/2.26/img/table-icon.gif" alt="Table Icon" /></a><div class="icnblk_cntnt"><h4 id="IntegrinNP111In.T1"><a href="/books/NBK23093/table/IntegrinNP111In.T1/?report=objectonly" target="object" rid-ob="figobIntegrinNP111InT1">Table</a></h4><p class="float-caption no_bottom_margin">
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<i>In vitro</i>
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Rodents
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</p></div></div><div id="IntegrinNP111In.Background"><h2 id="_IntegrinNP111In_Background_">Background</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=Integrin+targeted+111In+nanoparticles" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Integrins are a broad family of glycoprotein, transmembrane cell surface receptors that are formed by the association of an α and a β subunit. These receptors are involved in cell-matrix interactions and also play a role in cell signaling and migration (<a class="bibr" href="#IntegrinNP111In.EXTYLES.1" rid="IntegrinNP111In.EXTYLES.1">1</a>, <a class="bibr" href="#IntegrinNP111In.EXTYLES.2" rid="IntegrinNP111In.EXTYLES.2">2</a>). Because of their role in cell migration, the α<sub>v</sub>β<sub>3</sub> integrin (that binds proteins such as vitronectin, fibronectin, thrombospondin, collagen, osteopontin, etc.) is a target of interest for the investigation of cancer metastasis and angiogenesis (<a class="bibr" href="#IntegrinNP111In.EXTYLES.3" rid="IntegrinNP111In.EXTYLES.3">3</a>). Normally this receptor is expressed at low levels on epithelial and mature endothelial cells, but the expression is significantly upregulated during wound repair, cancer metastasis, and in neoplastic tumor vasculature (<a href="#IntegrinNP111In.EXTYLES.4">4-6</a>). However, the exact role of α<sub>v</sub>β<sub>3</sub> integrin in angiogenesis is unclear because the inhibition of this receptor inhibits tumor angiogenesis, but knockout mice lacking the β<sub>3</sub> integrins were shown to develop larger than normal and extremely vascularized tumors (<a class="bibr" href="#IntegrinNP111In.EXTYLES.7" rid="IntegrinNP111In.EXTYLES.7">7</a>, <a class="bibr" href="#IntegrinNP111In.EXTYLES.8" rid="IntegrinNP111In.EXTYLES.8">8</a>).</p><p>Visualization of small solid tumors has often helped in early detection of cancer and resulted in a favorable prognosis for the patient (<a class="bibr" href="#IntegrinNP111In.EXTYLES.9" rid="IntegrinNP111In.EXTYLES.9">9</a>). Using magnetic resonance imaging with nanoparticles (NP) that target the α<sub>v</sub>β<sub>3</sub> integrin, investigators have obtained high-resolution images of even minute tumors, but this technique requires knowledge of the exact location of the tumor to set up the equipment for imaging (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>). Although a variety of radiolabeled compounds such as peptides, antibodies, and other α<sub>v</sub>β<sub>3</sub> integrin antagonists have been used to visualize tumors in animals, these radiochemicals have limitations because of nonspecific binding (<a class="bibr" href="#IntegrinNP111In.EXTYLES.11" rid="IntegrinNP111In.EXTYLES.11">11</a>, <a class="bibr" href="#IntegrinNP111In.EXTYLES.12" rid="IntegrinNP111In.EXTYLES.12">12</a>). Perfluorocarbon NP was shown to biodistribute primarily to the reticuloendothelial organs (lungs, liver, and spleen), and Hu et al. investigated the use of these NP with a radionuclide payload to detect budding tumors and their vasculature in different regions of the body, including the brain, head, neck, prostate, and breasts (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>). The investigators developed an α<sub>v</sub>β<sub>3</sub> integrin anatagonist labeled with indium (<sup>111</sup>In) on a perfluorocarbon NP (α<sub>v</sub>β<sub>3</sub>-targeted <sup>111</sup>In/NP) and used the NP to visualize neoplastic tumor vasculature (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>). The α<sub>v</sub>β<sub>3</sub> integrin antagonist used to prepare the α<sub>v</sub>β<sub>3</sub>-targeted <sup>111</sup>In/NP was TA138 (known as 3-sulfon-<i>N</i>-[[4,7,10-tris(carboxymethyl)1,4,7,10-tetraaza-cyclododec-1-yl]acetyl]-L-alanyl-<i>N</i>-[2-[4-[[[(1S)-1-carboxy-2[[[1,4-dihydro-7-[(1<i>H</i>-imidazol-2-ylamino]methyl]-1-methyl-4-oxo-3-quinolinyl] carbonyl]amino]ethyl]amino]sulfonyl]-3,5-dimethylphenoxy]-1-oxobutyl]amino]ethyl]-3-sulfo-L-alaninamide) (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>).