Aglycon of Rhizochalin from the Rhizochalina incrustata Induces Apoptosis via Activation of AMP-Activated Protein Kinase in HT-29 Colon Cancer Cells
Rhizochalin is a two-headed sphingolipid-like compound isolated from the sponge Rhizochalina incrustata. It has been reported that rhizocalin and its derivates have a chemopreventive and chemotherapeutic effect. However, the molecular mechanism of these effects is not understood. Here, we demonstrat...
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| Veröffentlicht in: | Biological & Pharmaceutical Bulletin 2011/10/01, Vol.34(10), pp.1553-1558 |
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| creator | Khanal, Prem Kang, Bong Seok Yun, Hyo Jeong Cho, Hae-Guk Makarieva, Tatyana Nikolaevna Choi, Hong Seok |
| description | Rhizochalin is a two-headed sphingolipid-like compound isolated from the sponge Rhizochalina incrustata. It has been reported that rhizocalin and its derivates have a chemopreventive and chemotherapeutic effect. However, the molecular mechanism of these effects is not understood. Here, we demonstrate that aglycon of rhizochalin (AglRhz) from the Rhizochalina incrustata induces AMP-activated protein kinase (AMPK) phosphorylation, and thereby inhibits mammalian target of rapamycin (mTOR)-p70S6 kinase-extracellular signal-regulated kinase (ERK) signaling and activator protein 1 (AP-1) activity via phosphorylation of Raptor in HT-29 cells. In addition, AglRhz induced activation of caspase-3 and poly(ADP-ribose) polymerase (PARP), and DNA fragmentation in HT-29 cells, leads to induction of apoptosis as well as suppression of tumorigenicity of HT-29 cells. Notably, AglRhz inhibits insulin-like growth factor (IGF)-1-induced AP-1 activity and cell transformation in JB6 Cl41 cells. Overall, our findings identify AMPK as an important target protein for mediating the anti-tumor properties of AglRhz in HT-29 colon cancer cells and have important implication for sponges, the most important marine source, in colon cancer. |
| doi_str_mv | 10.1248/bpb.34.1553 |
| format | Article |
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It has been reported that rhizocalin and its derivates have a chemopreventive and chemotherapeutic effect. However, the molecular mechanism of these effects is not understood. Here, we demonstrate that aglycon of rhizochalin (AglRhz) from the Rhizochalina incrustata induces AMP-activated protein kinase (AMPK) phosphorylation, and thereby inhibits mammalian target of rapamycin (mTOR)-p70S6 kinase-extracellular signal-regulated kinase (ERK) signaling and activator protein 1 (AP-1) activity via phosphorylation of Raptor in HT-29 cells. In addition, AglRhz induced activation of caspase-3 and poly(ADP-ribose) polymerase (PARP), and DNA fragmentation in HT-29 cells, leads to induction of apoptosis as well as suppression of tumorigenicity of HT-29 cells. Notably, AglRhz inhibits insulin-like growth factor (IGF)-1-induced AP-1 activity and cell transformation in JB6 Cl41 cells. Overall, our findings identify AMPK as an important target protein for mediating the anti-tumor properties of AglRhz in HT-29 colon cancer cells and have important implication for sponges, the most important marine source, in colon cancer.