Phosphorylation of PTEN (phosphatase and tensin homologue deleted on chromosome ten) protein is enhanced in human fibromyomatous uteri
PTEN phosphatase, a product of PTEN tumor suppressor gene, exists in cells in phosphorylated and unphosphorylated form and has a central role in regulation of PI3K/Akt signalling which is involved in non-genomic action of estradiol. The purpose of this study was to analyze the level of total PTEN an...
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| Veröffentlicht in: | The Journal of steroid biochemistry and molecular biology 2007-02, Vol.103 (2), p.196-199 |
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| creator | Kovács, Kálmán A. Lengyel, Ferenc Vértes, Zsuzsanna Környei, József L. Gőcze, Péter M. Sumegi, Balazs Szabó, István Vértes, Marietta |
| description | PTEN phosphatase, a product of PTEN tumor suppressor gene, exists in cells in phosphorylated and unphosphorylated form and has a central role in regulation of PI3K/Akt signalling which is involved in non-genomic action of estradiol. The purpose of this study was to analyze the level of total PTEN and phosphoPTEN parallel to phosphoAkt in leiomyoma and adjacent myometrium during menstrual cycle and at menopause. The expression of total PTEN in leiomyoma and myometrium did not change throughout the experiments. However, the level of phosphoPTEN was increased in leiomyoma during menstrual cycle. The phosphorylation of PTEN in myometrium was lower during secretory phase than that of proliferative phase. The phosphoAkt was abundant in leiomyoma, and its expression was higher during menstrual cycle than in myometrium. The phosphorylation of PTEN was directly related to phosphoAkt, suggesting a direct link between the inactivation of PTEN and activation of Akt. At the decline of sexual steroids, at menopause, no differences were observed in the expression of studied proteins between the two types of tissues. Our results suggest that the altered phosphorylation of PTEN protein and the consequent activation of survival signals may contribute to the pathomechanism of leiomyoma. |
| doi_str_mv | 10.1016/j.jsbmb.2006.08.006 |
| format | Article |
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The purpose of this study was to analyze the level of total PTEN and phosphoPTEN parallel to phosphoAkt in leiomyoma and adjacent myometrium during menstrual cycle and at menopause. The expression of total PTEN in leiomyoma and myometrium did not change throughout the experiments. However, the level of phosphoPTEN was increased in leiomyoma during menstrual cycle. The phosphorylation of PTEN in myometrium was lower during secretory phase than that of proliferative phase. The phosphoAkt was abundant in leiomyoma, and its expression was higher during menstrual cycle than in myometrium. The phosphorylation of PTEN was directly related to phosphoAkt, suggesting a direct link between the inactivation of PTEN and activation of Akt. At the decline of sexual steroids, at menopause, no differences were observed in the expression of studied proteins between the two types of tissues. Our results suggest that the altered phosphorylation of PTEN protein and the consequent activation of survival signals may contribute to the pathomechanism of leiomyoma.</description><identifier>ISSN: 0960-0760</identifier><identifier>EISSN: 1879-1220</identifier><identifier>DOI: 10.1016/j.jsbmb.2006.08.006</identifier><identifier>PMID: 17097286</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Adult ; Biological and medical sciences ; Case-Control Studies ; Enhanced PTEN phosphorylation ; Female ; Female genital diseases ; Gene Expression ; Gynecology. Andrology. Obstetrics ; Humans ; Impaired PTEN/Akt signalling ; Leiomyoma ; Leiomyoma - metabolism ; Medical sciences ; Middle Aged ; Non tumoral diseases ; Oncogene Protein v-akt - metabolism ; Phosphorylation ; Protein Kinases - metabolism ; PTEN Phosphohydrolase - metabolism ; Uterine Neoplasms - metabolism</subject><ispartof>The Journal of steroid biochemistry and molecular biology, 2007-02, Vol.103 (2), p.196-199</ispartof><rights>2006 Elsevier Ltd</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c453t-67a360cc83719081c5b8d3572a8f32602bd034bc1eda87cb063a71fc555a77693</citedby><cites>FETCH-LOGICAL-c453t-67a360cc83719081c5b8d3572a8f32602bd034bc1eda87cb063a71fc555a77693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S096007600600286X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18497586$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17097286$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kovács, Kálmán A.