Adenomatous polyposis coli (APC) plays multiple roles in the intestinal and colorectal epithelia
The adenomatous polyposis coli (APC) gene is mutated in familial adenomatous polyposis and in most sporadic colorectal tumors. During both embryonic and postnatal periods, APC is widely expressed in a variety of tissues, including the brain and gastrointestinal tract. The APC gene product (APC) is a...
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| Veröffentlicht in: | Medical molecular morphology 2007-06, Vol.40 (2), p.68-81 |
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| description | The adenomatous polyposis coli (APC) gene is mutated in familial adenomatous polyposis and in most sporadic colorectal tumors. During both embryonic and postnatal periods, APC is widely expressed in a variety of tissues, including the brain and gastrointestinal tract. The APC gene product (APC) is a large multidomain protein consisting of 2843 amino acids. APC downregulates the Wnt signaling pathway through its binding to beta-catenin and Axin. Most mutated APC proteins in colorectal tumors lack the beta-catenin-binding regions and fail to inhibit Wnt signaling, leading to the overproliferation of tumor cells. Several mouse models (APC580D, APCDelta716, APC1309, APCMin, APC1638T) have been established to investigate carcinogenesis caused by APC mutations. APC also binds to APC-stimulated guanine nucleotide exchange factor, the kinesin superfamily-associated protein 3, IQGAP1, microtubules, EB1, and discs large (DLG). APC has both nuclear localization signals and nuclear export signals in its molecule, suggesting its occasional nuclear localization and export of beta-catenin from the nucleus. APC is highly expressed in the intestinal and colorectal epithelia and may be involved in homeostasis of the enterocyte renewal phenomena, in which proliferation, migration, differentiation, and apoptosis are highly regulated both temporally and spatially. Through the many binding proteins mentioned, APC can exert multiple functions involved in epithelial homeostasis. |
| doi_str_mv | 10.1007/s00795-006-0352-5 |
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During both embryonic and postnatal periods, APC is widely expressed in a variety of tissues, including the brain and gastrointestinal tract. The APC gene product (APC) is a large multidomain protein consisting of 2843 amino acids. APC downregulates the Wnt signaling pathway through its binding to beta-catenin and Axin. Most mutated APC proteins in colorectal tumors lack the beta-catenin-binding regions and fail to inhibit Wnt signaling, leading to the overproliferation of tumor cells. Several mouse models (APC580D, APCDelta716, APC1309, APCMin, APC1638T) have been established to investigate carcinogenesis caused by APC mutations. APC also binds to APC-stimulated guanine nucleotide exchange factor, the kinesin superfamily-associated protein 3, IQGAP1, microtubules, EB1, and discs large (DLG). APC has both nuclear localization signals and nuclear export signals in its molecule, suggesting its occasional nuclear localization and export of beta-catenin from the nucleus. APC is highly expressed in the intestinal and colorectal epithelia and may be involved in homeostasis of the enterocyte renewal phenomena, in which proliferation, migration, differentiation, and apoptosis are highly regulated both temporally and spatially. Through the many binding proteins mentioned, APC can exert multiple functions involved in epithelial homeostasis.