Elucidating the Functional Mechanism of PTK7 in Cancer Development through Spatial Assembly Analysis Using Super Resolution Imaging
Protein tyrosine kinase-7 (PTK7) has been reported as a vital participant in the Wnt signaling pathway, influencing tumorigenesis and metastasis. However, their specific roles in the mechanisms underlying cancer development and progression remain elusive. Here, using direct stochastic optical recons...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2024-05, Vol.96 (19), p.7669-7678 |
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| creator | Qiu, Luqi Xu, Haijiao Sui, Binglin Jiang, Pengwei Wang, Jiaqi Xu, Dandan Liang, Feng Ma, Tao Wang, Hongda Chen, Junling |
| description | Protein tyrosine kinase-7 (PTK7) has been reported as a vital participant in the Wnt signaling pathway, influencing tumorigenesis and metastasis. However, their specific roles in the mechanisms underlying cancer development and progression remain elusive. Here, using direct stochastic optical reconstruction microscopy (dSTORM) with aptamer-probe labeling, we first revealed that a weakening clustering distribution of PTK7 on the basal membranes happened as cellular migration increased during cancer progression. This correspondence was further supported by a diminished aggregated state of PTK7 caused by direct enhancement of cell migration. By comparing the alterations in PTK7 distribution with activation or inhibition of specific Wnt signaling pathway, we speculated that PTK7 could modulate cell migration by participating in the interplay between canonical Wnt (in MCF7 cells) and noncanonical Wnt signals (in MDA-MB-231 cells). Furthermore, we discovered that the spatial distribution morphology of PTK7 was also subject to the hydrolysis ability and activation state of the related hydrolase Matrix metallopeptidase14 (MMP14). This function-related specific assembly of PTK7 reveals a clear relationship between PTK7 and cancer. Meanwhile, potential molecular interactions predicted by the apparent assembly morphology can promote a deep understanding of the functional mechanism of PTK7 in cancer progress. |
| doi_str_mv | 10.1021/acs.analchem.4c00588 |
| format | Article |
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However, their specific roles in the mechanisms underlying cancer development and progression remain elusive. Here, using direct stochastic optical reconstruction microscopy (dSTORM) with aptamer-probe labeling, we first revealed that a weakening clustering distribution of PTK7 on the basal membranes happened as cellular migration increased during cancer progression. This correspondence was further supported by a diminished aggregated state of PTK7 caused by direct enhancement of cell migration. By comparing the alterations in PTK7 distribution with activation or inhibition of specific Wnt signaling pathway, we speculated that PTK7 could modulate cell migration by participating in the interplay between canonical Wnt (in MCF7 cells) and noncanonical Wnt signals (in MDA-MB-231 cells). Furthermore, we discovered that the spatial distribution morphology of PTK7 was also subject to the hydrolysis ability and activation state of the related hydrolase Matrix metallopeptidase14 (MMP14). This function-related specific assembly of PTK7 reveals a clear relationship between PTK7 and cancer. Meanwhile, potential molecular interactions predicted by the apparent assembly morphology can promote a deep understanding of the functional mechanism of PTK7 in cancer progress.