Retinoic Acid Alters the Mechanism of Attachment of Malignant Astrocytoma and Neuroblastoma Cells to Thrombospondin-1
Based on the hypothesis that the attachment of neuroectodermal cells to thrombospondin-1 (TSP-1) may affect tumor spread and play a role in the anti-tumor effects of retinoic acid, we investigated the expression of TSP-1 in these cellsin situand the effect of retinoic acid on the morphology of TSP-1...
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| Veröffentlicht in: | Experimental cell research 1999-05, Vol.249 (1), p.86-101 |
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| creator | Pijuan-Thompson, Vivian Grammer, J.Robert Stewart, Jerry Silverstein, Roy L. Pearce, S.Frieda Tuszynski, George P. Murphy-Ullrich, Joanne E. Gladson, Candece L. |
| description | Based on the hypothesis that the attachment of neuroectodermal cells to thrombospondin-1 (TSP-1) may affect tumor spread and play a role in the anti-tumor effects of retinoic acid, we investigated the expression of TSP-1 in these cellsin situand the effect of retinoic acid on the morphology of TSP-1-adherent neuroblastoma (SK-N-SH) and malignant astrocytoma (U-251MG) cellsin vitro.TSP-1-adherent SK-N-SH cells demonstrated process outgrowth, with further neuronal differentiation after retinoic acid treatment, consistent with thein situstudies showing that TSP-1 expression occurs in a differentiation-specific manner in neuroblastic tumors. TSP-1-adherent U-251MG cells failed to spread; however, after retinoic acid treatment the cells demonstrated broad lamellipodia containing radial actin fibers and organization of integrins α3β1 and α5β1 in clusters in lamellipodia and filopodia. The attachment of both SK-N-SH and U-251MG cells to TSP-1 was found to be mediated by heparan sulfate proteoglycans, integrins, and the CLESH-1 adhesion domain first identified in CD36. Heparin and heparitinase treatment inhibited TSP-1 attachment. Integrins α3β1 and α5β1 mediated TSP-1 attachment of SK-N-SH cells, and integrins α3β1, α5β1, and αvβ3 mediated TSP-1 attachment of U-251MG cells. Attachment was dependent on the RGD sequence which is located in the carboxy-terminus of TSP-1. Treatment with a pharmacologic dosage of retinoic acid altered the TSP-1 cell adhesion mechanism in both cell lines in that neither heparin nor micromolar concentrations of the RGD peptide inhibited attachment; after treatment, attachment was inhibited by the CSVTCG peptide located in the type I repeat domain of TSP-1 and a recombinant adhesion domain (CLESH-1) from CD36. Expression of CD36 was found in the retinoic acid-treated U-251MG cells. These data indicate that neuroectodermally derived cells utilize several mechanisms to attach to TSP-1, and these are differentially modulated by treatment with retinoic acid. These data also suggest that the CSVTCG sequence of TSP-1 modulates or directs cytoskeletal organization in neuroblastoma and astrocytoma cells. |
| doi_str_mv | 10.1006/excr.1999.4458 |
| format | Article |
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TSP-1-adherent U-251MG cells failed to spread; however, after retinoic acid treatment the cells demonstrated broad lamellipodia containing radial actin fibers and organization of integrins α3β1 and α5β1 in clusters in lamellipodia and filopodia. The attachment of both SK-N-SH and U-251MG cells to TSP-1 was found to be mediated by heparan sulfate proteoglycans, integrins, and the CLESH-1 adhesion domain first identified in CD36. Heparin and heparitinase treatment inhibited TSP-1 attachment. Integrins α3β1 and α5β1 mediated TSP-1 attachment of SK-N-SH cells, and integrins α3β1, α5β1, and αvβ3 mediated TSP-1 