</description><identifier>ISSN: 0918-6158</identifier><identifier>ISSN: 1347-5215</identifier><identifier>EISSN: 1347-5215</identifier><identifier>DOI: 10.1248/bpb.34.1553</identifier><identifier>PMID: 21963494</identifier><language>eng</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>AMP-activated protein kinase ; AMP-Activated Protein Kinases - genetics ; AMP-Activated Protein Kinases - metabolism ; Animals ; Antineoplastic Agents - metabolism ; Antineoplastic Agents - pharmacology ; Antineoplastic Agents - therapeutic use ; Apoptosis - drug effects ; c-Fos ; c-Jun ; Caspase 3 - metabolism ; cell transformation ; Cell Transformation, Neoplastic - drug effects ; Chemoprevention ; Colonic Neoplasms - drug therapy ; Colonic Neoplasms - enzymology ; Colonic Neoplasms - genetics ; Colonic Neoplasms - pathology ; DNA Fragmentation - drug effects ; Drug Evaluation, Preclinical ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Fatty Alcohols - metabolism ; Fatty Alcohols - pharmacology ; Fatty Alcohols - therapeutic use ; Glycosphingolipids - chemistry ; Glycosphingolipids - metabolism ; Glycosphingolipids - pharmacology ; Glycosphingolipids - therapeutic use ; HT29 Cells ; Humans ; Marine ; Mice ; Mitogen-Activated Protein Kinases - metabolism ; Molecular Targeted Therapy ; Oceans and Seas ; Phosphorylation ; Phytotherapy ; Plant Preparations - chemistry ; Plant Preparations - isolation & purification ; Plant Preparations - pharmacology ; Poly(ADP-ribose) Polymerases - metabolism ; Porifera ; Protein-Serine-Threonine Kinases - metabolism ; rhizochalin ; Rhizochalina ; Tetrazolium Salts ; Thiazoles ; TOR Serine-Threonine Kinases - genetics ; TOR Serine-Threonine Kinases - metabolism ; Tumor Cells, Cultured</subject><ispartof>Biological and Pharmaceutical Bulletin, 2011/10/01, Vol.34(10), pp.1553-1558</ispartof><rights>2011 The Pharmaceutical Society of Japan</rights><rights>Copyright Japan Science and Technology Agency 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c726t-1c591e49e390f1b81ce72d0cbf54a7dd38f5a6305ee3d1b9b7560a03629e0213</citedby><cites>FETCH-LOGICAL-c726t-1c591e49e390f1b81ce72d0cbf54a7dd38f5a6305ee3d1b9b7560a03629e0213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1877,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21963494$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Khanal, Prem</creatorcontrib><creatorcontrib>Kang, Bong Seok</creatorcontrib><creatorcontrib>Yun, Hyo Jeong</creatorcontrib><creatorcontrib>Cho, Hae-Guk</creatorcontrib><creatorcontrib>Makarieva, Tatyana Nikolaevna</creatorcontrib><creatorcontrib>Choi, Hong Seok</creatorcontrib><creatorcontrib>Chosun University</creatorcontrib><creatorcontrib>bBio-Medical Research Institute</creatorcontrib><creatorcontrib>Pacific Institute of Bioorganic Chemistry of the Russian Academy of Sciences</creatorcontrib><creatorcontrib>aBK Project Team</creatorcontrib><creatorcontrib>Kyungpook National University Hospital</creatorcontrib><creatorcontrib>cLaboratory of the MaNaPro Chemistry</creatorcontrib><creatorcontrib>College of Pharmacy</creatorcontrib><title>Aglycon of Rhizochalin from the Rhizochalina incrustata Induces Apoptosis via Activation of AMP-Activated Protein Kinase in HT-29 Colon Cancer Cells</title><title>Biological & Pharmaceutical Bulletin</title><addtitle>Biol Pharm Bull</addtitle><description>Rhizochalin is a two-headed sphingolipid-like compound isolated from the sponge Rhizochalina incrustata. It has been reported that rhizocalin and its derivates have a chemopreventive and chemotherapeutic effect. However, the molecular mechanism of these effects is not understood. Here, we demonstrate that aglycon of rhizochalin (AglRhz) from the Rhizochalina incrustata induces AMP-activated protein kinase (AMPK) phosphorylation, and thereby inhibits mammalian target of rapamycin (mTOR)-p70S6 kinase-extracellular signal-regulated kinase (ERK) signaling and activator protein 1 (AP-1) activity via phosphorylation of Raptor in HT-29 cells. In addition, AglRhz induced activation of caspase-3 and poly(ADP-ribose) polymerase (PARP), and DNA fragmentation in HT-29 cells, leads to induction of apoptosis as well as suppression of tumorigenicity of HT-29 cells. Notably, AglRhz inhibits insulin-like growth factor (IGF)-1-induced AP-1 activity and cell transformation in JB6 Cl41 cells. Overall, our findings identify AMPK as an important target protein for mediating the anti-tumor properties of AglRhz in HT-29 colon cancer cells and have important implication for sponges, the most important marine source, in colon cancer.