</creatorcontrib><creatorcontrib>Lengyel, Ferenc</creatorcontrib><creatorcontrib>Vértes, Zsuzsanna</creatorcontrib><creatorcontrib>Környei, József L.</creatorcontrib><creatorcontrib>Gőcze, Péter M.</creatorcontrib><creatorcontrib>Sumegi, Balazs</creatorcontrib><creatorcontrib>Szabó, István</creatorcontrib><creatorcontrib>Vértes, Marietta</creatorcontrib><title>Phosphorylation of PTEN (phosphatase and tensin homologue deleted on chromosome ten) protein is enhanced in human fibromyomatous uteri</title><title>The Journal of steroid biochemistry and molecular biology</title><addtitle>J Steroid Biochem Mol Biol</addtitle><description>PTEN phosphatase, a product of PTEN tumor suppressor gene, exists in cells in phosphorylated and unphosphorylated form and has a central role in regulation of PI3K/Akt signalling which is involved in non-genomic action of estradiol. The purpose of this study was to analyze the level of total PTEN and phosphoPTEN parallel to phosphoAkt in leiomyoma and adjacent myometrium during menstrual cycle and at menopause. The expression of total PTEN in leiomyoma and myometrium did not change throughout the experiments. However, the level of phosphoPTEN was increased in leiomyoma during menstrual cycle. The phosphorylation of PTEN in myometrium was lower during secretory phase than that of proliferative phase. The phosphoAkt was abundant in leiomyoma, and its expression was higher during menstrual cycle than in myometrium. The phosphorylation of PTEN was directly related to phosphoAkt, suggesting a direct link between the inactivation of PTEN and activation of Akt. At the decline of sexual steroids, at menopause, no differences were observed in the expression of studied proteins between the two types of tissues. Our results suggest that the altered phosphorylation of PTEN protein and the consequent activation of survival signals may contribute to the pathomechanism of leiomyoma.</description><subject>Adult</subject><subject>Biological and medical sciences</subject><subject>Case-Control Studies</subject><subject>Enhanced PTEN phosphorylation</subject><subject>Female</subject><subject>Female genital diseases</subject><subject>Gene Expression</subject><subject>Gynecology. Andrology. Obstetrics</subject><subject>Humans</subject><subject>Impaired PTEN/Akt signalling</subject><subject>Leiomyoma</subject><subject>Leiomyoma - metabolism</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>Non tumoral diseases</subject><subject>Oncogene Protein v-akt - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>PTEN Phosphohydrolase - metabolism</subject><subject>Uterine Neoplasms - metabolism</subject><issn>0960-0760</issn><issn>1879-1220</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1u1DAUhS0EotPCEyAhb0BlkXAdT2xn0QWqyo9UQRdlbTnODfEoiQfbQZoX4LlxZkbqjtWR7O9cHX2EvGFQMmDi467cxXZqywpAlKDKHM_IhinZFKyq4DnZQCOgACngglzGuAMAzpl8SS6YhEZWSmzI34fBx_3gw2E0yfmZ-p4-PN59p9f744dJJiI1c0cTztHNdPCTH_2vBWmHIybsaC7ZIeTn6CdcsQ90H3zCDLtIcR7MbDO2dpfJzLR3baYPfjLJL5EuCYN7RV70Zoz4-pxX5Ofnu8fbr8X9jy_fbj_dF3Zb81QIabgAaxWXrAHFbN2qjteyMqrnlYCq7YBvW8uwM0raFgQ3kvW2rmsjpWj4FXl_upsX_l4wJj25aHEczYx5jBaqqaGSKoP8BNrgYwzY631wkwkHzUCv-vVOH_XrVb8GpXPk1tvz-aWdsHvqnH1n4N0ZMNGasQ_ZjYtPnNo2sj5yNycOs4w_DoOO1uHq0QW0SXfe_XfIP3Ckplg</recordid><startdate>20070201</startdate><enddate>20070201</enddate><creator>Kovács, Kálmán A.</creator><creator>Lengyel, Ferenc</creator><creator>Vértes, Zsuzsanna</creator><creator>Környei, József L.</creator><creator>Gőcze, Péter M.