attachment of U-251MG cells. Attachment was dependent on the RGD sequence which is located in the carboxy-terminus of TSP-1. Treatment with a pharmacologic dosage of retinoic acid altered the TSP-1 cell adhesion mechanism in both cell lines in that neither heparin nor micromolar concentrations of the RGD peptide inhibited attachment; after treatment, attachment was inhibited by the CSVTCG peptide located in the type I repeat domain of TSP-1 and a recombinant adhesion domain (CLESH-1) from CD36. Expression of CD36 was found in the retinoic acid-treated U-251MG cells. These data indicate that neuroectodermally derived cells utilize several mechanisms to attach to TSP-1, and these are differentially modulated by treatment with retinoic acid. These data also suggest that the CSVTCG sequence of TSP-1 modulates or directs cytoskeletal organization in neuroblastoma and astrocytoma cells.</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1006/excr.1999.4458</identifier><identifier>PMID: 10328956</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Astrocytes - drug effects ; Astrocytes - pathology ; astrocytoma ; Astrocytoma - pathology ; Brain - cytology ; Brain - metabolism ; CD36 ; CD36 Antigens - physiology ; Cell Adhesion - drug effects ; Cell Differentiation ; Chondroitin ABC Lyase - pharmacology ; Chondroitin Sulfates - pharmacology ; Cytoskeleton - drug effects ; Cytoskeleton - ultrastructure ; Endothelium - cytology ; Endothelium - metabolism ; Ganglioneuroblastoma - pathology ; Ganglioneuroma - pathology ; glioblastoma ; Glioblastoma - pathology ; heparan sulfate proteoglycan ; Heparin - pharmacology ; Humans ; Integrin alpha3beta1 ; integrins ; Integrins - physiology ; neuroblastoma ; Neuroblastoma - pathology ; Neurons - drug effects ; Neurons - pathology ; Oligopeptides - physiology ; Peptide Fragments - pharmacology ; Polysaccharide-Lyases - pharmacology ; Receptors, Fibronectin - physiology ; Recombinant Proteins - pharmacology ; retinoic acid ; thrombospondin ; Thrombospondin 1 - metabolism ; Tretinoin - pharmacology ; Tumor Cells, Cultured</subject><ispartof>Experimental cell research, 1999-05, Vol.249 (1), p.86-101</ispartof><rights>1999 Academic Press</rights><rights>Copyright 1999 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-845fd4aefa44550fa012672a18686e9b4b8cfcb7e03e185de64f102dbcc5f3d13</citedby><cites>FETCH-LOGICAL-c340t-845fd4aefa44550fa012672a18686e9b4b8cfcb7e03e185de64f102dbcc5f3d13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/excr.1999.4458$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10328956$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pijuan-Thompson, Vivian</creatorcontrib><creatorcontrib>Grammer, J.Robert</creatorcontrib><creatorcontrib>Stewart, Jerry</creatorcontrib><creatorcontrib>Silverstein, Roy L.</creatorcontrib><creatorcontrib>Pearce, S.Frieda</creatorcontrib><creatorcontrib>Tuszynski, George P.</creatorcontrib><creatorcontrib>Murphy-Ullrich, Joanne E.</creatorcontrib><creatorcontrib>Gladson, Candece L.</creatorcontrib><title>Retinoic Acid Alters the Mechanism of Attachment of Malignant Astrocytoma and Neuroblastoma Cells to Thrombospondin-1</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>Based on the hypothesis that the attachment of neuroectodermal cells to thrombospondin-1 (TSP-1) may affect tumor spread and play a role in the anti-tumor effects of retinoic acid, we investigated the expression of TSP-1 in these cellsin situand the effect of retinoic acid on the morphology of TSP-1-adherent neuroblastoma (SK-N-SH) and malignant astrocytoma (U-251MG) cellsin vitro.TSP-1-adherent SK-N-SH cells demonstrated process outgrowth, with further