</description><subject>AMP-activated protein kinase</subject><subject>AMP-Activated Protein Kinases - genetics</subject><subject>AMP-Activated Protein Kinases - metabolism</subject><subject>Animals</subject><subject>Antineoplastic Agents - metabolism</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Antineoplastic Agents - therapeutic use</subject><subject>Apoptosis - drug effects</subject><subject>c-Fos</subject><subject>c-Jun</subject><subject>Caspase 3 - metabolism</subject><subject>cell transformation</subject><subject>Cell Transformation, Neoplastic - drug effects</subject><subject>Chemoprevention</subject><subject>Colonic Neoplasms - drug therapy</subject><subject>Colonic Neoplasms - enzymology</subject><subject>Colonic Neoplasms - genetics</subject><subject>Colonic Neoplasms - pathology</subject><subject>DNA Fragmentation - drug effects</subject><subject>Drug Evaluation, Preclinical</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Fatty Alcohols - metabolism</subject><subject>Fatty Alcohols - pharmacology</subject><subject>Fatty Alcohols - therapeutic use</subject><subject>Glycosphingolipids - chemistry</subject><subject>Glycosphingolipids - metabolism</subject><subject>Glycosphingolipids - pharmacology</subject><subject>Glycosphingolipids - therapeutic use</subject><subject>HT29 Cells</subject><subject>Humans</subject><subject>Marine</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Molecular Targeted Therapy</subject><subject>Oceans and Seas</subject><subject>Phosphorylation</subject><subject>Phytotherapy</subject><subject>Plant Preparations - chemistry</subject><subject>Plant Preparations - isolation & purification</subject><subject>Plant Preparations - pharmacology</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Porifera</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>rhizochalin</subject><subject>Rhizochalina</subject><subject>Tetrazolium Salts</subject><subject>Thiazoles</subject><subject>TOR Serine-Threonine Kinases - genetics</subject><subject>TOR Serine-Threonine Kinases - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>0918-6158</issn><issn>1347-5215</issn><issn>1347-5215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ks9v0zAUxyMEYt3gxB1Z4sAklOKfSXzMKtgmhphQ75bjvKyu0rjYyaTxd_AH87p2BXHg4lj2R5_38r7OsjeMzhmX1cdm28yFnDOlxLNsxoQsc8WZep7NqGZVXjBVnWSnKa0ppSXl4mV2wpkuhNRylv2q7_oHFwYSOvJ95X8Gt7K9H0gXw4aMK_j70BI_uDil0Y6WXA_t5CCRehu2Y0g-kXtvSe1Gf29HvxfWX2_zwwm05DaGEVD9BU0J0EWuljnXZBF6xBd2cBDJAvo-vcpedLZP8PrwPcuWnz8tF1f5zbfL60V9k7uSF2POnNIMpAahaceaijkoeUtd0ylpy7YVVadsIagCEC1rdFOqgloqCq6BcibOsvd77TaGHxOk0Wx8ctiAHSBMyVS64LLkXCN5_l-ScWwIaSoRffcPug5THPA3DJNSi4qVBUfqw55yMaQUoTPb6Dc2PhhGzS5Vg6kaIc0uVaTfHpxTs4H2yD7FiMDlHsBb7yzOE-OCP5VdKhuPYzacMmYoFRLLUKoe9bul2m1ksZvJxd60xpjv4FjKxtG7Ho5t0cP6KHi6xGcSDQziN2O4yn4</recordid><startdate>2011</startdate><enddate>2011</enddate><creator>Khanal, Prem</creator><creator>Kang, Bong Seok</creator><creator>Yun, Hyo Jeong</creator><creator>Cho, Hae-Guk</creator><creator>Makarieva, Tatyana Nikolaevna</creator><creator>Choi, Hong Seok</creator><general>The Pharmaceutical Society of Japan</general><general>Pharmaceutical Society of Japan</general><general>Japan