Expression of matrix metalloproteinases in human glioma cell lines in the presence of IL-10
Matrix metalloproteinases have been implicated to play a vital role in glioma invasion as they degrade extracellular matrix to facilitate the subsequent migration of tumor cells into the surrounding brain tissue. The cytokine Interleukin-10 (IL-10) was detected recently in glial tumors in vivo. Expr...
Gespeichert in:
| Veröffentlicht in: | Journal of neuro-oncology 1998-11, Vol.40 (2), p.113-122 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 122 |
|---|---|
| container_issue | 2 |
| container_start_page | 113 |
| container_title | Journal of neuro-oncology |
| container_volume | 40 |
| creator | WAGNER, S STEGEN, C BOUTERFA, H HUETTNER, C KERKAU, S ROGGENDORF, W ROOSEN, K TONN, J.-C |
| description | Matrix metalloproteinases have been implicated to play a vital role in glioma invasion as they degrade extracellular matrix to facilitate the subsequent migration of tumor cells into the surrounding brain tissue. The cytokine Interleukin-10 (IL-10) was detected recently in glial tumors in vivo. Expression of specific IL-10 mRNA as well as blood serum levels of IL-10 in glioma patients increased with malignancy suggesting a functional role of IL-10 in glioma progression. Moreover, glioma cell migration in vitro was enhanced in the presence of IL-10. We therefore investigated the expression of the matrix metalloproteinases (MMPs) stromelysin-1 (MMP-3), 72-kDa collagenase (MMP-2), 92-kDa collagenase (MMP-9), matrilysin (MMP-7) and the human macrophage metalloelastase (MMP-12). In addition, a possible relation between exposure of glioma cells to IL-10 and invasiveness of these cells due to MMP expression was analyzed. Experiments with Matrigel coated Boyden chambers revealed a pronounced dose dependent effect of IL-10 on glioma invasiveness. The synthetic MMP-inhibitor Marimastat markedly reduced cell invasion in the Boyden chambers confirming the significance of MMPs in the process of invasion. Subsequently, the expression level of MMPs and the serine protease uPA was investigated in 7 glioma cell lines (U373, GaMG, U251, GHE, SNB19, U138 and D54) by RT-PCR. In all but one cell line no enhancement of MMP expression by IL-10 was detected. Matrilysin in U373 cells was the only protease found to be upregulated in the presence of IL-10 dependent on cell density. The present data suggest that IL-10 related effects on the invasive properties of the cell lines are not directly mediated by an upregulation of matrix metalloproteinase expression. |
| doi_str_mv | 10.1023/a:1006146405880 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_69137145</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2389522731</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-72be7ab6dcdf76a8edff661bb1c9c35043564bfc7be51a6cfc4df0b1316adf663</originalsourceid><addsrcrecordid>eNpdkM9LwzAAhYMoc07PnoSA4q2aNL8abzKmDgZeFAQPJUkTl5Gms2lh_vd2rHjw9A7v4-PxALjE6A6jnNyrB4wQx5RTxIoCHYEpZoJkgghyDKYIc5ExST9OwVlKG4QQFQRPwEQWMkeSTMHnYrdtbUq-ibBxsFZd63ewtp0Kodm2TWd9VMkm6CNc97WK8Cv4plbQ2BBg8PFQdWsL9x4bjd17lqsMo3Nw4lRI9mLMGXh_WrzNX7LV6_Ny_rjKDBGsy0SurVCaV6ZygqvCVs5xjrXGRhrCECWMU-2M0JZhxY0ztHJIY4K5qgaSzMDtwTvs_e5t6srap_0-FW3Tp5JLTASmbACv_4Gbpm_jsK3MSSFZng_vDNTVSPW6tlW5bX2t2p9y_Gzob8ZeJaOCa1U0Pv1hmDPCiSS_Njx7Gg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2389522731</pqid></control><display><type>article</type><title>Expression of matrix metalloproteinases in human glioma cell lines in the presence of IL-10</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>WAGNER, S ; STEGEN, C ; BOUTERFA, H ; HUETTNER, C ; KERKAU, S ; ROGGENDORF, W ; ROOSEN, K ; TONN, J.-C</creator><creatorcontrib>WAGNER, S ; STEGEN, C ; BOUTERFA, H ; HUETTNER, C ; KERKAU, S ; ROGGENDORF, W ; ROOSEN, K ; TONN, J.