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Interactions moléculaires des calpaïnes 1 et 3 avec la région N1 de la titine humaine

Abstract : Calpains are papain-like cystéine protease first identified several years ago. Because they are present in the cytosol of mammalian cells and because they are activated in response to Ca2+ mobilization, they are thought to be involved mainly in cell signalling pathways. They could participate in cellular responses such as apoptosis, proliferation, extracellular matrix adhesion and motility, that have relevance to pathophysiological issues in dystrophies, ischemia, neuronal diseases, tumor progression. The objective of our investigations is to elucidate activation mechanisms of calpains since association between calpain 3 and titin was shown to be essential to regulate activity of the protease. Here we consider molecular intercations between calpains (1 and 3) and the N1 line region of human titin. We first showed that calcium binding in this region induced a spontaneous agregation. These structural changes could affect the amount of calpain 1 bound to the immunoglobulin-like domain I4 of titin. We further defined the immunoglobulin-like I5 as the calpain 3 binding site that sized in the extreme vincinity of the calpain 1 binding site. Nevertheless, it sounds that calcium dependant changes on titin have no effects on calpain 3 binding. Only structural changes on calpain 3 itself could influence its association with the N1 line region of titin. In light of these results, titin appears to be a strong modulator of calpainolytic activity.
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Gerald Coulis. Interactions moléculaires des calpaïnes 1 et 3 avec la région N1 de la titine humaine. Biologie cellulaire. Université Blaise Pascal - Clermont-Ferrand II, 2007. Français. ⟨NNT : 2007CLF21776⟩. ⟨tel-00718302⟩

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