</description><identifier>ISSN: 1860-1480</identifier><identifier>EISSN: 1860-1499</identifier><identifier>DOI: 10.1007/s00795-006-0352-5</identifier><identifier>PMID: 17572842</identifier><identifier>CODEN: MELMEJ</identifier><language>eng</language><publisher>Japan: Springer Nature B.V</publisher><subject>Adenomatous polyposis coli ; Adenomatous Polyposis Coli Protein - deficiency ; Adenomatous Polyposis Coli Protein - metabolism ; Animal models ; Animals ; Apoptosis ; Binding Sites - genetics ; Carcinogenesis ; Cell culture ; Colon - physiology ; Colon - physiopathology ; Colorectal cancer ; Colorectal Neoplasms - metabolism ; Colorectal Neoplasms - physiopathology ; Embryos ; Epithelium - physiology ; Epithelium - physiopathology ; Familial adenomatous polyposis ; Gastroenterology ; Gastrointestinal tract ; Gene Expression Regulation, Neoplastic ; Genes, APC ; Genetic disorders ; Genetics ; Guanine ; Guanine nucleotide exchange factor ; Homeostasis ; Humans ; Intestine ; IQGAP1 protein ; Kinesin ; Localization ; Medical research ; Mice ; Mice, Knockout ; Microtubules ; Microtubules - metabolism ; Molecular biology ; Mutation ; Mutation - genetics ; Nuclear transport ; Polyposis coli ; Polyps ; Protein Binding - genetics ; Rats ; Repressor Proteins - metabolism ; Rodents ; Signal Transduction ; Tumor cells ; Tumors ; Wnt protein ; β-Catenin</subject><ispartof>Medical molecular morphology, 2007-06, Vol.40 (2), p.68-81</ispartof><rights>The Japanese Society for Clinical Molecular Morphology 2007</rights><rights>The Japanese Society for Clinical Molecular Morphology 2007.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-df48fdebf2404b201b48598541c056b82a16c3adb5d966803dead8a8761745e03</citedby><cites>FETCH-LOGICAL-c473t-df48fdebf2404b201b48598541c056b82a16c3adb5d966803dead8a8761745e03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17572842$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Senda, Takao</creatorcontrib><creatorcontrib>Iizuka-Kogo, Akiko</creatorcontrib><creatorcontrib>Onouchi, Takanori</creatorcontrib><creatorcontrib>Shimomura, Atsushi</creatorcontrib><title>Adenomatous polyposis coli (APC) plays multiple roles in the intestinal and colorectal epithelia</title><title>Medical molecular morphology</title><addtitle>Med Mol Morphol</addtitle><description>The adenomatous polyposis coli (APC) gene is mutated in familial adenomatous polyposis and in most sporadic colorectal tumors. During both embryonic and postnatal periods, APC is widely expressed in a variety of tissues, including the brain and gastrointestinal tract. The APC gene product (APC) is a large multidomain protein consisting of 2843 amino acids. APC downregulates the Wnt signaling pathway through its binding to beta-catenin and Axin. Most mutated APC proteins in colorectal tumors lack the beta-catenin-binding regions and fail to inhibit Wnt signaling, leading to the overproliferation of tumor cells. Several mouse models (APC580D, APCDelta716, APC1309, APCMin, APC1638T) have been established to investigate carcinogenesis caused by APC mutations. APC also binds to APC-stimulated guanine nucleotide exchange factor, the kinesin superfamily-associated protein 3, IQGAP1, microtubules, EB1, and discs large (DLG). APC has both nuclear localization signals and nuclear export signals in its molecule, suggesting its occasional nuclear localization and export of beta-catenin from the nucleus. APC is highly expressed in the intestinal and colorectal epithelia and may be involved in homeostasis of the enterocyte renewal phenomena, in which proliferation, migration, differentiation, and apoptosis are highly regulated both temporally and spatially. Through the many binding proteins mentioned, APC can exert multiple functions involved in epithelial homeostasis.