-C</creatorcontrib><description>Matrix metalloproteinases have been implicated to play a vital role in glioma invasion as they degrade extracellular matrix to facilitate the subsequent migration of tumor cells into the surrounding brain tissue. The cytokine Interleukin-10 (IL-10) was detected recently in glial tumors in vivo. Expression of specific IL-10 mRNA as well as blood serum levels of IL-10 in glioma patients increased with malignancy suggesting a functional role of IL-10 in glioma progression. Moreover, glioma cell migration in vitro was enhanced in the presence of IL-10. We therefore investigated the expression of the matrix metalloproteinases (MMPs) stromelysin-1 (MMP-3), 72-kDa collagenase (MMP-2), 92-kDa collagenase (MMP-9), matrilysin (MMP-7) and the human macrophage metalloelastase (MMP-12). In addition, a possible relation between exposure of glioma cells to IL-10 and invasiveness of these cells due to MMP expression was analyzed. Experiments with Matrigel coated Boyden chambers revealed a pronounced dose dependent effect of IL-10 on glioma invasiveness. The synthetic MMP-inhibitor Marimastat markedly reduced cell invasion in the Boyden chambers confirming the significance of MMPs in the process of invasion. Subsequently, the expression level of MMPs and the serine protease uPA was investigated in 7 glioma cell lines (U373, GaMG, U251, GHE, SNB19, U138 and D54) by RT-PCR. In all but one cell line no enhancement of MMP expression by IL-10 was detected. Matrilysin in U373 cells was the only protease found to be upregulated in the presence of IL-10 dependent on cell density. The present data suggest that IL-10 related effects on the invasive properties of the cell lines are not directly mediated by an upregulation of matrix metalloproteinase expression.</description><identifier>ISSN: 0167-594X</identifier><identifier>EISSN: 1573-7373</identifier><identifier>DOI: 10.1023/a:1006146405880</identifier><identifier>PMID: 9892093</identifier><identifier>CODEN: JNODD2</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Biological and medical sciences ; Brain Neoplasms - drug therapy ; Brain Neoplasms - enzymology ; Brain Neoplasms - pathology ; Brain tumors ; Cell adhesion & migration ; Cell density ; Cell Line ; Collagen ; Collagenase ; Endopeptidases - biosynthesis ; Endopeptidases - isolation & purification ; Extracellular matrix ; Extracellular Matrix - drug effects ; Extracellular Matrix - enzymology ; Gelatinase A ; Gelatinase B ; Gene expression ; Glioma ; Glioma - drug therapy ; Glioma - enzymology ; Glioma - pathology ; Glioma cells ; Humans ; Interleukin 10 ; Interleukin-10 - pharmacology ; Invasiveness ; Leukocyte migration ; Macrophages ; Malignancy ; Matrilysin ; Matrix metalloproteinase ; Medical sciences ; Metalloendopeptidases - biosynthesis ; Metalloendopeptidases - metabolism ; Metalloproteinase ; mRNA ; Neurology ; Polymerase chain reaction ; Recombinant Proteins - pharmacology ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - biosynthesis ; RNA, Neoplasm - biosynthesis ; Serine ; Serine proteinase ; Serum levels ; Stromelysin ; Tumor cells ; Tumors of the nervous system. Phacomatoses</subject><ispartof>Journal of neuro-oncology, 1998-11, Vol.40 (2), p.113-122</ispartof><rights>1999 INIST-CNRS</rights><rights>Kluwer Academic Publishers 1998.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-72be7ab6dcdf76a8edff661bb1c9c35043564bfc7be51a6cfc4df0b1316adf663</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1653639$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9892093$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>WAGNER, S</creatorcontrib><creatorcontrib>STEGEN, C</creatorcontrib><creatorcontrib>BOUTERFA, H</creatorcontrib><creatorcontrib>HUETTNER, C</creatorcontrib><creatorcontrib>KERKAU, S</creatorcontrib><creatorcontrib>ROGGENDORF, W</creatorcontrib><creatorcontrib>ROOSEN, K</creatorcontrib><creatorcontrib>TONN, J.