Endothelial Cell Spreading on Type IV Collagen and Spreading-Induced FAK Phosphorylation Is Regulated by Ca2+Influx
The interaction of endothelial cells with their basement membrane and local stroma is highly regulated. The observation that CAI, an inhibitor of Ca++influx, inhibited human umbilical vein endothelial cell (HUVEC) adhesion suggested that Ca++influx was a regulator of HUVEC–matrix interaction. Exposu...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1998-07, Vol.248 (3), p.635-640 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Alessandro, Riccardo Masiero, Laura Lapidos, Karen Spoonster, Joseph Kohn, Elise C. |
| description | The interaction of endothelial cells with their basement membrane and local stroma is highly regulated. The observation that CAI, an inhibitor of Ca++influx, inhibited human umbilical vein endothelial cell (HUVEC) adhesion suggested that Ca++influx was a regulator of HUVEC–matrix interaction. Exposure of HUVEC cells to CAI or SK&F 96365, another Ca++influx inhibitor, selectively blocked spreading but not attachment on type IV collagen but not type I collagen. Ca++influx blockade also prevented spreading-induced FAK phosphorylation and kinase activity and secondary paxillin phosphorylation. No inhibitory effect was observed when the cells spread on type I collagen. The inhibitory effect of CAI on spreading and spreading-associated FAK phosphorylation and kinase activity was reversible. These data indicate that HUVEC cells have a selective requirement for Ca++influx for spreading and downstream signaling on basement membrane type IV collagen. |
| doi_str_mv | 10.1006/bbrc.1998.8705 |
| format | Article |
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The observation that CAI, an inhibitor of Ca++influx, inhibited human umbilical vein endothelial cell (HUVEC) adhesion suggested that Ca++influx was a regulator of HUVEC–matrix interaction. Exposure of HUVEC cells to CAI or SK&F 96365, another Ca++influx inhibitor, selectively blocked spreading but not attachment on type IV collagen but not type I collagen. Ca++influx blockade also prevented spreading-induced FAK phosphorylation and kinase activity and secondary paxillin phosphorylation. No inhibitory effect was observed when the cells spread on type I collagen. The inhibitory effect of CAI on spreading and spreading-associated FAK phosphorylation and kinase activity was reversible. These data indicate that HUVEC cells have a selective requirement for Ca++influx for spreading and downstream signaling on basement membrane type IV collagen.</description><subject>Calcium - metabolism</subject><subject>Calcium Channel Blockers - pharmacology</subject><subject>Cell Adhesion</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Movement - physiology</subject><subject>Cells, Cultured</subject><subject>Collagen</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Endothelium, Vascular - cytology</subject><subject>Endothelium, Vascular - drug effects</subject><subject>Endothelium, Vascular - physiology</subject><subject>Focal Adhesion Kinase 1</subject><subject>Focal Adhesion Protein-Tyrosine Kinases</subject><subject>Humans</subject><subject>Imidazoles - pharmacology</subject><subject>Kinetics</subject><subject>Paxillin</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Triazoles - pharmacology</subject><subject>Umbilical Veins</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEGP0zAQRi0EWsrClRuST1xQyjhpavu4inYhYiUQLIibZceT1si1g50g-u9x1QpOnEajed8nzSPkJYM1A9i-NSYNayalWAsO7SOyYiChqhlsHpMVFKKqJfv-lDzL-QcAY5utvCJXkkMjuViRfBtsnPfonfa0Q-_plymhti7saAz04Tgh7b_RLnqvdxioDvYfUfXBLgNaenfzgX7axzztYzp6PbsS7TP9jLulbAUwR9rp-k0fRr_8fk6ejNpnfHGZ1-Tr3e1D9766__iu727uq6HmbK7QjFYACGO4aFHWVljeSGwMmg0DjmhNu2VNy5jllo_jWINhKEepjeRtDc01eX3unVL8uWCe1cHlofyoA8YlK96IVkC9KeD6DA4p5pxwVFNyB52OioE6WVYny-pkWZ0sl8CrS_NiDmj_4het5S7Odyzv_XKYVB4chqLKJRxmZaP7X_UfwDuMRg</recordid><startdate>19980730</startdate><enddate>19980730</enddate><creator>Alessandro, Riccardo</creator><creator>Masiero, Laura</creator><creator>Lapidos, Karen</creator><creator>Spoonster, Joseph</creator><creator>Kohn, Elise C.</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>19980730</creationdate><title>Endothelial Cell Spreading on Type IV Collagen and Spreading-Induced FAK Phosphorylation Is Regulated by Ca2+Influx</title><author>Alessandro, Riccardo ; 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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Calcium - metabolism Calcium Channel Blockers - pharmacology Cell Adhesion Cell Adhesion Molecules - metabolism Cell Movement - physiology Cells, Cultured Collagen Cytoskeletal Proteins - metabolism Endothelium, Vascular - cytology Endothelium, Vascular - drug effects Endothelium, Vascular - physiology Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Humans Imidazoles - pharmacology Kinetics Paxillin Phosphoproteins - metabolism Phosphorylation Protein-Tyrosine Kinases - metabolism Triazoles - pharmacology Umbilical Veins |
| title | Endothelial Cell Spreading on Type IV Collagen and Spreading-Induced FAK Phosphorylation Is Regulated by Ca2+Influx |
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