Laminin-mediated process formation in neuronal cells involves protein dephosphorylation
Laminin mediates neural adhesion and process formation. A possible signal transduction pathway for laminin was investigated in both NG108‐15 and PC12 neuronal cells using radiolabeling studies as well as various stimulators and inhibitors of phosphatases and kinases. Using [32p]‐ortho‐phosphate, lam...
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| Veröffentlicht in: | Journal of neuroscience research 1990-11, Vol.27 (3), p.418-426 |
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| creator | Weeks, B. S. DiSalvo, J. Kleinman, H. K. |
| description | Laminin mediates neural adhesion and process formation. A possible signal transduction pathway for laminin was investigated in both NG108‐15 and PC12 neuronal cells using radiolabeling studies as well as various stimulators and inhibitors of phosphatases and kinases. Using [32p]‐ortho‐phosphate, laminin caused a decrease in the TCA‐precipitable counts. Further, laminin stimulated dephosphorylation of laminin binding proteins of 110 kDa, 67 kDa, and 45 kDa and this dephosphorylation was blocked by the phosphatase inhibitor, okadaic acid, and the protein kinase C stimulator, TPA. The phosphatase inhibitors okadaic acid and vanadate, as well as the protein kinase C stimulators, TPA and DAG, blocked laminin‐mediated process formation. Inhibitors of kinase activity such as H‐7, H‐8, and H‐9 increased laminin‐mediated neural process formation. Since phosphate incorporation into laminin‐binding proteins is decreased by laminin and because both phosphatase inhibitors and kinase stimulators inhibit laminin‐mediated process formation, we conclude that dephosphorylation events promote the neural cell response to laminin. |
| doi_str_mv | 10.1002/jnr.490270321 |
| format | Article |
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S. ; DiSalvo, J. ; Kleinman, H. K.</creator><creatorcontrib>Weeks, B. S. ; DiSalvo, J. ; Kleinman, H. K.</creatorcontrib><description>Laminin mediates neural adhesion and process formation. A possible signal transduction pathway for laminin was investigated in both NG108‐15 and PC12 neuronal cells using radiolabeling studies as well as various stimulators and inhibitors of phosphatases and kinases. Using [32p]‐ortho‐phosphate, laminin caused a decrease in the TCA‐precipitable counts. Further, laminin stimulated dephosphorylation of laminin binding proteins of 110 kDa, 67 kDa, and 45 kDa and this dephosphorylation was blocked by the phosphatase inhibitor, okadaic acid, and the protein kinase C stimulator, TPA. The phosphatase inhibitors okadaic acid and vanadate, as well as the protein kinase C stimulators, TPA and DAG, blocked laminin‐mediated process formation. Inhibitors of kinase activity such as H‐7, H‐8, and H‐9 increased laminin‐mediated neural process formation. Since phosphate incorporation into laminin‐binding proteins is decreased by laminin and because both phosphatase inhibitors and kinase stimulators inhibit laminin‐mediated process formation, we conclude that dephosphorylation events promote the neural cell response to laminin.</description><identifier>ISSN: 0360-4012</identifier><identifier>EISSN: 1097-4547</identifier><identifier>DOI: 10.1002/jnr.490270321</identifier><identifier>PMID: 1965840</identifier><identifier>CODEN: JNREDK</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Adrenal Gland Neoplasms - pathology ; Animals ; Biological and medical sciences ; Cell Adhesion - drug effects ; Cell differentiation, maturation, development, hematopoiesis ; Cell physiology ; Diglycerides - pharmacology ; Ethers, Cyclic - pharmacology ; Fundamental and applied biological sciences. Psychology ; Glioma - pathology ; kinase ; laminin ; Laminin - pharmacology ; Molecular and cellular biology ; Neoplasm Proteins - metabolism ; neural process dephosphorylation ; Neuroblastoma - pathology ; Neurons - drug effects ; Neurons - ultrastructure ; Okadaic Acid ; Pheochromocytoma - pathology ; Phorbol Esters - pharmacology ; phosphatase ; Phosphoprotein Phosphatases - metabolism ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Kinase C - antagonists & inhibitors ; Protein Kinase C - metabolism ; Protein Processing, Post-Translational - drug effects ; Rats ; Signal Transduction ; Tumor Cells, Cultured - drug effects ; Tumor Cells, Cultured - ultrastructure ; Vanadates - pharmacology</subject><ispartof>Journal of neuroscience research, 1990-11, Vol.27 (3), p.418-426</ispartof><rights>Copyright © 1990 Wiley‐Liss, Inc.