-C</creatorcontrib><title>Expression of matrix metalloproteinases in human glioma cell lines in the presence of IL-10</title><title>Journal of neuro-oncology</title><addtitle>J Neurooncol</addtitle><description>Matrix metalloproteinases have been implicated to play a vital role in glioma invasion as they degrade extracellular matrix to facilitate the subsequent migration of tumor cells into the surrounding brain tissue. The cytokine Interleukin-10 (IL-10) was detected recently in glial tumors in vivo. Expression of specific IL-10 mRNA as well as blood serum levels of IL-10 in glioma patients increased with malignancy suggesting a functional role of IL-10 in glioma progression. Moreover, glioma cell migration in vitro was enhanced in the presence of IL-10. We therefore investigated the expression of the matrix metalloproteinases (MMPs) stromelysin-1 (MMP-3), 72-kDa collagenase (MMP-2), 92-kDa collagenase (MMP-9), matrilysin (MMP-7) and the human macrophage metalloelastase (MMP-12). In addition, a possible relation between exposure of glioma cells to IL-10 and invasiveness of these cells due to MMP expression was analyzed. Experiments with Matrigel coated Boyden chambers revealed a pronounced dose dependent effect of IL-10 on glioma invasiveness. The synthetic MMP-inhibitor Marimastat markedly reduced cell invasion in the Boyden chambers confirming the significance of MMPs in the process of invasion. Subsequently, the expression level of MMPs and the serine protease uPA was investigated in 7 glioma cell lines (U373, GaMG, U251, GHE, SNB19, U138 and D54) by RT-PCR. In all but one cell line no enhancement of MMP expression by IL-10 was detected. Matrilysin in U373 cells was the only protease found to be upregulated in the presence of IL-10 dependent on cell density. The present data suggest that IL-10 related effects on the invasive properties of the cell lines are not directly mediated by an upregulation of matrix metalloproteinase expression.</description><subject>Biological and medical sciences</subject><subject>Brain Neoplasms - drug therapy</subject><subject>Brain Neoplasms - enzymology</subject><subject>Brain Neoplasms - pathology</subject><subject>Brain tumors</subject><subject>Cell adhesion & migration</subject><subject>Cell density</subject><subject>Cell Line</subject><subject>Collagen</subject><subject>Collagenase</subject><subject>Endopeptidases - biosynthesis</subject><subject>Endopeptidases - isolation & purification</subject><subject>Extracellular matrix</subject><subject>Extracellular Matrix - drug effects</subject><subject>Extracellular Matrix - enzymology</subject><subject>Gelatinase A</subject><subject>Gelatinase B</subject><subject>Gene expression</subject><subject>Glioma</subject><subject>Glioma - drug therapy</subject><subject>Glioma - enzymology</subject><subject>Glioma - pathology</subject><subject>Glioma cells</subject><subject>Humans</subject><subject>Interleukin 10</subject><subject>Interleukin-10 - pharmacology</subject><subject>Invasiveness</subject><subject>Leukocyte migration</subject><subject>Macrophages</subject><subject>Malignancy</subject><subject>Matrilysin</subject><subject>Matrix metalloproteinase</subject><subject>Medical sciences</subject><subject>Metalloendopeptidases - biosynthesis</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Metalloproteinase</subject><subject>mRNA</subject><subject>Neurology</subject><subject>Polymerase chain reaction</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA, Neoplasm - biosynthesis</subject><subject>Serine</subject><subject>Serine proteinase</subject><subject>Serum levels</subject><subject>Stromelysin</subject><subject>Tumor cells</subject><subject>Tumors of the nervous system. Phacomatoses</subject><issn>0167-594X</issn><issn>1573-7373</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNpdkM9LwzAAhYMoc07PnoSA4q2aNL8abzKmDgZeFAQPJUkTl5Gms2lh_vd2rHjw9A7v4-PxALjE6A6jnNyrB4wQx5RTxIoCHYEpZoJkgghyDKYIc5ExST9OwVlKG4QQFQRPwEQWMkeSTMHnYrdtbUq-ibBxsFZd63ewtp0Kodm2TWd9VMkm6CNc97WK8Cv4plbQ2BBg8PFQdWsL9x4bjd17lqsMo3Nw4lRI9mLMGXh_WrzNX7LV6_Ny_rjKDBGsy0SurVCaV6ZygqvCVs5xjrXGRhrCECWMU-2M0JZhxY0ztHJIY4K5qgaSzMDtwTvs_e5t6srap_0-FW3Tp5JLTASmbACv_4Gbpm_jsK3MSSFZng_vDNTVSPW6tlW5bX2t2p9y_Gzob8ZeJaOCa1U0Pv1hmDPCiSS_Njx7Gg</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>WAGNER, S</creator><creator>STEGEN, C</creator><creator>BOUTERFA, H</creator><creator>HUETTNER, C</creator><creator>KERKAU, S</creator><creator>ROGGENDORF, W</creator><creator>ROOSEN, K</creator><creator>TONN, J.