</p></div><div id="IntegrinNP111In.Synthesis"><h2 id="_IntegrinNP111In_Synthesis_">Synthesis</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=perfluorocarbon+nanoparticles+synthesis" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>The perfluorocarbon NP were produced as detailed by Hu et al. (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>). A mixture of perfluorooctylbromide (PFOB), a surfactant commixture, with glycerin and water was evaporated under reduced pressure and dried overnight at 50°C in a vacuum oven. The commixture consisted of lecithin, dipalmitoyl-L-α-ethanolamine, cholesterol, methoxy-1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid-caproyl-phosphatidylethanolamine and TA138 conjugated to polyethylene glycol 2000 dissolved in chloroform (<a href="#IntegrinNP111In.EXTYLES.13">13-15</a>). The dried mixture was then suspended in water by sonication to produce a liposomal suspension (<a class="bibr" href="#IntegrinNP111In.EXTYLES.14" rid="IntegrinNP111In.EXTYLES.14">14</a>). The liposomes were blended with PFOB and distilled, deionized water and emulsified at 20,000 psi for 4 minutes. The completed emulsion was aliquoted into a vial, sealed under nitrogen, and stored until use. The exact storage conditions were not provided in the publication. The NP size was determined with a laser light–scattering submicron particle size analyzer to be nominally 242 nm with a polydispersity index of 0.231 at 37°C (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>).</p><p>The synthesis of TA138 was described by Liu et al. (<a class="bibr" href="#IntegrinNP111In.EXTYLES.16" rid="IntegrinNP111In.EXTYLES.16">16</a>). For this, 2-{[(4-{3-[<i>N</i>-(2-{(2<i>R</i>)-2-[(2R)-3-sulfo-2-(2-{1,4,7,10-tetraaza-4,7,10-tris[(<i>tert</i>-butoxycarbonyl)methyl] cyclododecyl}acetylamino)propyl]-3-sulfopropyl}ethyl)carbamoyl]propoxy}-2,6-dimethylphenyl) sulfonyl]amino}(2<i>S</i>)-3-{[1-methyl-4-oxo-7-({[1-(triphenylmethyl)imidazol-2-yl]-amino}methyl)(3-hydroquinolyl)]carbonylamino}propanoic acid (DPC-AG1613) was dissolved in trifluoroacetic acid and triethylsilane, heated at 70°C under nitrogen for 60 min, and concentrated under vacuum to obtain an oily solid. The solid was partitioned between diethyl ether and aqueous acetonitrile (ACN). The ether layer was once again extracted with aqueous ACN, and the two aqueous extractions were pooled for freeze-drying to obtain crude TA138 (<a class="bibr" href="#IntegrinNP111In.EXTYLES.16" rid="IntegrinNP111In.EXTYLES.16">16</a>). Pure TA138 was obtained by several runs of the crude preparation on high-performance liquid chromatography using a Vydac C<sub>18</sub> pharmaceutical column. The salt was subsequently extracted in ACN and water and then freeze-dried to obtain pure TA138 as a fluffy solid (<a class="bibr" href="#IntegrinNP111In.EXTYLES.16" rid="IntegrinNP111In.EXTYLES.16">16</a>).</p><p>Coupling of <sup>111</sup>In to α<sub>v</sub>β<sub>3</sub> integrin–targeted perfluorocarbon NP was done at two different concentrations of the radionuclide (to produce particles with ~1 and ~10 radionuclides per NP, respectively), and it was achieved in citrate buffer (pH 5.7) (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>). Briefly, α<sub>v</sub>β<sub>3</sub> integrin–targeted perfluorocarbon NP was combined with [<sup>111</sup>In]indium chloride (in hydrochloric acid) in citrate buffer and incubated overnight at 40°C in a shaker water bath. The reaction was stopped by adding free diethylenetriamine pentaacetic acid for 5 min to remove all the free <sup>111</sup>In. Coupling efficiency was determined by thin-layer chromatography at room temperature. It ranged from 50% to 70% for the ~10 nuclides/NP and 85% to 90% for the ~1 nuclide/NP. The specific activity and radiochemical purity of the final product were not reported by the investigators (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>)</p></div><div id="IntegrinNP111In.In_Vitro_Studies_Tes"><h2 id="_IntegrinNP111In_In_Vitro_Studies_Tes_"><i>In Vitro</i> Studies: Testing in Cells and Tissues</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=%CE%B1v%CE%B23+integrin-targeted+perfluorocarbon+NP+in+vitro" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publications are currently available.</p></div><div id="IntegrinNP111In.Animal_Studies"><h2 id="_IntegrinNP111In_Animal_Studies_">Animal Studies</h2><div id="IntegrinNP111In.Rodents"><h3>Rodents</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=%CE%B1v%CE%B23+integrin-targeted+perfluorocarbon+NP+rodentia" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publications are currently available.</p></div><div id="IntegrinNP111In.Other_NonPrimate_Mam"><h3>Other Non-Primate Mammals</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=%CE%B1v%CE%B23+integrin-targeted+perfluorocarbon+NP+Non-Primate+Mammals" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Hu et al. investigated <i>in vivo</i> angiogenesis in 15 New Zealand rabbits bearing Vx-2 carcinoma tumors (<a class="bibr" href="#IntegrinNP111In.EXTYLES.10" rid="IntegrinNP111In.EXTYLES.10">10</a>). The rabbits were divided into five groups and administered the respective ~10 <sup>111</sup>In/NP α<sub>v</sub>β<sub>3</sub> integrin–targeted (<i>n</i> = 3) or the ~1 <sup>111</sup>In/NP α<sub>v</sub>β<sub>3</sub> integrin–targeted (<i>n</i> = 4) preparations. The control rabbits (<i>n</i> = 4) received non-targeted <sup>111</sup>In/NP, and for the competition study a group of animals (<i>n</i> = 4) received an excess of non-radioactive α<sub>v</sub>β<sub>3</sub>-targeted NP, along with α<sub>v</sub>β<sub>3</sub>-targeted ~10 <sup>111</sup>In/NP at a ratio of 3:1. The control animals received non-targeted NP as either ~10 <sup>111</sup>In/NP (<i>n</i> = 2) or ~1 <sup>111</sup>In/NP (<i>n</i> = 2). The animals were examined 18 and 48 h after administration to assess persistence of the label. From planar images it was clear that the tumor contrast in animals injected with the α<sub>v</sub>β<sub>3</sub>-targeted NP was higher than in animals injected with the non-targeted preparation. On average, animals injected with the targeted formulation had approximately four times higher (<i>P</i> < 0.05; 0.48 ± 0.05% of the injected dose (ID)) accumulation of radioactivity in the tumors compared to the animals that received the non-targeted dose (0.10 ± 0.06% ID).</p><p>Imaging of the tumor neovasculature was performed up to 2 h after administration of α<sub>v</sub>β<sub>3</sub>-targeted <sup>111</sup>In/NP bearing ~10 <sup>111</sup>In/NP and compared with animals receiving three-fold more unlabeled α<sub>v</sub>β<sub>3</sub>-targeted NP. During the 2-h period, the tumor/muscle ratio (TMR) of animals injected with the radiolabeled ligand averaged to 6.3 ± 0.2 compared with an average TMR of 4.1 ± 0.2 observed in animals injected with the unlabeled ligand. This difference was reported to persist over the entire 2 h of imaging. A similar difference and persistence in TMR was observed between animals that received the ~10 <sup>111</sup>In/NP and ~1 <sup>111</sup>In/NP α<sub>v</sub>β<sub>3</sub>-targeted doses.</p></div><div id="IntegrinNP111In.NonHuman_Primates"><h3>Non-Human Primates</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=%CE%B1v%CE%B23+integrin-targeted+perfluorocarbon+NP+Non-Human+Primates" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publications are currently available.</p></div></div><div id="IntegrinNP111In.Human_Studies"><h2 id="_IntegrinNP111In_Human_Studies_">Human Studies</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=%CE%B1v%CE%B23+integrin-targeted+perfluorocarbon+NP+Human" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publications are currently available.</p></div><div id="IntegrinNP111In.references"><h2 id="_IntegrinNP111In_references_">References</h2><dl class="temp-labeled-list"><dl class="bkr_refwrap"><dt>1.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.1">Chan K.T. , Cortesio C.L. , Huttenlocher A. Integrins in cell migration. <span><span class="ref-journal">Methods Enzymol. </span>2007;<span class="ref-vol">
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<strong>426</strong>
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</span>:47–67.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17697879" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17697879</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>2.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.2">Lad Y. , Harburger D.S. , Calderwood D.A. Integrin cytoskeletal interactions. <span><span class="ref-journal">Methods Enzymol. </span>2007;<span class="ref-vol">
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</span>:69–84.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17697880" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17697880</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>3.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.3">Barrett T. , Brechbiel M. , Bernardo M. , Choyke P.L. MRI of tumor angiogenesis. <span><span class="ref-journal">J Magn Reson Imaging. </span>2007;<span class="ref-vol">
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</span>(2):235–49.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17623889" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17623889</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>4.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.4">Cai W. , Chen X. Anti-angiogenic cancer therapy based on integrin alphavbeta3 antagonism. <span><span class="ref-journal">Anticancer Agents Med Chem. </span>2006;<span class="ref-vol">
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<strong>6</strong>
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</span>(5):407–28.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17017851" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17017851</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>5.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.5">Honda Y. , Kitano T. , Fukuya F. , Sato Y. , Iwama S. , Morie T. , Notake M. A Novel alphavbeta3 integrin antagonist suppresses neointima formation for more than 4 weeks after balloon injury in rats. <span><span class="ref-journal">Arterioscler Thromb Vasc Biol. </span>2005;<span class="ref-vol">
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<strong>25</strong>
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</span>(7):1376–82.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15879304" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15879304</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>6.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.6">Zhao Y. , Bachelier R. , Treilleux I. , Pujuguet P. , Peyruchaud O. , Baron R. , Clement-Lacroix P. , Clezardin P. Tumor alphavbeta3 integrin is a therapeutic target for breast cancer bone metastases. <span><span class="ref-journal">Cancer Res. </span>2007;<span class="ref-vol">
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<strong>67</strong>
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</span>(12):5821–30.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17575150" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17575150</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>7.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.7">Kumar C.C. , Malkowski M. , Yin Z. , Tanghetti E. , Yaremko B. , Nechuta T. , Varner J. , Liu M. , Smith E.M. , Neustadt B. , Presta M. , Armstrong L. Inhibition of angiogenesis and tumor growth by SCH221153, a dual alpha(v)beta3 and alpha(v)beta5 integrin receptor antagonist. <span><span class="ref-journal">Cancer Res. </span>2001;<span class="ref-vol">
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<strong>61</strong>
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</span>(5):2232–8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/11280792" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11280792</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>8.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.8">Reynolds L.E. , Wyder L. , Lively J.C. , Taverna D. , Robinson S.D. , Huang X. , Sheppard D. , Hynes R.O. , Hodivala-Dilke K.M. Enhanced pathological angiogenesis in mice lacking beta3 integrin or beta3 and beta5 integrins. <span><span class="ref-journal">Nat Med. </span>2002;<span class="ref-vol">
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<strong>8</strong>
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</span>(1):27–34.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/11786903" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11786903</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>9.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.9">Elkin E.B. , Hudis C. , Begg C.B. , Schrag D. The effect of changes in tumor size on breast carcinoma survival in the U.S.: 1975-1999. <span><span class="ref-journal">Cancer. </span>2005;<span class="ref-vol">
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<strong>104</strong>
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</span>(6):1149–57.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16088887" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16088887</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>10.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.10">Hu G. , Lijowski M. , Zhang H. , Partlow K.C. , Caruthers S.D. , Kiefer G. , Gulyas G. , Athey P. , Scott M.J. , Wickline S.A. , Lanza G.M. Imaging of Vx-2 rabbit tumors with alpha(nu)beta3-integrin-targeted 111In nanoparticles. <span><span class="ref-journal">Int J Cancer. </span>2007;<span class="ref-vol">
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<strong>120</strong>
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</span>(9):1951–7.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17278104" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17278104</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>11.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.11">Knight L.C. , Romano J.E. , Cosenza S.C. , Iqbal N.M. , Marcinkiewicz C. Differences in binding of (99m)Tc-disintegrins to integrin alphavbeta3 on tumor and vascular cells. <span><span class="ref-journal">Nucl Med Biol. </span>2007;<span class="ref-vol">
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<strong>34</strong>
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</span>(4):371–81.</span> [<a href="/pmc/articles/PMC1986642/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC1986642</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/17499726" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17499726</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>12.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.12">Shin I.S. , Jang B.S. , Danthi S.N. , Xie J. , Yu S. , Le N. , Maeng J.S. , Hwang I.S. , Li K.C. , Carrasquillo J.A. , Paik C.H. Use of antibody as carrier of oligomers of peptidomimetic alphavbeta3 antagonist to target tumor-induced neovasculature. <span><span class="ref-journal">Bioconjug Chem. </span>2007;<span class="ref-vol">
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<strong>18</strong>
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</span>(3):821–8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17375899" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17375899</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>13.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.13">Harris T.D. , Kalogeropoulos S. , Nguyen T. , Liu S. , Bartis J. , Ellars C. , Edwards S. , Onthank D. , Silva P. , Yalamanchili P. , Robinson S. , Lazewatsky J. , Barrett J. , Bozarth J. Design, synthesis, and evaluation of radiolabeled integrin alpha v beta 3 receptor antagonists for tumor imaging and radiotherapy. <span><span class="ref-journal">Cancer Biother Radiopharm. </span>2003;<span class="ref-vol">
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<strong>18</strong>
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</span>(4):627–41.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/14503959" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 14503959</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>14.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.14">Lanza G.M. , Wallace K.D. , Scott M.J. , Cacheris W.P. , Abendschein D.R. , Christy D.H. , Sharkey A.M. , Miller J.G. , Gaffney P.J. , Wickline S.A. A novel site-targeted ultrasonic contrast agent with broad biomedical application. <span><span class="ref-journal">Circulation. </span>1996;<span class="ref-vol">
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<strong>94</strong>
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</span>(12):3334–40.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/8989148" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 8989148</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>15.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.15">Winter P.M. , Caruthers S.D. , Kassner A. , Harris T.D. , Chinen L.K. , Allen J.S. , Lacy E.K. , Zhang H. , Robertson J.D. , Wickline S.A. , Lanza G.M. Molecular imaging of angiogenesis in nascent Vx-2 rabbit tumors using a novel alpha(nu)beta3-targeted nanoparticle and 1.5 tesla magnetic resonance imaging. <span><span class="ref-journal">Cancer Res. </span>2003;<span class="ref-vol">
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<strong>63</strong>
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</span>(18):5838–43.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/14522907" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 14522907</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>16.</dt><dd><div class="bk_ref" id="IntegrinNP111In.EXTYLES.16">Liu S. , Harris T.D. , Ellars C.E. , Edwards D.S. Anaerobic 90Y- and 177Lu-labeling of a DOTA-conjugated nonpeptide vitronectin receptor antagonist. <span><span class="ref-journal">Bioconjug Chem. </span>2003;<span class="ref-vol">
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<strong>14</strong>
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</span>(5):1030–7.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/13129408" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 13129408</span></a>]</div></dd></dl></dl></div><div id="bk_toc_contnr"></div></div></div><div class="fm-sec"><h2 id="_NBK23093_pubdet_">Publication Details</h2><h3>Author Information and Affiliations</h3><div class="contrib half_rhythm"><span itemprop="author">Arvind Chopra</span>, PhD<div class="affiliation small">
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National Center for Biotechnology Information, NLM, NIH, Bethesda, MD 20894,
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<span class="before-email-separator"></span><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>