</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4041-36ddc0510b45d97af84cc6118bf45f7f00ebd142cfd2cfffbfe59376458118a23</citedby><cites>FETCH-LOGICAL-c4041-36ddc0510b45d97af84cc6118bf45f7f00ebd142cfd2cfffbfe59376458118a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjnr.490270321$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjnr.490270321$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19545766$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1965840$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Weeks, B. S.</creatorcontrib><creatorcontrib>DiSalvo, J.</creatorcontrib><creatorcontrib>Kleinman, H. K.</creatorcontrib><title>Laminin-mediated process formation in neuronal cells involves protein dephosphorylation</title><title>Journal of neuroscience research</title><addtitle>J. Neurosci. Res</addtitle><description>Laminin mediates neural adhesion and process formation. A possible signal transduction pathway for laminin was investigated in both NG108‐15 and PC12 neuronal cells using radiolabeling studies as well as various stimulators and inhibitors of phosphatases and kinases. Using [32p]‐ortho‐phosphate, laminin caused a decrease in the TCA‐precipitable counts. Further, laminin stimulated dephosphorylation of laminin binding proteins of 110 kDa, 67 kDa, and 45 kDa and this dephosphorylation was blocked by the phosphatase inhibitor, okadaic acid, and the protein kinase C stimulator, TPA. The phosphatase inhibitors okadaic acid and vanadate, as well as the protein kinase C stimulators, TPA and DAG, blocked laminin‐mediated process formation. Inhibitors of kinase activity such as H‐7, H‐8, and H‐9 increased laminin‐mediated neural process formation. Since phosphate incorporation into laminin‐binding proteins is decreased by laminin and because both phosphatase inhibitors and kinase stimulators inhibit laminin‐mediated process formation, we conclude that dephosphorylation events promote the neural cell response to laminin.</description><subject>Adrenal Gland Neoplasms - pathology</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell differentiation, maturation, development, hematopoiesis</subject><subject>Cell physiology</subject><subject>Diglycerides - pharmacology</subject><subject>Ethers, Cyclic - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glioma - pathology</subject><subject>kinase</subject><subject>laminin</subject><subject>Laminin - pharmacology</subject><subject>Molecular and cellular biology</subject><subject>Neoplasm Proteins - metabolism</subject><subject>neural process dephosphorylation</subject><subject>Neuroblastoma - pathology</subject><subject>Neurons - drug effects</subject><subject>Neurons - ultrastructure</subject><subject>Okadaic Acid</subject><subject>Pheochromocytoma - pathology</subject><subject>Phorbol Esters - pharmacology</subject><subject>phosphatase</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein Kinase C - metabolism</subject><subject>Protein Processing, Post-Translational - drug effects</subject><subject>Rats</subject><subject>Signal Transduction</subject><subject>Tumor Cells, Cultured - drug effects</subject><subject>Tumor Cells, Cultured - ultrastructure</subject><subject>Vanadates - pharmacology</subject><issn>0360-4012</issn><issn>1097-4547</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM9PwjAUxxujQUSPHk128Th83dp1OxqioAFMjAZuTde1sTi2pQWU_97iCHLy8PKS9_28X1-ErjH0MUB0t6hsn2QQMYgjfIK6GDIWEkrYKepCnEBIAEfn6MK5BQBkGY07qIOzhKYEumg2FktTmSpcqsKIlSqCxtZSORfo2i7FytRVYKqgUmtbV6IMpCpL5yubutwot4NXyuuFaj5q58Nuy9-mS3SmRenU1T730Pvjw9tgFI5fhk-D-3EoCRAcxklRSKAYckKLjAmdEikTjNNcE6qZBlB5gUkkdeFD61wrmsUsITT1kIjiHgrbudLWzlmleWPNUtgtx8B3_nDvDz_44_mblm_WuX_5j24N8frtXhdOilJbUUnjjjBKKEsSz7GW-zKl2v6_lD9PX48v2F9s3Ep9HzqF_eQJixnls-mQw3wyH0xmI07jH7wSj6Q</recordid><startdate>199011</startdate><enddate>199011</enddate><creator>Weeks, B. S.</creator><creator>DiSalvo, J.</creator><creator>Kleinman, H. K.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><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></search><sort><creationdate>199011</creationdate><title>Laminin-mediated process formation in neuronal cells involves protein dephosphorylation</title><author>Weeks, B. S. ; DiSalvo, J. ; Kleinman, H. K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4041-36ddc0510b45d97af84cc6118bf45f7f00ebd142cfd2cfffbfe59376458118a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Adrenal Gland Neoplasms - pathology</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell differentiation, maturation, development, hematopoiesis</topic><topic>Cell physiology</topic><topic>Diglycerides - pharmacology</topic><topic>Ethers, Cyclic - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glioma - pathology</topic><topic>kinase</topic><topic>laminin</topic><topic>Laminin - pharmacology</topic><topic>Molecular and cellular biology</topic><topic>Neoplasm Proteins - metabolism</topic><topic>neural process dephosphorylation</topic><topic>Neuroblastoma - pathology</topic><topic>Neurons - drug effects</topic><topic>Neurons - ultrastructure</topic><topic>Okadaic Acid</topic><topic>Pheochromocytoma - pathology</topic><topic>Phorbol Esters - pharmacology</topic><topic>phosphatase</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinase C - antagonists & inhibitors</topic><topic>Protein Kinase C - metabolism</topic><topic>Protein Processing, Post-Translational - drug effects</topic><topic>Rats</topic><topic>Signal Transduction</topic><topic>Tumor Cells, Cultured - drug effects</topic><topic>Tumor Cells, Cultured - ultrastructure</topic><topic>Vanadates - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Weeks, B. S.</creatorcontrib><creatorcontrib>DiSalvo, J.</creatorcontrib><creatorcontrib>Kleinman, H. K.</creatorcontrib><collection>Istex</collection><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><jtitle>Journal of neuroscience research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Weeks, B. S.</au><au>DiSalvo, J.</au><au>Kleinman, H. K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Laminin-mediated process formation in neuronal cells involves protein dephosphorylation</atitle><jtitle>Journal of neuroscience research</jtitle><addtitle>J. Neurosci. Res</addtitle><date>1990-11</date><risdate>1990</risdate><volume>27</volume><issue>3</issue><spage>418</spage><epage>426</epage><pages>418-426</pages><issn>0360-4012</issn><eissn>1097-4547</eissn><coden>JNREDK</coden><abstract>Laminin mediates neural adhesion and process formation. A possible signal transduction pathway for laminin was investigated in both NG108‐15 and PC12 neuronal cells using radiolabeling studies as well as various stimulators and inhibitors of phosphatases and kinases. Using [32p]‐ortho‐phosphate, laminin caused a decrease in the TCA‐precipitable counts. Further, laminin stimulated dephosphorylation of laminin binding proteins of 110 kDa, 67 kDa, and 45 kDa and this dephosphorylation was blocked by the phosphatase inhibitor, okadaic acid, and the protein kinase C stimulator, TPA. The phosphatase inhibitors okadaic acid and vanadate, as well as the protein kinase C stimulators, TPA and DAG, blocked laminin‐mediated process formation. Inhibitors of kinase activity such as H‐7, H‐8, and H‐9 increased laminin‐mediated neural process formation. Since phosphate incorporation into laminin‐binding proteins is decreased by laminin and because both phosphatase inhibitors and kinase stimulators inhibit laminin‐mediated process formation, we conclude that dephosphorylation events promote the neural cell response to laminin.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>1965840</pmid><doi>10.1002/jnr.490270321</doi><tpages>9</tpages></addata></record> |
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| subjects | Adrenal Gland Neoplasms - pathology Animals Biological and medical sciences Cell Adhesion - drug effects Cell differentiation, maturation, development, hematopoiesis Cell physiology Diglycerides - pharmacology Ethers, Cyclic - pharmacology Fundamental and applied biological sciences. Psychology Glioma - pathology kinase laminin Laminin - pharmacology Molecular and cellular biology Neoplasm Proteins - metabolism neural process dephosphorylation Neuroblastoma - pathology Neurons - drug effects Neurons - ultrastructure Okadaic Acid Pheochromocytoma - pathology Phorbol Esters - pharmacology phosphatase Phosphoprotein Phosphatases - metabolism Phosphoproteins - metabolism Phosphorylation Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Protein Processing, Post-Translational - drug effects Rats Signal Transduction Tumor Cells, Cultured - drug effects Tumor Cells, Cultured - ultrastructure Vanadates - pharmacology |
| title | Laminin-mediated process formation in neuronal cells involves protein dephosphorylation |
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