</description><identifier>ISSN: 0003-2700</identifier><identifier>ISSN: 1520-6882</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/acs.analchem.4c00588</identifier><identifier>PMID: 38708542</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>analytical chemistry ; Aptamers ; Assembly ; Cancer ; carcinogenesis ; Cell adhesion & migration ; Cell Adhesion Molecules - metabolism ; Cell Line, Tumor ; Cell migration ; Cell Movement ; Clustering ; Cytology ; Humans ; hydrolases ; hydrolysis ; Kinases ; Matrix Metalloproteinase 14 - metabolism ; Metastases ; metastasis ; microscopy ; Molecular interactions ; Morphology ; neoplasm progression ; Neoplasms - metabolism ; Neoplasms - pathology ; Protein-tyrosine kinase ; Receptor Protein-Tyrosine Kinases - metabolism ; Signal transduction ; Spatial analysis ; Spatial distribution ; Tumorigenesis ; Tyrosine ; Wnt protein ; Wnt Signaling Pathway</subject><ispartof>Analytical chemistry (Washington), 2024-05, Vol.96 (19), p.7669-7678</ispartof><rights>2024 American Chemical Society</rights><rights>Copyright American Chemical Society May 14, 2024</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a358t-4ae42755c72cf328f5850001165c403bf17a23992c3125d129ec0ec9bfda45793</cites><orcidid>0000-0003-4266-9012</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.analchem.4c00588$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.analchem.4c00588$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38708542$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Qiu, Luqi</creatorcontrib><creatorcontrib>Xu, Haijiao</creatorcontrib><creatorcontrib>Sui, Binglin</creatorcontrib><creatorcontrib>Jiang, Pengwei</creatorcontrib><creatorcontrib>Wang, Jiaqi</creatorcontrib><creatorcontrib>Xu, Dandan</creatorcontrib><creatorcontrib>Liang, Feng</creatorcontrib><creatorcontrib>Ma, Tao</creatorcontrib><creatorcontrib>Wang, Hongda</creatorcontrib><creatorcontrib>Chen, Junling</creatorcontrib><title>Elucidating the Functional Mechanism of PTK7 in Cancer Development through Spatial Assembly Analysis Using Super Resolution Imaging</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Protein tyrosine kinase-7 (PTK7) has been reported as a vital participant in the Wnt signaling pathway, influencing tumorigenesis and metastasis. However, their specific roles in the mechanisms underlying cancer development and progression remain elusive. Here, using direct stochastic optical reconstruction microscopy (dSTORM) with aptamer-probe labeling, we first revealed that a weakening clustering distribution of PTK7 on the basal membranes happened as cellular migration increased during cancer progression. This correspondence was further supported by a diminished aggregated state of PTK7 caused by direct enhancement of cell migration. By comparing the alterations in PTK7 distribution with activation or inhibition of specific Wnt signaling pathway, we speculated that PTK7 could modulate cell migration by participating in the interplay between canonical Wnt (in MCF7 cells) and noncanonical Wnt signals (in MDA-MB-231 cells). Furthermore, we discovered that the spatial distribution morphology of PTK7 was also subject to the hydrolysis ability and activation state of the related hydrolase Matrix metallopeptidase14 (MMP14). This function-related specific assembly of PTK7 reveals a clear relationship between PTK7 and cancer. Meanwhile, potential molecular interactions predicted by the apparent assembly morphology can promote a deep understanding of the functional mechanism of PTK7 in cancer progress.</description><subject>analytical chemistry</subject><subject>Aptamers</subject><subject>Assembly</subject><subject>Cancer</subject><subject>carcinogenesis</subject><subject>Cell adhesion & migration</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Cell migration</subject><subject>Cell Movement</subject><subject>Clustering</subject><subject>Cytology</subject><subject>Humans</subject><subject>hydrolases</subject><subject>hydrolysis</subject><subject>Kinases</subject><subject>Matrix Metalloproteinase 14 - metabolism</subject><subject>Metastases</subject><subject>metastasis</subject><subject>microscopy</subject><subject>Molecular interactions</subject><subject>Morphology</subject><subject>neoplasm progression</subject><subject>Neoplasms - metabolism</subject><subject>Neoplasms - pathology</subject><subject>Protein-tyrosine kinase</subject><subject>Receptor Protein-Tyrosine Kinases - metabolism</subject><subject>Signal transduction</subject><subject>Spatial analysis</subject><subject>Spatial distribution</subject><subject>Tumorigenesis</subject><subject>Tyrosine</subject><subject>Wnt