... the regulation of detyrosination. Here, we found that intracellular Ca 2+ is required for efficient MT detyrosination. Furthermore, we show that the Ca 2+ -dependent proteases calpains 1 and 2 (CAPN1 and CAPN2, respectively) regulate MT detyrosination in VASH1- and SVBP-overexpressing human embryonic kidney...

... involving calpain-mediated activation of Bax and mitochondrial release of apoptosis-inducing factor (AIF). However, whether these two mechanisms represent distinct pathways for PARP1-induced necrosis, or whether they are simply different components of the same pathway has yet to be tested. Mouse embryonic...

... plays a key role in such crosstalk at the leading edge of migrating cells in order to promote lamellipodial formation. However, the mechanism underlying the link between microtubules and Rac1 activation remains unclear. Here, we show that calpain-6 (CAPN6), a non-proteolytic calpain with microtubule...

... of Fam38A in epithelial cells inactivates endogenous β1 integrin, reducing cell adhesion. Fam38A mediates integrin activation by recruiting the small GTPase R-Ras to the ER, which activates the calcium-activated protease calpain by increasing Ca 2+ release from cytoplasmic stores. Fam38A-induced integrin...

... levels in cortical neurons and in a model of cerebral ischemia. Kidins220/ARMS downregulation is triggered by overactivation of NMDARs containing NR2B subunits and subsequent Ca 2+ influx, and involves a dual mechanism: rapid cleavage by the Ca 2+ -dependent protease calpain and calpain-independent...

...Magali Louis; Nadège Zanou; Monique Van Schoor; Philippe Gailly Myoblast migration is a key step in myogenesis and regeneration. It allows myoblast alignment and their fusion into myotubes. The process has been shown to involve m-calpain or μ-calpain, two Ca 2+ -dependent cysteine proteases. Here...

... place. Members of the calpain family of calcium-dependent proteases are believed to have a central role in these processes, possibly through the regulation of focal adhesion dynamics. The ubiquitous calpains, calpain 1 (μ-calpain) and calpain 2 (m-calpain), are heterodimers consisting of large catalytic...

... and the mechanisms that regulate their high turnover are unknown at present. The cysteine protease calpain is involved in the regulation of cell migration in part by promoting either formation or disassembly of adhesion sites. Despite the fact that many known substrates of calpain are also structural components...

...Santos J. Franco; Anna Huttenlocher The calpain family of proteases has been implicated in cellular processes such as apoptosis, proliferation and cell migration. Calpains are involved in several key aspects of migration, including: adhesion and spreading; detachment of the rear; integrin...

...Katarzyna Bialkowska; Takaomi C. Saido; Joan E. B. Fox In this study, we used cultured cells spreading on β3 integrin substrates to examine the possibility that spectrin is involved in signal transduction. Spectrin clustered with specialized calpain-induced β3 integrin signaling complexes...

... in the pulmonary epithelium of foxj1 +/+ and foxj1 -/- mice. In the absence of Foxj1, the expression of calpastatin, an inhibitor of the protease calpain, decreased. RNase protection confirmed the decrease in calpastatin expression and decreased calpastatin was detected in the proximal pulmonary epithelium...

...Amit Bhatt; Irina Kaverina; