Differential effects of transforming growth factor on cell cycle regulatory molecules in human myeloid leukemia cells
In this report we have studied the mechanism by which Transforming Growth Factor beta (TGF beta) inhibits growth of human myeloid leukemia cell lines. TGF beta 1 arrested cells in G1 phase and significantly downregulated the expression of cyclin D2, cyclin D3, cdk4, cyclin A, and cdk2. The downregul...
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| Veröffentlicht in: | Oncogene 2001-10, Vol.20 (47), p.6840-6850 |
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| creator | XIAOTANG HU XIAOHONG ZHANG QING ZHONG FISHER, Ariana B BRYINGTON, Matthew ZUCKERMAN, Kenneth S |
| description | In this report we have studied the mechanism by which Transforming Growth Factor beta (TGF beta) inhibits growth of human myeloid leukemia cell lines. TGF beta 1 arrested cells in G1 phase and significantly downregulated the expression of cyclin D2, cyclin D3, cdk4, cyclin A, and cdk2. The downregulation of the molecules resulted in approximately 50-90% decrease of the molecule-dependent kinase activity, varying with each molecule. Although treatment of cells with TGF beta 1 up-regulated accumulation of p27(kip1) in both nucleus and cytoplasm, the association of the p27(kip1) with cdk2, cyclin A, cyclin D2, cyclin D3, and cdk4 was markedly down-regulated, suggesting that p27(kip1) is not responsible for the downregulation of the kinase activity. In contrast, TGF beta 1 upregulated cyclin E-associated p27(kip1) with no effect on the expression of cyclin E. p27(kip1)-immunodepletion upregulated cyclin E-dependent kinase activity by more than 10-fold in TGF beta 1-treated cells but not in proliferating cells; whereas immunodepletion of p27(kip1) from cdk2-immunoprecipitates markedly downregulated cdk2 kinase activity in the lysates extracted from both proliferating and TGF beta-treated cells. Consistent with this observation, TGF beta 1 and p27(kip1) antisense cDNA had a synergistic or additive inhibitory effect on cdk2 but not cyclin E-dependent kinase activity. Our data suggest that (1) TGF beta 1-mediated growth inhibition is accomplished through multiple pathways and (2) p27(kip1) has opposing effects on cdk2 and cyclin E activity in response to TGF beta 1. |
| doi_str_mv | 10.1038/sj.onc.1204790 |
| format | Article |
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TGF beta 1 arrested cells in G1 phase and significantly downregulated the expression of cyclin D2, cyclin D3, cdk4, cyclin A, and cdk2. The downregulation of the molecules resulted in approximately 50-90% decrease of the molecule-dependent kinase activity, varying with each molecule. Although treatment of cells with TGF beta 1 up-regulated accumulation of p27(kip1) in both nucleus and cytoplasm, the association of the p27(kip1) with cdk2, cyclin A, cyclin D2, cyclin D3, and cdk4 was markedly down-regulated, suggesting that p27(kip1) is not responsible for the downregulation of the kinase activity. In contrast, TGF beta 1 upregulated cyclin E-associated p27(kip1) with no effect on the expression of cyclin E. p27(kip1)-immunodepletion upregulated cyclin E-dependent kinase activity by more than 10-fold in TGF beta 1-treated cells but not in proliferating cells; whereas immunodepletion of p27(kip1) from cdk2-immunoprecipitates markedly downregulated cdk2 kinase activity in the lysates extracted from both proliferating and TGF beta-treated cells. Consistent with this observation, TGF beta 1 and p27(kip1) antisense cDNA had a synergistic or additive inhibitory effect on cdk2 but not cyclin E-dependent kinase activity. Our data suggest that (1) TGF beta 1-mediated growth inhibition is accomplished through multiple pathways and (2) p27(kip1) has opposing effects on cdk2 and cyclin E activity in response to TGF beta 1.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/sj.onc.1204790</identifier><identifier>PMID: 11687963</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>Basingstoke: Nature Publishing</publisher><subject>Antisense DNA ; Biological and medical sciences ; Cancer ; CDC2-CDC28 Kinases ; Cell cycle ; Cell Cycle Proteins - metabolism ; Cell Cycle Proteins - physiology ; Cell cycle, cell proliferation ; Cell Division ; Cell physiology ; Cyclin A ; Cyclin D ; Cyclin D2 ; Cyclin D3 ; Cyclin E ; Cyclin E - antagonists & inhibitors ; Cyclin E - metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases - antagonists & inhibitors ; Cyclin-Dependent Kinases - biosynthesis ; Cyclin-Dependent Kinases - metabolism ; Cyclins - metabolism ; Cytoplasm ; Down-Regulation ; Fundamental and applied biological sciences. Psychology ; G1 Phase ; Growth factors ; Humans ; Kinases ; kip1 gene ; Leukemia ; Leukemia, Myeloid - metabolism ; Leukemia, Myeloid - pathology ; Lysates ; Molecular and cellular biology ; Myeloid leukemia ; Oncology ; p27 protein ; Phosphorylation ; Protein-Serine-Threonine Kinases - antagonists & inhibitors ; Protein-Serine-Threonine Kinases - biosynthesis ; Proteins ; Proto-Oncogene Proteins ; Research centers ; Retinoblastoma Protein - metabolism ; Transforming Growth Factor beta - pharmacology ; Transforming Growth Factor beta1 ; Transforming growth factor-b ; Transforming growth factor-b1 ; Tumor cell lines ; Tumor Cells, Cultured ; Tumor Suppressor Proteins - physiology</subject><ispartof>Oncogene, 2001-10, Vol.20 (47), p.6840-6850</ispartof><rights>2002 INIST-CNRS</rights><rights>Copyright Nature Publishing Group Oct 18, 2001</rights><rights>Macmillan Publishers Limited 2001.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c407t-72be3e5f627a69bcb66022e82ca1328c3b8bbe9db36b7eb850ef589417ca19683</citedby><cites>FETCH-LOGICAL-c407t-72be3e5f627a69bcb66022e82ca1328c3b8bbe9db36b7eb850ef589417ca19683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14154204$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11687963$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>XIAOTANG HU</creatorcontrib><creatorcontrib>XIAOHONG ZHANG</creatorcontrib><creatorcontrib>QING ZHONG</creatorcontrib><creatorcontrib>FISHER, Ariana B</creatorcontrib><creatorcontrib>BRYINGTON, Matthew</creatorcontrib><creatorcontrib>ZUCKERMAN, Kenneth S</creatorcontrib><title>Differential effects of transforming growth factor on cell cycle regulatory molecules in human myeloid leukemia cells</title><title>Oncogene</title><addtitle>Oncogene</addtitle><description>In this report we have studied the mechanism by which Transforming Growth Factor beta (TGF beta) inhibits growth of human myeloid leukemia cell lines. TGF beta 1 arrested cells in G1 phase and significantly downregulated the expression of cyclin D2, cyclin D3, cdk4, cyclin A, and cdk2. The downregulation of the molecules resulted in approximately 50-90% decrease of the molecule-dependent kinase activity, varying with each molecule. Although treatment of cells with TGF beta 1 up-regulated accumulation of p27(kip1) in both nucleus and cytoplasm, the association of the p27(kip1) with cdk2, cyclin A, cyclin D2, cyclin D3, and cdk4 was markedly down-regulated, suggesting that p27(kip1) is not responsible for the downregulation of the kinase activity. In contrast, TGF beta 1 upregulated cyclin E-associated p27(kip1) with no effect on the expression of cyclin E. p27(kip1)-immunodepletion upregulated cyclin E-dependent kinase activity by more than 10-fold in TGF beta 1-treated cells but not in proliferating cells; whereas immunodepletion of p27(kip1) from cdk2-immunoprecipitates markedly downregulated cdk2 kinase activity in the lysates extracted from both proliferating and TGF beta-treated cells. Consistent with this observation, TGF beta 1 and p27(kip1) antisense cDNA had a synergistic or additive inhibitory effect on cdk2 but not cyclin E-dependent kinase activity. Our data suggest that (1) TGF beta 1-mediated growth inhibition is accomplished through multiple pathways and (2) p27(kip1) has opposing effects on cdk2 and cyclin E activity in response to TGF beta 1.</description><subject>Antisense DNA</subject><subject>Biological and medical sciences</subject><subject>Cancer</subject><subject>CDC2-CDC28 Kinases</subject><subject>Cell cycle</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Cycle Proteins - physiology</subject><subject>Cell cycle, cell proliferation</subject><subject>Cell Division</subject><subject>Cell physiology</subject><subject>Cyclin A</subject><subject>Cyclin D</subject><subject>Cyclin D2</subject><subject>Cyclin D3</subject><subject>Cyclin E</subject><subject>Cyclin E - antagonists & inhibitors</subject><subject>Cyclin E - metabolism</subject><subject>Cyclin-Dependent Kinase 2</subject><subject>Cyclin-Dependent Kinase 4</subject><subject>Cyclin-Dependent Kinase Inhibitor p27</subject><subject>Cyclin-Dependent Kinases - antagonists & inhibitors</subject><subject>Cyclin-Dependent Kinases - biosynthesis</subject><subject>Cyclin-Dependent Kinases - metabolism</subject><subject>Cyclins - metabolism</subject><subject>Cytoplasm</subject><subject>Down-Regulation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>G1 Phase</subject><subject>Growth factors</subject><subject>Humans</subject><subject>Kinases</subject><subject>kip1 gene</subject><subject>Leukemia</subject><subject>Leukemia, Myeloid - metabolism</subject><subject>Leukemia, Myeloid - pathology</subject><subject>Lysates</subject><subject>Molecular and cellular biology</subject><subject>Myeloid leukemia</subject><subject>Oncology</subject><subject>p27 protein</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - antagonists & inhibitors</subject><subject>Protein-Serine-Threonine Kinases - biosynthesis</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins</subject><subject>Research centers</subject><subject>Retinoblastoma Protein - metabolism</subject><subject>Transforming Growth Factor beta - pharmacology</subject><subject>Transforming Growth Factor beta1</subject><subject>Transforming growth factor-b</subject><subject>Transforming growth factor-b1</subject><subject>Tumor cell lines</subject><subject>Tumor Cells, Cultured</subject><subject>Tumor Suppressor Proteins - physiology</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0c1rFDEYBvAgFrtWrx4lKHqbNR8z-ThK_SoUetFzSLJvtlkzk5rMIPvfN2sHCoJ4Sgi_9yEvD0KvKNlSwtWHetjmyW8pI73U5Ana0F6Kbhh0_xRtiB5Ipxln5-h5rQdCSDPsGTqnVCipBd-g5VMMAQpMc7QJQ7v7ueIc8FzsVEMuY5z2eF_y7_kWB-vnXHCesIeUsD_6BLjAfkm2vR_xmBP4JUHFccK3y2gnPB4h5bjDCZafMEb7Z7K-QGfBpgov1_MC_fjy-fvlt-765uvV5cfrzvdEzp1kDjgMQTBphXbeCUEYA8W8pZwpz51yDvTOceEkODUQCIPSPZUNaKH4BXr_kHtX8q8F6mzGWE8_sBPkpRrJWM8lZ_-FVDHGlDwlvv0LHvJSpraEYaKnnCqqZFNv_qmY5EQM-hS1fUC-5FoLBHNX4mjL0VBiTuWaejCtXLOW2wZer6mLG2H3yNc2G3i3Alu9TaFV6GN9dD0d-pbF7wE2Tq5P</recordid><startdate>20011018</startdate><enddate>20011018</enddate><creator>XIAOTANG HU</creator><creator>XIAOHONG ZHANG</creator><creator>QING ZHONG</creator><creator>FISHER, Ariana B</creator><creator>BRYINGTON, Matthew</creator><creator>ZUCKERMAN, Kenneth S</creator><general>Nature Publishing</general><general>Nature Publishing Group</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>3V.</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</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>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20011018</creationdate><title>Differential effects of transforming growth factor on cell cycle regulatory molecules in human myeloid leukemia cells</title><author>XIAOTANG HU ; XIAOHONG ZHANG ; QING ZHONG ; FISHER, Ariana B ; BRYINGTON, Matthew ; ZUCKERMAN, Kenneth S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c407t-72be3e5f627a69bcb66022e82ca1328c3b8bbe9db36b7eb850ef589417ca19683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Antisense DNA</topic><topic>Biological and medical sciences</topic><topic>Cancer</topic><topic>CDC2-CDC28 Kinases</topic><topic>Cell cycle</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell Cycle Proteins - physiology</topic><topic>Cell cycle, cell proliferation</topic><topic>Cell Division</topic><topic>Cell physiology</topic><topic>Cyclin A</topic><topic>Cyclin D</topic><topic>Cyclin D2</topic><topic>Cyclin D3</topic><topic>Cyclin E</topic><topic>Cyclin E - antagonists & inhibitors</topic><topic>Cyclin E - metabolism</topic><topic>Cyclin-Dependent Kinase 2</topic><topic>Cyclin-Dependent Kinase 4</topic><topic>Cyclin-Dependent Kinase Inhibitor p27</topic><topic>Cyclin-Dependent Kinases - antagonists & inhibitors</topic><topic>Cyclin-Dependent Kinases - biosynthesis</topic><topic>Cyclin-Dependent Kinases - metabolism</topic><topic>Cyclins - metabolism</topic><topic>Cytoplasm</topic><topic>Down-Regulation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>G1 Phase</topic><topic>Growth factors</topic><topic>Humans</topic><topic>Kinases</topic><topic>kip1 gene</topic><topic>Leukemia</topic><topic>Leukemia, Myeloid - metabolism</topic><topic>Leukemia, Myeloid - pathology</topic><topic>Lysates</topic><topic>Molecular and cellular biology</topic><topic>Myeloid leukemia</topic><topic>Oncology</topic><topic>p27 protein</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - antagonists & inhibitors</topic><topic>Protein-Serine-Threonine Kinases - biosynthesis</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins</topic><topic>Research centers</topic><topic>Retinoblastoma Protein - metabolism</topic><topic>Transforming Growth Factor beta - pharmacology</topic><topic>Transforming Growth Factor beta1</topic><topic>Transforming growth factor-b</topic><topic>Transforming growth factor-b1</topic><topic>Tumor cell lines</topic><topic>Tumor Cells, Cultured</topic><topic>Tumor Suppressor Proteins - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>XIAOTANG