neuronal differentiation after retinoic acid treatment, consistent with thein situstudies showing that TSP-1 expression occurs in a differentiation-specific manner in neuroblastic tumors. TSP-1-adherent U-251MG cells failed to spread; however, after retinoic acid treatment the cells demonstrated broad lamellipodia containing radial actin fibers and organization of integrins α3β1 and α5β1 in clusters in lamellipodia and filopodia. The attachment of both SK-N-SH and U-251MG cells to TSP-1 was found to be mediated by heparan sulfate proteoglycans, integrins, and the CLESH-1 adhesion domain first identified in CD36. Heparin and heparitinase treatment inhibited TSP-1 attachment. Integrins α3β1 and α5β1 mediated TSP-1 attachment of SK-N-SH cells, and integrins α3β1, α5β1, and αvβ3 mediated TSP-1 attachment of U-251MG cells. Attachment was dependent on the RGD sequence which is located in the carboxy-terminus of TSP-1. Treatment with a pharmacologic dosage of retinoic acid altered the TSP-1 cell adhesion mechanism in both cell lines in that neither heparin nor micromolar concentrations of the RGD peptide inhibited attachment; after treatment, attachment was inhibited by the CSVTCG peptide located in the type I repeat domain of TSP-1 and a recombinant adhesion domain (CLESH-1) from CD36. Expression of CD36 was found in the retinoic acid-treated U-251MG cells. These data indicate that neuroectodermally derived cells utilize several mechanisms to attach to TSP-1, and these are differentially modulated by treatment with retinoic acid. These data also suggest that the CSVTCG sequence of TSP-1 modulates or directs cytoskeletal organization in neuroblastoma and astrocytoma cells.</description><subject>Astrocytes - drug effects</subject><subject>Astrocytes - pathology</subject><subject>astrocytoma</subject><subject>Astrocytoma - pathology</subject><subject>Brain - cytology</subject><subject>Brain - metabolism</subject><subject>CD36</subject><subject>CD36 Antigens - physiology</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Differentiation</subject><subject>Chondroitin ABC Lyase - pharmacology</subject><subject>Chondroitin Sulfates - pharmacology</subject><subject>Cytoskeleton - drug effects</subject><subject>Cytoskeleton - ultrastructure</subject><subject>Endothelium - cytology</subject><subject>Endothelium - metabolism</subject><subject>Ganglioneuroblastoma - pathology</subject><subject>Ganglioneuroma - pathology</subject><subject>glioblastoma</subject><subject>Glioblastoma - pathology</subject><subject>heparan sulfate proteoglycan</subject><subject>Heparin - pharmacology</subject><subject>Humans</subject><subject>Integrin alpha3beta1</subject><subject>integrins</subject><subject>Integrins - physiology</subject><subject>neuroblastoma</subject><subject>Neuroblastoma - pathology</subject><subject>Neurons - drug effects</subject><subject>Neurons - pathology</subject><subject>Oligopeptides - physiology</subject><subject>Peptide Fragments - pharmacology</subject><subject>Polysaccharide-Lyases - pharmacology</subject><subject>Receptors, Fibronectin - physiology</subject><subject>Recombinant Proteins - pharmacology</subject><subject>retinoic acid</subject><subject>thrombospondin</subject><subject>Thrombospondin 1 - metabolism</subject><subject>Tretinoin - pharmacology</subject><subject>Tumor Cells, Cultured</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFv1DAQRi0EokvhyhH5xC3LOHES5xitKEVqQaras-XYY9YosRfbQfTf43R74IIvoxk9f5p5hLxnsGcA3Sf8o-OeDcOw57wVL8iOwQBVzev6JdkBMF5xUfcX5E1KPwFACNa9JhcMmloMbbcj6x1m54PTdNTO0HHOGBPNR6S3qI_Ku7TQYOmYs9LHBX3euls1ux9elWZMOQb9mMOiqPKGfsM1hmlW6WlywHkuYYHeH2NYppBOwRvnK_aWvLJqTvjuuV6Sh6vP94fr6ub7l6-H8abSDYdcCd5awxVaVY5rwSpgddfXiolOdDhMfBLa6qlHaJCJ1mDHLYPaTFq3tjGsuSQfz7mnGH6tmLJcXNJlK-UxrEl2Q9-W1xdwfwZ1DClFtPIU3aLio2QgN9FyEy030XITXT58eE5epwXNP_jZbAHEGcBy32-HUSbt0Gs0LqLO0gT3v-y_e9CO3A</recordid><startdate>19990525</startdate><enddate>19990525</enddate><creator>Pijuan-Thompson, Vivian</creator><creator>Grammer, J.Robert</creator><creator>Stewart, Jerry</creator><creator>Silverstein, Roy L.