-C</creator><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Expression of matrix metalloproteinases in human glioma cell lines in the presence of IL-10</title><author>WAGNER, S ; STEGEN, C ; BOUTERFA, H ; HUETTNER, C ; KERKAU, S ; ROGGENDORF, W ; ROOSEN, K ; TONN, J.-C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-72be7ab6dcdf76a8edff661bb1c9c35043564bfc7be51a6cfc4df0b1316adf663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Biological and medical sciences</topic><topic>Brain Neoplasms - drug therapy</topic><topic>Brain Neoplasms - enzymology</topic><topic>Brain Neoplasms - pathology</topic><topic>Brain tumors</topic><topic>Cell adhesion & migration</topic><topic>Cell density</topic><topic>Cell Line</topic><topic>Collagen</topic><topic>Collagenase</topic><topic>Endopeptidases - biosynthesis</topic><topic>Endopeptidases - isolation & purification</topic><topic>Extracellular matrix</topic><topic>Extracellular Matrix - drug effects</topic><topic>Extracellular Matrix - enzymology</topic><topic>Gelatinase A</topic><topic>Gelatinase B</topic><topic>Gene expression</topic><topic>Glioma</topic><topic>Glioma - drug therapy</topic><topic>Glioma - enzymology</topic><topic>Glioma - pathology</topic><topic>Glioma cells</topic><topic>Humans</topic><topic>Interleukin 10</topic><topic>Interleukin-10 - pharmacology</topic><topic>Invasiveness</topic><topic>Leukocyte migration</topic><topic>Macrophages</topic><topic>Malignancy</topic><topic>Matrilysin</topic><topic>Matrix metalloproteinase</topic><topic>Medical sciences</topic><topic>Metalloendopeptidases - biosynthesis</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Metalloproteinase</topic><topic>mRNA</topic><topic>Neurology</topic><topic>Polymerase chain reaction</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - biosynthesis</topic><topic>RNA, Neoplasm - biosynthesis</topic><topic>Serine</topic><topic>Serine proteinase</topic><topic>Serum levels</topic><topic>Stromelysin</topic><topic>Tumor cells</topic><topic>Tumors of the nervous system. Phacomatoses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WAGNER, S</creatorcontrib><creatorcontrib>STEGEN, C</creatorcontrib><creatorcontrib>BOUTERFA, H</creatorcontrib><creatorcontrib>HUETTNER, C</creatorcontrib><creatorcontrib>KERKAU, S</creatorcontrib><creatorcontrib>ROGGENDORF, W</creatorcontrib><creatorcontrib>ROOSEN, K</creatorcontrib><creatorcontrib>TONN, J.-C</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>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</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</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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>MEDLINE - Academic</collection><jtitle>Journal of neuro-oncology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WAGNER, S</au><au>STEGEN, C</au><au>BOUTERFA, H</au><au>HUETTNER, C</au><au>KERKAU, S</au><au>ROGGENDORF, W</au><au>ROOSEN, K</au><au>TONN, J.