protein</subject><subject>Wnt Signaling Pathway</subject><issn>0003-2700</issn><issn>1520-6882</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkT1v2zAQhokiReOm_QdFQCBLFrnHL5EaDSdpg6Zo0SSzQNMnW4EkKqJYwHP_eKnaydAhmW64530Oh5eQTwzmDDj7bF2Y2842bovtXDoAZcwbMmOKQ5Ybw4_IDABExjXAMXkfwgMAY8Dyd-RYGA1GST4jfy6b6Oq1HetuQ8ct0qvYubH2SUy_o9varg4t9RX9efdN07qjS9s5HOgF_sbG9y12Y4oNPm629LZPmpRbhIDtqtnRRbLsQh3ofZj0t7FPyV8YfBOnE_S6tZu0-EDeVrYJ-PEwT8j91eXd8mt28-PL9XJxk1mhzJhJi5JrpZzmrhLcVMoomH7KlZMgVhXTloui4E4wrtaMF-gAXbGq1lYqXYgTcr739oN_jBjGsq2Dw6axHfoYSsGUUFpxLV5HQTHJpeQTevYf-uDjkD7_R-Vc5IyZRMk95QYfwoBV2Q91a4ddyaCc-ixTn-VTn-WhzxQ7PcjjqsX1c-ipwATAHpjiz4dfdP4Fxcyurw</recordid><startdate>20240514</startdate><enddate>20240514</enddate><creator>Qiu, Luqi</creator><creator>Xu, Haijiao</creator><creator>Sui, Binglin</creator><creator>Jiang, Pengwei</creator><creator>Wang, Jiaqi</creator><creator>Xu, Dandan</creator><creator>Liang, Feng</creator><creator>Ma, Tao</creator><creator>Wang, Hongda</creator><creator>Chen, Junling</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0003-4266-9012</orcidid></search><sort><creationdate>20240514</creationdate><title>Elucidating the Functional Mechanism of PTK7 in Cancer Development through Spatial Assembly Analysis Using Super Resolution Imaging</title><author>Qiu, Luqi ; 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Chem</addtitle><date>2024-05-14</date><risdate>2024</risdate><volume>96</volume><issue>19</issue><spage>7669</spage><epage>7678</epage><pages>7669-7678</pages><issn>0003-2700</issn><issn>1520-6882</issn><eissn>1520-6882</eissn><abstract>Protein tyrosine kinase-7 (PTK7) has been reported as a vital participant in the Wnt signaling pathway, influencing tumorigenesis and metastasis. However, their specific roles in the mechanisms underlying cancer development and progression remain elusive. Here, using direct stochastic optical reconstruction microscopy (dSTORM) with aptamer-probe labeling, we first revealed that a weakening clustering distribution of PTK7 on the basal membranes happened as cellular migration increased during cancer progression. This correspondence was further supported by a diminished aggregated state of PTK7 caused by direct enhancement of cell migration. By comparing the alterations in PTK7 distribution with activation or inhibition of specific Wnt signaling pathway, we speculated that PTK7 could modulate cell migration by participating in the interplay between canonical Wnt (in MCF7 cells) and noncanonical Wnt signals (in MDA-MB-231 cells). Furthermore, we discovered that the spatial distribution morphology of PTK7 was also subject to the hydrolysis ability and activation state of the related hydrolase Matrix metallopeptidase14 (MMP14). This function-related specific assembly of PTK7 reveals a clear relationship between PTK7 and cancer. Meanwhile, potential molecular interactions predicted by the apparent assembly morphology can promote a deep understanding of the functional mechanism of PTK7 in cancer progress.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>38708542</pmid><doi>10.1021/acs.analchem.4c00588</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-4266-9012</orcidid></addata></record> |
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| subjects | analytical chemistry Aptamers Assembly Cancer carcinogenesis Cell adhesion & migration Cell Adhesion Molecules - metabolism Cell Line, Tumor Cell migration Cell Movement Clustering Cytology Humans hydrolases hydrolysis Kinases Matrix Metalloproteinase 14 - metabolism Metastases metastasis microscopy Molecular interactions Morphology neoplasm progression Neoplasms - metabolism Neoplasms - pathology Protein-tyrosine kinase Receptor Protein-Tyrosine Kinases - metabolism Signal transduction Spatial analysis Spatial distribution Tumorigenesis Tyrosine Wnt protein Wnt Signaling Pathway |
| title | Elucidating the Functional Mechanism of PTK7 in Cancer Development through Spatial Assembly Analysis Using Super Resolution Imaging |
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