</creator><creator>Pearce, S.Frieda</creator><creator>Tuszynski, George P.</creator><creator>Murphy-Ullrich, Joanne E.</creator><creator>Gladson, Candece L.</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>19990525</creationdate><title>Retinoic Acid Alters the Mechanism of Attachment of Malignant Astrocytoma and Neuroblastoma Cells to Thrombospondin-1</title><author>Pijuan-Thompson, Vivian ; Grammer, J.Robert ; Stewart, Jerry ; Silverstein, Roy L. ; Pearce, S.Frieda ; Tuszynski, George P. ; Murphy-Ullrich, Joanne E. ; Gladson, Candece L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-845fd4aefa44550fa012672a18686e9b4b8cfcb7e03e185de64f102dbcc5f3d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Astrocytes - drug effects</topic><topic>Astrocytes - pathology</topic><topic>astrocytoma</topic><topic>Astrocytoma - pathology</topic><topic>Brain - cytology</topic><topic>Brain - metabolism</topic><topic>CD36</topic><topic>CD36 Antigens - physiology</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Differentiation</topic><topic>Chondroitin ABC Lyase - pharmacology</topic><topic>Chondroitin Sulfates - pharmacology</topic><topic>Cytoskeleton - drug effects</topic><topic>Cytoskeleton - ultrastructure</topic><topic>Endothelium - cytology</topic><topic>Endothelium - metabolism</topic><topic>Ganglioneuroblastoma - pathology</topic><topic>Ganglioneuroma - pathology</topic><topic>glioblastoma</topic><topic>Glioblastoma - pathology</topic><topic>heparan sulfate proteoglycan</topic><topic>Heparin - pharmacology</topic><topic>Humans</topic><topic>Integrin alpha3beta1</topic><topic>integrins</topic><topic>Integrins - physiology</topic><topic>neuroblastoma</topic><topic>Neuroblastoma - pathology</topic><topic>Neurons - drug effects</topic><topic>Neurons - pathology</topic><topic>Oligopeptides - physiology</topic><topic>Peptide Fragments - pharmacology</topic><topic>Polysaccharide-Lyases - pharmacology</topic><topic>Receptors, Fibronectin - physiology</topic><topic>Recombinant Proteins - pharmacology</topic><topic>retinoic acid</topic><topic>thrombospondin</topic><topic>Thrombospondin 1 - metabolism</topic><topic>Tretinoin - pharmacology</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pijuan-Thompson, Vivian</creatorcontrib><creatorcontrib>Grammer, J.Robert</creatorcontrib><creatorcontrib>Stewart, Jerry</creatorcontrib><creatorcontrib>Silverstein, Roy L.</creatorcontrib><creatorcontrib>Pearce, S.Frieda</creatorcontrib><creatorcontrib>Tuszynski, George P.</creatorcontrib><creatorcontrib>Murphy-Ullrich, Joanne E.</creatorcontrib><creatorcontrib>Gladson, Candece L.</creatorcontrib><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>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pijuan-Thompson, Vivian</au><au>Grammer, J.Robert</au><au>Stewart, Jerry</au><au>Silverstein, Roy L.</au><au>Pearce, S.Frieda</au><au>Tuszynski, George P.</au><au>Murphy-Ullrich, Joanne E.