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</div></div><h3>Publication History</h3><p class="small">Created: <span itemprop="datePublished">October 22, 2007</span>; Last Update: <span itemprop="dateModified">November 13, 2007</span>.</p><h3>Copyright</h3><div><div class="half_rhythm"><a href="/books/about/copyright/">Copyright Notice</a></div></div><h3>Publisher</h3><p><a href="http://www.ncbi.nlm.nih.gov/" ref="pagearea=page-banner&targetsite=external&targetcat=link&targettype=publisher">National Center for Biotechnology Information (US)</a>, Bethesda (MD)</p><h3>NLM Citation</h3><p>Chopra A. TA138-conjugated 111In nanoparticles. 2007 Oct 22 [Updated 2007 Nov 13]. 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></p></div><div class="small-screen-prev"><a href="/books/n/micad/CNT-rituximab111In/?report=reader"><svg xmlns="http://www.w3.org/2000/svg" viewBox="0 0 100 100" preserveAspectRatio="none"><path d="M75,30 c-80,60 -80,0 0,60 c-30,-60 -30,0 0,-60"></path><text x="20" y="28" textLength="60" style="font-size:25px">Prev</text></svg></a></div><div class="small-screen-next"><a href="/books/n/micad/sos123i/?report=reader"><svg xmlns="http://www.w3.org/2000/svg" viewBox="0 0 100 100" preserveAspectRatio="none"><path d="M25,30c80,60 80,0 0,60 c30,-60 30,0 0,-60"></path><text x="20" y="28" textLength="60" style="font-size:25px">Next</text></svg></a></div></article><article data-type="table-wrap" id="figobIntegrinNP111InT1"><div id="IntegrinNP111In.T1" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK23093/table/IntegrinNP111In.T1/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__IntegrinNP111In.T1_lrgtbl__"><table><tbody><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Chemical name:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">TA138-conjugated <sup>111</sup>In nanoparticles</td><td rowspan="9" colspan="1" style="text-align:left;vertical-align:middle;">
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<div class="graphic"><img src="/books/NBK23093/bin/IntegrinNPStr.jpg" alt="Image IntegrinNPStr.jpg" /></div>
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</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Abbreviated name:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">α<sub>v</sub>β<sub>3</sub>-targeted <sup>111</sup>In/NP</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Synonym:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Agent Category:</b>
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</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;">
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<b>Target:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">α<sub>v</sub>β<sub>3</sub>-integrin receptor</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Target Category:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Receptor-ligand binding</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Method of detection:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Single-photon emission computed tomography (SPECT) or planar gamma imaging</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Source of signal:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"><sup>111</sup>In</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Activation:</b>
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</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;">
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<b>Studies:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">
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<ul class="simple-list"><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" />
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<i>In vitro</i>
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</div></li></ul>
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<ul class="simple-list"><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Rodents
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</div></li></ul>
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<ul class="simple-list"><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Non-primate non-rodent mammals
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</div></li></ul>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Structure of TA138 (an α<sub>v</sub>β<sub>3</sub> integrin receptor antagonist) that is conjugated to the nanoparticles.</td></tr></tbody></table></div></div></article></div><div id="jr-scripts"><script src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/libs.min.js"> </script><script src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.min.js"> </script></div></div>
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