On the contractile function of protein phosphatases in isolated human coronary arteries
Autor: | Sabine Huke, Hartmut Lüss, Wilhelm Schmitz, Iva Lüss, Bettina Linck, F.U. Müller, Jörg Knapp, Ute Vahlensieck, Joachim Neumann, Peter Nacke, Oliver Klein-Wiele, Mario C. Deng, H. H. Scheld, Peter Boknik |
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Rok vydání: | 1999 |
Předmět: |
Immunoblotting
Phosphatase macromolecular substances Myosins Biology environment and public health Chromatography Affinity Muscle Smooth Vascular Serine Affinity chromatography Myosin Phosphoprotein Phosphatases Humans Phosphorylation Threonine Pharmacology Messenger RNA Myocardium Nucleic Acid Hybridization General Medicine Protein phosphatase 2 Coronary Vessels Phosphoric Monoester Hydrolases enzymes and coenzymes (carbohydrates) Biochemistry embryonic structures Muscle Contraction |
Zdroj: | Naunyn-Schmiedeberg's Archives of Pharmacology. 360:464-472 |
ISSN: | 1432-1912 0028-1298 |
DOI: | 10.1007/s002109900124 |
Popis: | It is unknown whether protein phosphatases types 1 and 2A are present in and can regulate the tone of human vascular tissue. The expression and possible function of serine/threonine protein phosphatases (PP) type 1 (PP1) and type 2A (PP2A) were studied in isolated human coronary arteries. Catalytic subunits of PPI and PP2A were identified by means of phosphatase activity measurement in tissue homogenates, by separation of enriched extracts through affinity column chromatography, by immunoblotting with specific antibodies, by hybridization of mRNA with specific DNA probes and PCR of reverse transcribed mRNA. Based on these methods, the catalytic subunits of PP1(alpha,beta,gamma) and PP2A(alpha,beta) were identified. Appropriately, cantharidin, an inhibitor of PP1 and PP2A, increased basal tone of human isolated coronary artery rings with an EC50 of about 16 micromol/l by increasing the phosphorylation state of the regulatory light chains of myosin. In summary, PP1 and PP2A are expressed in human coronary arteries and they can alter vascular tone. |
Databáze: | OpenAIRE |
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