</description><subject>Adenomatous polyposis coli</subject><subject>Adenomatous Polyposis Coli Protein - deficiency</subject><subject>Adenomatous Polyposis Coli Protein - metabolism</subject><subject>Animal models</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Binding Sites - genetics</subject><subject>Carcinogenesis</subject><subject>Cell culture</subject><subject>Colon - physiology</subject><subject>Colon - physiopathology</subject><subject>Colorectal cancer</subject><subject>Colorectal Neoplasms - metabolism</subject><subject>Colorectal Neoplasms - physiopathology</subject><subject>Embryos</subject><subject>Epithelium - physiology</subject><subject>Epithelium - physiopathology</subject><subject>Familial adenomatous polyposis</subject><subject>Gastroenterology</subject><subject>Gastrointestinal tract</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Genes, APC</subject><subject>Genetic disorders</subject><subject>Genetics</subject><subject>Guanine</subject><subject>Guanine nucleotide exchange factor</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Intestine</subject><subject>IQGAP1 protein</subject><subject>Kinesin</subject><subject>Localization</subject><subject>Medical research</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Microtubules</subject><subject>Microtubules - metabolism</subject><subject>Molecular biology</subject><subject>Mutation</subject><subject>Mutation - genetics</subject><subject>Nuclear transport</subject><subject>Polyposis coli</subject><subject>Polyps</subject><subject>Protein Binding - genetics</subject><subject>Rats</subject><subject>Repressor Proteins - metabolism</subject><subject>Rodents</subject><subject>Signal Transduction</subject><subject>Tumor cells</subject><subject>Tumors</subject><subject>Wnt protein</subject><subject>β-Catenin</subject><issn>1860-1480</issn><issn>1860-1499</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp1kLtOwzAUhi0EolB4ABZkwQJDwHc7Y1VxkyrBALNxYke4cuoQJ0PfHketYGI5F-k7v44-AC4wusMIyfuUS8kLhESBKCcFPwAnWAlUYFaWh7-zQjNwmtIaISoF4cdghiWXRDFyAj4X1m1ia4Y4JtjFsO1i8gnWMXh4s3hb3sIumG2C7RgG3wUH-xhcgn4Dhy-X2-DS4DcmQLOx01XsXT3k1XU-A8GbM3DUmJDc-b7Pwcfjw_vyuVi9Pr0sF6uiZpIOhW2YaqyrGsIQqwjCFVO8VJzhGnFRKWKwqKmxFbelEApR64xVRkmBJeMO0Tm43uV2ffwe81d6Hcc-f5Y0EYIpJaTgmbr6j8KllFQpIjKEd1Ddx5R61-iu963ptxojPYnXO_E6i9eTeD0FX-6Dx6p19u9ib5r-AIYpfYk</recordid><startdate>20070601</startdate><enddate>20070601</enddate><creator>Senda, Takao</creator><creator>Iizuka-Kogo, Akiko</creator><creator>Onouchi, Takanori</creator><creator>Shimomura, Atsushi</creator><general>Springer Nature B.V</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>3V.</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>20070601</creationdate><title>Adenomatous polyposis coli (APC) plays multiple roles in the intestinal and colorectal epithelia</title><author>Senda, Takao ; Iizuka-Kogo, Akiko ; Onouchi, Takanori ; Shimomura, Atsushi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c473t-df48fdebf2404b201b48598541c056b82a16c3adb5d966803dead8a8761745e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adenomatous polyposis coli</topic><topic>Adenomatous Polyposis Coli Protein - deficiency</topic><topic>Adenomatous Polyposis Coli Protein - metabolism</topic><topic>Animal models</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Binding Sites - genetics</topic><topic>Carcinogenesis</topic><topic>Cell culture</topic><topic>Colon - physiology</topic><topic>Colon - physiopathology</topic><topic>Colorectal cancer</topic><topic>Colorectal Neoplasms - metabolism</topic><topic>Colorectal Neoplasms - physiopathology</topic><topic>Embryos</topic><topic>Epithelium - physiology</topic><topic>Epithelium - physiopathology</topic><topic>Familial adenomatous polyposis</topic><topic>Gastroenterology</topic><topic>Gastrointestinal tract</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Genes, APC</topic><topic>Genetic disorders</topic><topic>Genetics</topic><topic>Guanine</topic><topic>Guanine nucleotide exchange factor</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Intestine</topic><topic>IQGAP1 protein</topic><topic>Kinesin</topic><topic>Localization</topic><topic>Medical research</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Microtubules</topic><topic>Microtubules - metabolism</topic><topic>Molecular biology</topic><topic>Mutation</topic><topic>Mutation - genetics</topic><topic>Nuclear transport</topic><topic>Polyposis coli</topic><topic>Polyps</topic><topic>Protein Binding - genetics</topic><topic>Rats</topic><topic>Repressor Proteins - metabolism</topic><topic>Rodents</topic><topic>Signal Transduction</topic><topic>Tumor cells</topic><topic>Tumors</topic><topic>Wnt protein</topic><topic>β-Catenin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Senda, Takao</creatorcontrib><creatorcontrib>Iizuka-Kogo, Akiko</creatorcontrib><creatorcontrib>Onouchi, Takanori</creatorcontrib><creatorcontrib>Shimomura, Atsushi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><jtitle>Medical molecular morphology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Senda, Takao</au><au>Iizuka-Kogo, Akiko</au><au>Onouchi, Takanori</au><au>Shimomura, Atsushi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adenomatous polyposis coli (APC) plays multiple roles in the intestinal and colorectal epithelia</atitle><jtitle>Medical molecular morphology</jtitle><addtitle>Med Mol Morphol</addtitle><date>2007-06-01</date><risdate>2007</risdate><volume>40</volume><issue>2</issue><spage>68</spage><epage>81</epage><pages>68-81</pages><issn>1860-1480</issn><eissn>1860-1499</eissn><coden>MELMEJ</coden><abstract>The adenomatous polyposis coli (APC) gene is mutated in familial adenomatous polyposis and in most sporadic colorectal tumors. During both embryonic and postnatal periods, APC is widely expressed in a variety of tissues, including the brain and gastrointestinal tract. The APC gene product (APC) is a large multidomain protein consisting of 2843 amino acids. APC downregulates the Wnt signaling pathway through its binding to beta-catenin and Axin. Most mutated APC proteins in colorectal tumors lack the beta-catenin-binding regions and fail to inhibit Wnt signaling, leading to the overproliferation of tumor cells. Several mouse models (APC580D, APCDelta716, APC1309, APCMin, APC1638T) have been established to investigate carcinogenesis caused by APC mutations. APC also binds to APC-stimulated guanine nucleotide exchange factor, the kinesin superfamily-associated protein 3, IQGAP1, microtubules, EB1, and discs large (DLG). APC has both nuclear localization signals and nuclear export signals in its molecule, suggesting its occasional nuclear localization and export of beta-catenin from the nucleus. APC is highly expressed in the intestinal and colorectal epithelia and may be involved in homeostasis of the enterocyte renewal phenomena, in which proliferation, migration, differentiation, and apoptosis are highly regulated both temporally and spatially. Through the many binding proteins mentioned, APC can exert multiple functions involved in epithelial homeostasis.</abstract><cop>Japan</cop><pub>Springer Nature B.V</pub><pmid>17572842</pmid><doi>10.1007/s00795-006-0352-5</doi><tpages>14</tpages></addata></record> |
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| subjects | Adenomatous polyposis coli Adenomatous Polyposis Coli Protein - deficiency Adenomatous Polyposis Coli Protein - metabolism Animal models Animals Apoptosis Binding Sites - genetics Carcinogenesis Cell culture Colon - physiology Colon - physiopathology Colorectal cancer Colorectal Neoplasms - metabolism Colorectal Neoplasms - physiopathology Embryos Epithelium - physiology Epithelium - physiopathology Familial adenomatous polyposis Gastroenterology Gastrointestinal tract Gene Expression Regulation, Neoplastic Genes, APC Genetic disorders Genetics Guanine Guanine nucleotide exchange factor Homeostasis Humans Intestine IQGAP1 protein Kinesin Localization Medical research Mice Mice, Knockout Microtubules Microtubules - metabolism Molecular biology Mutation Mutation - genetics Nuclear transport Polyposis coli Polyps Protein Binding - genetics Rats Repressor Proteins - metabolism Rodents Signal Transduction Tumor cells Tumors Wnt protein β-Catenin |
| title | Adenomatous polyposis coli (APC) plays multiple roles in the intestinal and colorectal epithelia |
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