Modulation of Calpastatin Specificity in Rat Tissues by Reversible Phosphorylation and Dephosphorylation
| Autor: | P. Mengotti, Mauro Michetti, F. Salamino, R. Detullio, Sandro Pontremoli, E. Melloni |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Erythrocytes
Biophysics Cysteine Proteinase Inhibitors Biology Kidney Biochemistry Chromatography Affinity Chromatography DEAE-Cellulose Dephosphorylation medicine Animals Humans Phosphorylation Protein kinase A Molecular Biology Protein Kinase C Calpastatin chemistry.chemical_classification Calpain Myocardium Calcium-Binding Proteins Skeletal muscle Cell Biology Cyclic AMP-Dependent Protein Kinases Globins Rats Kinetics medicine.anatomical_structure Enzyme chemistry Enzyme inhibitor biology.protein Protein Kinases |
| Zdroj: | Biochemical and Biophysical Research Communications. 199:1326-1332 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1994.1376 |
| Popis: | Two calpastatins, with Mr 110 KD and named calpastatin I and II, have been isolated from rat heart and kidney and displayed distinct inhibitory efficiency with mu- and m-calpain, respectively, as those isolated from rat skeletal muscle. Whereas the level of calpastatin I always exceeds that of mu-calpain, the level of calpastatin II appears to be more closely correlated to the level of m-calpain. As previously shown for skeletal muscle, the two inhibitor proteins can be interconverted by a phosphorylation-dephosphorylation reaction; the enzyme responsible for phosphate incorporation in calpastatin I is now identified in c-AMP dependent protein kinase A. In rat erythrocytes, containing a single calpain form, the single low Mr calpastatin form does not undergo reversible phosphorylation and is equally efficient in respect to typical mu- and m-calpain. The presence of two interconvertible calpastatin forms provides the cells with a highly sensitive mechanism of regulation of the Ca(2+)-dependent proteolytic system. |
| Databáze: | OpenAIRE |
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