Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells
Background: The aim of this study was to characterize the effects of the coagulation proteinase thrombin on proteomic level in human hepatic stellate LX-2 cells. Methods: Proteomic analyses were performed using surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF-...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Society of Medical Biochemists of Serbia, Belgrade
2014-01-01
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| Series: | Journal of Medical Biochemistry |
| Subjects: | |
| Online Access: | https://scindeks-clanci.ceon.rs/data/pdf/1452-8258/2014/1452-82581404371K.pdf |
| _version_ | 1818849139412172800 |
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| author | Kaufmann Roland Mußbach Franziska Urbanek Annett Settmacher Utz von Eggeling Ferdinand |
| author_facet | Kaufmann Roland Mußbach Franziska Urbanek Annett Settmacher Utz von Eggeling Ferdinand |
| author_sort | Kaufmann Roland |
| collection | DOAJ |
| description | Background: The aim of this study was to characterize the effects of the coagulation proteinase thrombin on proteomic level in human hepatic stellate LX-2 cells. Methods: Proteomic analyses were performed using surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF-MS). The protein profiles obtained from LX-2 cell lysates using strong anion exchanger Q10 ProteinChip arrays were statistically analyzed. Results: The peak intensities of 50 protein/peptide clusters were identified as being different between nonstimulated and LX-2 cells treated with thrombin for 6 h and 24 h, respectively. As the most significantly enhanced single signal in LX-2 cells stimulated with thrombin, a protein with a molecular mass of 13.560 kDa has been identified that corresponds exactly to calcium dependent phospholipase 2 (cPLA2). Thrombin-induced increase in the cPLA2 protein expression in LX-2 cells was confirmed by using the Western blotting technique. Conclusions: Together with the finding that thrombin induced phosphorylating activation of cPLA2 in LX-2 cells, our data point to an important function of the thrombin-mediated modulation of cytosolic phospholipase A2 in hepatic stellate cells. |
| first_indexed | 2024-12-19T06:28:29Z |
| format | Article |
| id | doaj.art-f672d3e2c06f4c32ab6c1785b33329ed |
| institution | Directory Open Access Journal |
| issn | 1452-8258 1452-8266 |
| language | English |
| last_indexed | 2024-12-19T06:28:29Z |
| publishDate | 2014-01-01 |
| publisher | Society of Medical Biochemists of Serbia, Belgrade |
| record_format | Article |
| series | Journal of Medical Biochemistry |
| spelling | doaj.art-f672d3e2c06f4c32ab6c1785b33329ed2022-12-21T20:32:29ZengSociety of Medical Biochemists of Serbia, BelgradeJournal of Medical Biochemistry1452-82581452-82662014-01-013343713751452-82581404371KProteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cellsKaufmann Roland0Mußbach Franziska1Urbanek Annett2Settmacher Utz3von Eggeling Ferdinand4Jena University Hospital, Department of General, Visceral and Vascular Surgery, Experimental Transplantation Surgery, Jena, GermanyJena University Hospital, Department of General, Visceral and Vascular Surgery, Experimental Transplantation Surgery, Jena, GermanyJena University Hospital, Institute of Human Genetics, Core Unit Chip Application, Jena, GermanyJena University Hospital, Department of General, Visceral and Vascular Surgery, Jena, GermanyJena University Hospital, Institute of Human Genetics, Core Unit Chip Application, Jena, GermanyBackground: The aim of this study was to characterize the effects of the coagulation proteinase thrombin on proteomic level in human hepatic stellate LX-2 cells. Methods: Proteomic analyses were performed using surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF-MS). The protein profiles obtained from LX-2 cell lysates using strong anion exchanger Q10 ProteinChip arrays were statistically analyzed. Results: The peak intensities of 50 protein/peptide clusters were identified as being different between nonstimulated and LX-2 cells treated with thrombin for 6 h and 24 h, respectively. As the most significantly enhanced single signal in LX-2 cells stimulated with thrombin, a protein with a molecular mass of 13.560 kDa has been identified that corresponds exactly to calcium dependent phospholipase 2 (cPLA2). Thrombin-induced increase in the cPLA2 protein expression in LX-2 cells was confirmed by using the Western blotting technique. Conclusions: Together with the finding that thrombin induced phosphorylating activation of cPLA2 in LX-2 cells, our data point to an important function of the thrombin-mediated modulation of cytosolic phospholipase A2 in hepatic stellate cells.https://scindeks-clanci.ceon.rs/data/pdf/1452-8258/2014/1452-82581404371K.pdfthrombinhepatic stellate cellslx-2proteomic profilingmass spectrometry |
| spellingShingle | Kaufmann Roland Mußbach Franziska Urbanek Annett Settmacher Utz von Eggeling Ferdinand Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells Journal of Medical Biochemistry thrombin hepatic stellate cells lx-2 proteomic profiling mass spectrometry |
| title | Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells |
| title_full | Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells |
| title_fullStr | Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells |
| title_full_unstemmed | Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells |
| title_short | Proteomic effects of the coagulation proteinase thrombin on LX-2 hepatic stellate cells |
| title_sort | proteomic effects of the coagulation proteinase thrombin on lx 2 hepatic stellate cells |
| topic | thrombin hepatic stellate cells lx-2 proteomic profiling mass spectrometry |
| url | https://scindeks-clanci.ceon.rs/data/pdf/1452-8258/2014/1452-82581404371K.pdf |
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