-C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of matrix metalloproteinases in human glioma cell lines in the presence of IL-10</atitle><jtitle>Journal of neuro-oncology</jtitle><addtitle>J Neurooncol</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>40</volume><issue>2</issue><spage>113</spage><epage>122</epage><pages>113-122</pages><issn>0167-594X</issn><eissn>1573-7373</eissn><coden>JNODD2</coden><abstract>Matrix metalloproteinases have been implicated to play a vital role in glioma invasion as they degrade extracellular matrix to facilitate the subsequent migration of tumor cells into the surrounding brain tissue. The cytokine Interleukin-10 (IL-10) was detected recently in glial tumors in vivo. Expression of specific IL-10 mRNA as well as blood serum levels of IL-10 in glioma patients increased with malignancy suggesting a functional role of IL-10 in glioma progression. Moreover, glioma cell migration in vitro was enhanced in the presence of IL-10. We therefore investigated the expression of the matrix metalloproteinases (MMPs) stromelysin-1 (MMP-3), 72-kDa collagenase (MMP-2), 92-kDa collagenase (MMP-9), matrilysin (MMP-7) and the human macrophage metalloelastase (MMP-12). In addition, a possible relation between exposure of glioma cells to IL-10 and invasiveness of these cells due to MMP expression was analyzed. Experiments with Matrigel coated Boyden chambers revealed a pronounced dose dependent effect of IL-10 on glioma invasiveness. The synthetic MMP-inhibitor Marimastat markedly reduced cell invasion in the Boyden chambers confirming the significance of MMPs in the process of invasion. Subsequently, the expression level of MMPs and the serine protease uPA was investigated in 7 glioma cell lines (U373, GaMG, U251, GHE, SNB19, U138 and D54) by RT-PCR. In all but one cell line no enhancement of MMP expression by IL-10 was detected. Matrilysin in U373 cells was the only protease found to be upregulated in the presence of IL-10 dependent on cell density. The present data suggest that IL-10 related effects on the invasive properties of the cell lines are not directly mediated by an upregulation of matrix metalloproteinase expression.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>9892093</pmid><doi>10.1023/a:1006146405880</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0167-594X |
| ispartof | Journal of neuro-oncology, 1998-11, Vol.40 (2), p.113-122 |
| issn | 0167-594X 1573-7373 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69137145 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Biological and medical sciences Brain Neoplasms - drug therapy Brain Neoplasms - enzymology Brain Neoplasms - pathology Brain tumors Cell adhesion & migration Cell density Cell Line Collagen Collagenase Endopeptidases - biosynthesis Endopeptidases - isolation & purification Extracellular matrix Extracellular Matrix - drug effects Extracellular Matrix - enzymology Gelatinase A Gelatinase B Gene expression Glioma Glioma - drug therapy Glioma - enzymology Glioma - pathology Glioma cells Humans Interleukin 10 Interleukin-10 - pharmacology Invasiveness Leukocyte migration Macrophages Malignancy Matrilysin Matrix metalloproteinase Medical sciences Metalloendopeptidases - biosynthesis Metalloendopeptidases - metabolism Metalloproteinase mRNA Neurology Polymerase chain reaction Recombinant Proteins - pharmacology Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - biosynthesis RNA, Neoplasm - biosynthesis Serine Serine proteinase Serum levels Stromelysin Tumor cells Tumors of the nervous system. Phacomatoses |
| title | Expression of matrix metalloproteinases in human glioma cell lines in the presence of IL-10 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T10%3A01%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Expression%20of%20matrix%20metalloproteinases%20in%20human%20glioma%20cell%20lines%20in%20the%20presence%20of%20IL-10&rft.jtitle=Journal%20of%20neuro-oncology&rft.au=WAGNER,%20S&rft.date=1998-11-01&rft.volume=40&rft.issue=2&rft.spage=113&rft.epage=122&rft.pages=113-122&rft.issn=0167-594X&rft.eissn=1573-7373&rft.coden=JNODD2&rft_id=info:doi/10.1023/a:1006146405880&rft_dat=%3Cproquest_pubme%3E2389522731%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2389522731&rft_id=info:pmid/9892093&rfr_iscdi=true |