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Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan
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| Zeitschriftentitel: | Biochemical Journal |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Biochemical Journal, 299, 1994, 2, S. 507-513 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
|
| Schlagwörter: |
| author_facet |
Pejler, G Söderström, K Karlström, A Pejler, G Söderström, K Karlström, A |
|---|---|
| author |
Pejler, G Söderström, K Karlström, A |
| spellingShingle |
Pejler, G Söderström, K Karlström, A Biochemical Journal Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan Cell Biology Molecular Biology Biochemistry |
| author_sort |
pejler, g |
| spelling |
Pejler, G Söderström, K Karlström, A 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2990507 <jats:p>Rat peritoneal mast cells were shown to inactivate thrombin rapidly. The thrombin-inactivating activity was purified to homogeneity by a combination of anion-exchange chromatography and h.p.l.c. on a Superdex 75 column. The purified thrombin inactivator had an apparent molecular mass of 29 kDa and an N-terminal amino acid sequence identical to rat mast-cell protease 1 (RMCP-1). After labelling of the mast cells in vivo with 35SO4(2-), RMCP-1 was recovered in a macromolecular complex with [35S]heparin proteoglycans. Dissociation of RMCP-1 from the heparin proteoglycans by Superdex 75 chromatography in the presence of 2 M NaCl resulted in a marked loss of the thrombin-inactivating activity displayed by the enzyme. When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties. Affinity chromatography of endogenous [35S]heparin on matrix-linked RMCP-1 demonstrated that all of the heparin molecules contained high-affinity binding sites for the mast-cell protease. In contrast, the endogenous mast-cell heparin showed low affinity for antithrombin, a protease inhibitor involved in the regulation of coagulation enzymes.</jats:p> Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan Biochemical Journal |
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1994 |
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Biochemical Journal |
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| title |
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_unstemmed |
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_full |
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_fullStr |
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_full_unstemmed |
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_short |
Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_sort |
inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1042/bj2990507 |
| publishDate |
1994 |
| physical |
507-513 |
| description |
<jats:p>Rat peritoneal mast cells were shown to inactivate thrombin rapidly. The thrombin-inactivating activity was purified to homogeneity by a combination of anion-exchange chromatography and h.p.l.c. on a Superdex 75 column. The purified thrombin inactivator had an apparent molecular mass of 29 kDa and an N-terminal amino acid sequence identical to rat mast-cell protease 1 (RMCP-1). After labelling of the mast cells in vivo with 35SO4(2-), RMCP-1 was recovered in a macromolecular complex with [35S]heparin proteoglycans. Dissociation of RMCP-1 from the heparin proteoglycans by Superdex 75 chromatography in the presence of 2 M NaCl resulted in a marked loss of the thrombin-inactivating activity displayed by the enzyme. When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties. Affinity chromatography of endogenous [35S]heparin on matrix-linked RMCP-1 demonstrated that all of the heparin molecules contained high-affinity binding sites for the mast-cell protease. In contrast, the endogenous mast-cell heparin showed low affinity for antithrombin, a protease inhibitor involved in the regulation of coagulation enzymes.</jats:p> |
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| author | Pejler, G, Söderström, K, Karlström, A |
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| description | <jats:p>Rat peritoneal mast cells were shown to inactivate thrombin rapidly. The thrombin-inactivating activity was purified to homogeneity by a combination of anion-exchange chromatography and h.p.l.c. on a Superdex 75 column. The purified thrombin inactivator had an apparent molecular mass of 29 kDa and an N-terminal amino acid sequence identical to rat mast-cell protease 1 (RMCP-1). After labelling of the mast cells in vivo with 35SO4(2-), RMCP-1 was recovered in a macromolecular complex with [35S]heparin proteoglycans. Dissociation of RMCP-1 from the heparin proteoglycans by Superdex 75 chromatography in the presence of 2 M NaCl resulted in a marked loss of the thrombin-inactivating activity displayed by the enzyme. When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties. Affinity chromatography of endogenous [35S]heparin on matrix-linked RMCP-1 demonstrated that all of the heparin molecules contained high-affinity binding sites for the mast-cell protease. In contrast, the endogenous mast-cell heparin showed low affinity for antithrombin, a protease inhibitor involved in the regulation of coagulation enzymes.</jats:p> |
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| imprint | Portland Press Ltd., 1994 |
| imprint_str_mv | Portland Press Ltd., 1994 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 507-513 |
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| series | Biochemical Journal |
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| spelling | Pejler, G Söderström, K Karlström, A 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2990507 <jats:p>Rat peritoneal mast cells were shown to inactivate thrombin rapidly. The thrombin-inactivating activity was purified to homogeneity by a combination of anion-exchange chromatography and h.p.l.c. on a Superdex 75 column. The purified thrombin inactivator had an apparent molecular mass of 29 kDa and an N-terminal amino acid sequence identical to rat mast-cell protease 1 (RMCP-1). After labelling of the mast cells in vivo with 35SO4(2-), RMCP-1 was recovered in a macromolecular complex with [35S]heparin proteoglycans. Dissociation of RMCP-1 from the heparin proteoglycans by Superdex 75 chromatography in the presence of 2 M NaCl resulted in a marked loss of the thrombin-inactivating activity displayed by the enzyme. When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties. Affinity chromatography of endogenous [35S]heparin on matrix-linked RMCP-1 demonstrated that all of the heparin molecules contained high-affinity binding sites for the mast-cell protease. In contrast, the endogenous mast-cell heparin showed low affinity for antithrombin, a protease inhibitor involved in the regulation of coagulation enzymes.</jats:p> Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan Biochemical Journal |
| spellingShingle | Pejler, G, Söderström, K, Karlström, A, Biochemical Journal, Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan, Cell Biology, Molecular Biology, Biochemistry |
| title | Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_full | Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_fullStr | Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_full_unstemmed | Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_short | Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_sort | inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| title_unstemmed | Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1042/bj2990507 |