HU</creatorcontrib><creatorcontrib>XIAOHONG ZHANG</creatorcontrib><creatorcontrib>QING ZHONG</creatorcontrib><creatorcontrib>FISHER, Ariana B</creatorcontrib><creatorcontrib>BRYINGTON, Matthew</creatorcontrib><creatorcontrib>ZUCKERMAN, Kenneth S</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>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</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>Public Health Database</collection><collection>Technology Research Database</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>Research Library (Alumni Edition)</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>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</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><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>XIAOTANG HU</au><au>XIAOHONG ZHANG</au><au>QING ZHONG</au><au>FISHER, Ariana B</au><au>BRYINGTON, Matthew</au><au>ZUCKERMAN, Kenneth S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential effects of transforming growth factor on cell cycle regulatory molecules in human myeloid leukemia cells</atitle><jtitle>Oncogene</jtitle><addtitle>Oncogene</addtitle><date>2001-10-18</date><risdate>2001</risdate><volume>20</volume><issue>47</issue><spage>6840</spage><epage>6850</epage><pages>6840-6850</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><coden>ONCNES</coden><abstract>In this report we have studied the mechanism by which Transforming Growth Factor beta (TGF beta) inhibits growth of human myeloid leukemia cell lines. TGF beta 1 arrested cells in G1 phase and significantly downregulated the expression of cyclin D2, cyclin D3, cdk4, cyclin A, and cdk2. The downregulation of the molecules resulted in approximately 50-90% decrease of the molecule-dependent kinase activity, varying with each molecule. Although treatment of cells with TGF beta 1 up-regulated accumulation of p27(kip1) in both nucleus and cytoplasm, the association of the p27(kip1) with cdk2, cyclin A, cyclin D2, cyclin D3, and cdk4 was markedly down-regulated, suggesting that p27(kip1) is not responsible for the downregulation of the kinase activity. In contrast, TGF beta 1 upregulated cyclin E-associated p27(kip1) with no effect on the expression of cyclin E. p27(kip1)-immunodepletion upregulated cyclin E-dependent kinase activity by more than 10-fold in TGF beta 1-treated cells but not in proliferating cells; whereas immunodepletion of p27(kip1) from cdk2-immunoprecipitates markedly downregulated cdk2 kinase activity in the lysates extracted from both proliferating and TGF beta-treated cells. Consistent with this observation, TGF beta 1 and p27(kip1) antisense cDNA had a synergistic or additive inhibitory effect on cdk2 but not cyclin E-dependent kinase activity. Our data suggest that (1) TGF beta 1-mediated growth inhibition is accomplished through multiple pathways and (2) p27(kip1) has opposing effects on cdk2 and cyclin E activity in response to TGF beta 1.</abstract><cop>Basingstoke</cop><pub>Nature Publishing</pub><pmid>11687963</pmid><doi>10.1038/sj.onc.1204790</doi><tpages>11</tpages></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Antisense DNA Biological and medical sciences Cancer CDC2-CDC28 Kinases Cell cycle Cell Cycle Proteins - metabolism Cell Cycle Proteins - physiology Cell cycle, cell proliferation Cell Division Cell physiology Cyclin A Cyclin D Cyclin D2 Cyclin D3 Cyclin E Cyclin E - antagonists & inhibitors Cyclin E - metabolism Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinase 4 Cyclin-Dependent Kinase Inhibitor p27 Cyclin-Dependent Kinases - antagonists & inhibitors Cyclin-Dependent Kinases - biosynthesis Cyclin-Dependent Kinases - metabolism Cyclins - metabolism Cytoplasm Down-Regulation Fundamental and applied biological sciences. Psychology G1 Phase Growth factors Humans Kinases kip1 gene Leukemia Leukemia, Myeloid - metabolism Leukemia, Myeloid - pathology Lysates Molecular and cellular biology Myeloid leukemia Oncology p27 protein Phosphorylation Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - biosynthesis Proteins Proto-Oncogene Proteins Research centers Retinoblastoma Protein - metabolism Transforming Growth Factor beta - pharmacology Transforming Growth Factor beta1 Transforming growth factor-b Transforming growth factor-b1 Tumor cell lines Tumor Cells, Cultured Tumor Suppressor Proteins - physiology |
| title | Differential effects of transforming growth factor on cell cycle regulatory molecules in human myeloid leukemia cells |
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