</creator><creator>Sumegi, Balazs</creator><creator>Szabó, István</creator><creator>Vértes, Marietta</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><scope>IQODW</scope><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>7X8</scope></search><sort><creationdate>20070201</creationdate><title>Phosphorylation of PTEN (phosphatase and tensin homologue deleted on chromosome ten) protein is enhanced in human fibromyomatous uteri</title><author>Kovács, Kálmán A. ; Lengyel, Ferenc ; Vértes, Zsuzsanna ; Környei, József L. ; Gőcze, Péter M. ; Sumegi, Balazs ; Szabó, István ; Vértes, Marietta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-67a360cc83719081c5b8d3572a8f32602bd034bc1eda87cb063a71fc555a77693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adult</topic><topic>Biological and medical sciences</topic><topic>Case-Control Studies</topic><topic>Enhanced PTEN phosphorylation</topic><topic>Female</topic><topic>Female genital diseases</topic><topic>Gene Expression</topic><topic>Gynecology. Andrology. Obstetrics</topic><topic>Humans</topic><topic>Impaired PTEN/Akt signalling</topic><topic>Leiomyoma</topic><topic>Leiomyoma - metabolism</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>Non tumoral diseases</topic><topic>Oncogene Protein v-akt - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>PTEN Phosphohydrolase - metabolism</topic><topic>Uterine Neoplasms - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kovács, Kálmán A.</creatorcontrib><creatorcontrib>Lengyel, Ferenc</creatorcontrib><creatorcontrib>Vértes, Zsuzsanna</creatorcontrib><creatorcontrib>Környei, József L.</creatorcontrib><creatorcontrib>Gőcze, Péter M.</creatorcontrib><creatorcontrib>Sumegi, Balazs</creatorcontrib><creatorcontrib>Szabó, István</creatorcontrib><creatorcontrib>Vértes, Marietta</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of steroid biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kovács, Kálmán A.</au><au>Lengyel, Ferenc</au><au>Vértes, Zsuzsanna</au><au>Környei, József L.</au><au>Gőcze, Péter M.</au><au>Sumegi, Balazs</au><au>Szabó, István</au><au>Vértes, Marietta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of PTEN (phosphatase and tensin homologue deleted on chromosome ten) protein is enhanced in human fibromyomatous uteri</atitle><jtitle>The Journal of steroid biochemistry and molecular biology</jtitle><addtitle>J Steroid Biochem Mol Biol</addtitle><date>2007-02-01</date><risdate>2007</risdate><volume>103</volume><issue>2</issue><spage>196</spage><epage>199</epage><pages>196-199</pages><issn>0960-0760</issn><eissn>1879-1220</eissn><abstract>PTEN phosphatase, a product of PTEN tumor suppressor gene, exists in cells in phosphorylated and unphosphorylated form and has a central role in regulation of PI3K/Akt signalling which is involved in non-genomic action of estradiol. The purpose of this study was to analyze the level of total PTEN and phosphoPTEN parallel to phosphoAkt in leiomyoma and adjacent myometrium during menstrual cycle and at menopause. The expression of total PTEN in leiomyoma and myometrium did not change throughout the experiments. However, the level of phosphoPTEN was increased in leiomyoma during menstrual cycle. The phosphorylation of PTEN in myometrium was lower during secretory phase than that of proliferative phase. The phosphoAkt was abundant in leiomyoma, and its expression was higher during menstrual cycle than in myometrium. The phosphorylation of PTEN was directly related to phosphoAkt, suggesting a direct link between the inactivation of PTEN and activation of Akt. At the decline of sexual steroids, at menopause, no differences were observed in the expression of studied proteins between the two types of tissues. 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| ispartof | The Journal of steroid biochemistry and molecular biology, 2007-02, Vol.103 (2), p.196-199 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adult Biological and medical sciences Case-Control Studies Enhanced PTEN phosphorylation Female Female genital diseases Gene Expression Gynecology. Andrology. Obstetrics Humans Impaired PTEN/Akt signalling Leiomyoma Leiomyoma - metabolism Medical sciences Middle Aged Non tumoral diseases Oncogene Protein v-akt - metabolism Phosphorylation Protein Kinases - metabolism PTEN Phosphohydrolase - metabolism Uterine Neoplasms - metabolism |
| title | Phosphorylation of PTEN (phosphatase and tensin homologue deleted on chromosome ten) protein is enhanced in human fibromyomatous uteri |
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