Science and Technology Agency</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>2011</creationdate><title>Aglycon of Rhizochalin from the Rhizochalina incrustata Induces Apoptosis via Activation of AMP-Activated Protein Kinase in HT-29 Colon Cancer Cells</title><author>Khanal, Prem ; Kang, Bong Seok ; Yun, Hyo Jeong ; Cho, Hae-Guk ; Makarieva, Tatyana Nikolaevna ; Choi, Hong Seok</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c726t-1c591e49e390f1b81ce72d0cbf54a7dd38f5a6305ee3d1b9b7560a03629e0213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>AMP-activated protein kinase</topic><topic>AMP-Activated Protein Kinases - genetics</topic><topic>AMP-Activated Protein Kinases - metabolism</topic><topic>Animals</topic><topic>Antineoplastic Agents - metabolism</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Antineoplastic Agents - therapeutic use</topic><topic>Apoptosis - drug effects</topic><topic>c-Fos</topic><topic>c-Jun</topic><topic>Caspase 3 - metabolism</topic><topic>cell transformation</topic><topic>Cell Transformation, Neoplastic - drug effects</topic><topic>Chemoprevention</topic><topic>Colonic Neoplasms - drug therapy</topic><topic>Colonic Neoplasms - enzymology</topic><topic>Colonic Neoplasms - genetics</topic><topic>Colonic Neoplasms - pathology</topic><topic>DNA Fragmentation - drug effects</topic><topic>Drug Evaluation, Preclinical</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Fatty Alcohols - metabolism</topic><topic>Fatty Alcohols - pharmacology</topic><topic>Fatty Alcohols - therapeutic use</topic><topic>Glycosphingolipids - chemistry</topic><topic>Glycosphingolipids - metabolism</topic><topic>Glycosphingolipids - pharmacology</topic><topic>Glycosphingolipids - therapeutic use</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>Marine</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Molecular Targeted Therapy</topic><topic>Oceans and Seas</topic><topic>Phosphorylation</topic><topic>Phytotherapy</topic><topic>Plant Preparations - chemistry</topic><topic>Plant Preparations - isolation & purification</topic><topic>Plant Preparations - pharmacology</topic><topic>Poly(ADP-ribose) Polymerases - metabolism</topic><topic>Porifera</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>rhizochalin</topic><topic>Rhizochalina</topic><topic>Tetrazolium Salts</topic><topic>Thiazoles</topic><topic>TOR Serine-Threonine Kinases - genetics</topic><topic>TOR Serine-Threonine Kinases - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Khanal, Prem</creatorcontrib><creatorcontrib>Kang, Bong Seok</creatorcontrib><creatorcontrib>Yun, Hyo Jeong</creatorcontrib><creatorcontrib>Cho, Hae-Guk</creatorcontrib><creatorcontrib>Makarieva, Tatyana Nikolaevna</creatorcontrib><creatorcontrib>Choi, Hong Seok</creatorcontrib><creatorcontrib>Chosun University</creatorcontrib><creatorcontrib>bBio-Medical Research Institute</creatorcontrib><creatorcontrib>Pacific Institute of Bioorganic Chemistry of the Russian Academy of Sciences</creatorcontrib><creatorcontrib>aBK Project Team</creatorcontrib><creatorcontrib>Kyungpook National University Hospital</creatorcontrib><creatorcontrib>cLaboratory of the MaNaPro Chemistry</creatorcontrib><creatorcontrib>College of Pharmacy</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Biological & Pharmaceutical Bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khanal, Prem</au><au>Kang, Bong Seok</au><au>Yun, Hyo Jeong</au><au>Cho, Hae-Guk</au><au>Makarieva, Tatyana Nikolaevna</au><au>Choi, Hong Seok</au><aucorp>Chosun University</aucorp><aucorp>bBio-Medical Research Institute</aucorp><aucorp>Pacific Institute of Bioorganic Chemistry of the Russian Academy of