</au><au>Gladson, Candece L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Retinoic Acid Alters the Mechanism of Attachment of Malignant Astrocytoma and Neuroblastoma Cells to Thrombospondin-1</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>1999-05-25</date><risdate>1999</risdate><volume>249</volume><issue>1</issue><spage>86</spage><epage>101</epage><pages>86-101</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><abstract>Based on the hypothesis that the attachment of neuroectodermal cells to thrombospondin-1 (TSP-1) may affect tumor spread and play a role in the anti-tumor effects of retinoic acid, we investigated the expression of TSP-1 in these cellsin situand the effect of retinoic acid on the morphology of TSP-1-adherent neuroblastoma (SK-N-SH) and malignant astrocytoma (U-251MG) cellsin vitro.TSP-1-adherent SK-N-SH cells demonstrated process outgrowth, with further neuronal differentiation after retinoic acid treatment, consistent with thein situstudies showing that TSP-1 expression occurs in a differentiation-specific manner in neuroblastic tumors. TSP-1-adherent U-251MG cells failed to spread; however, after retinoic acid treatment the cells demonstrated broad lamellipodia containing radial actin fibers and organization of integrins α3β1 and α5β1 in clusters in lamellipodia and filopodia. The attachment of both SK-N-SH and U-251MG cells to TSP-1 was found to be mediated by heparan sulfate proteoglycans, integrins, and the CLESH-1 adhesion domain first identified in CD36. Heparin and heparitinase treatment inhibited TSP-1 attachment. Integrins α3β1 and α5β1 mediated TSP-1 attachment of SK-N-SH cells, and integrins α3β1, α5β1, and αvβ3 mediated TSP-1 attachment of U-251MG cells. Attachment was dependent on the RGD sequence which is located in the carboxy-terminus of TSP-1. Treatment with a pharmacologic dosage of retinoic acid altered the TSP-1 cell adhesion mechanism in both cell lines in that neither heparin nor micromolar concentrations of the RGD peptide inhibited attachment; after treatment, attachment was inhibited by the CSVTCG peptide located in the type I repeat domain of TSP-1 and a recombinant adhesion domain (CLESH-1) from CD36. Expression of CD36 was found in the retinoic acid-treated U-251MG cells. These data indicate that neuroectodermally derived cells utilize several mechanisms to attach to TSP-1, and these are differentially modulated by treatment with retinoic acid. These data also suggest that the CSVTCG sequence of TSP-1 modulates or directs cytoskeletal organization in neuroblastoma and astrocytoma cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10328956</pmid><doi>10.1006/excr.1999.4458</doi><tpages>16</tpages></addata></record> |
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| ispartof | Experimental cell research, 1999-05, Vol.249 (1), p.86-101 |
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| subjects | Astrocytes - drug effects Astrocytes - pathology astrocytoma Astrocytoma - pathology Brain - cytology Brain - metabolism CD36 CD36 Antigens - physiology Cell Adhesion - drug effects Cell Differentiation Chondroitin ABC Lyase - pharmacology Chondroitin Sulfates - pharmacology Cytoskeleton - drug effects Cytoskeleton - ultrastructure Endothelium - cytology Endothelium - metabolism Ganglioneuroblastoma - pathology Ganglioneuroma - pathology glioblastoma Glioblastoma - pathology heparan sulfate proteoglycan Heparin - pharmacology Humans Integrin alpha3beta1 integrins Integrins - physiology neuroblastoma Neuroblastoma - pathology Neurons - drug effects Neurons - pathology Oligopeptides - physiology Peptide Fragments - pharmacology Polysaccharide-Lyases - pharmacology Receptors, Fibronectin - physiology Recombinant Proteins - pharmacology retinoic acid thrombospondin Thrombospondin 1 - metabolism Tretinoin - pharmacology Tumor Cells, Cultured |
| title | Retinoic Acid Alters the Mechanism of Attachment of Malignant Astrocytoma and Neuroblastoma Cells to Thrombospondin-1 |
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