Sciences</aucorp><aucorp>aBK Project Team</aucorp><aucorp>Kyungpook National University Hospital</aucorp><aucorp>cLaboratory of the MaNaPro Chemistry</aucorp><aucorp>College of Pharmacy</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aglycon of Rhizochalin from the Rhizochalina incrustata Induces Apoptosis via Activation of AMP-Activated Protein Kinase in HT-29 Colon Cancer Cells</atitle><jtitle>Biological & Pharmaceutical Bulletin</jtitle><addtitle>Biol Pharm Bull</addtitle><date>2011</date><risdate>2011</risdate><volume>34</volume><issue>10</issue><spage>1553</spage><epage>1558</epage><pages>1553-1558</pages><issn>0918-6158</issn><issn>1347-5215</issn><eissn>1347-5215</eissn><abstract>Rhizochalin is a two-headed sphingolipid-like compound isolated from the sponge Rhizochalina incrustata. It has been reported that rhizocalin and its derivates have a chemopreventive and chemotherapeutic effect. However, the molecular mechanism of these effects is not understood. Here, we demonstrate that aglycon of rhizochalin (AglRhz) from the Rhizochalina incrustata induces AMP-activated protein kinase (AMPK) phosphorylation, and thereby inhibits mammalian target of rapamycin (mTOR)-p70S6 kinase-extracellular signal-regulated kinase (ERK) signaling and activator protein 1 (AP-1) activity via phosphorylation of Raptor in HT-29 cells. In addition, AglRhz induced activation of caspase-3 and poly(ADP-ribose) polymerase (PARP), and DNA fragmentation in HT-29 cells, leads to induction of apoptosis as well as suppression of tumorigenicity of HT-29 cells. Notably, AglRhz inhibits insulin-like growth factor (IGF)-1-induced AP-1 activity and cell transformation in JB6 Cl41 cells. Overall, our findings identify AMPK as an important target protein for mediating the anti-tumor properties of AglRhz in HT-29 colon cancer cells and have important implication for sponges, the most important marine source, in colon cancer.</abstract><cop>Japan</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>21963494</pmid><doi>10.1248/bpb.34.1553</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | AMP-activated protein kinase AMP-Activated Protein Kinases - genetics AMP-Activated Protein Kinases - metabolism Animals Antineoplastic Agents - metabolism Antineoplastic Agents - pharmacology Antineoplastic Agents - therapeutic use Apoptosis - drug effects c-Fos c-Jun Caspase 3 - metabolism cell transformation Cell Transformation, Neoplastic - drug effects Chemoprevention Colonic Neoplasms - drug therapy Colonic Neoplasms - enzymology Colonic Neoplasms - genetics Colonic Neoplasms - pathology DNA Fragmentation - drug effects Drug Evaluation, Preclinical Extracellular Signal-Regulated MAP Kinases - metabolism Fatty Alcohols - metabolism Fatty Alcohols - pharmacology Fatty Alcohols - therapeutic use Glycosphingolipids - chemistry Glycosphingolipids - metabolism Glycosphingolipids - pharmacology Glycosphingolipids - therapeutic use HT29 Cells Humans Marine Mice Mitogen-Activated Protein Kinases - metabolism Molecular Targeted Therapy Oceans and Seas Phosphorylation Phytotherapy Plant Preparations - chemistry Plant Preparations - isolation & purification Plant Preparations - pharmacology Poly(ADP-ribose) Polymerases - metabolism Porifera Protein-Serine-Threonine Kinases - metabolism rhizochalin Rhizochalina Tetrazolium Salts Thiazoles TOR Serine-Threonine Kinases - genetics TOR Serine-Threonine Kinases - metabolism Tumor Cells, Cultured |
| title | Aglycon of Rhizochalin from the Rhizochalina incrustata Induces Apoptosis via Activation of AMP-Activated Protein Kinase in HT-29 Colon Cancer Cells |
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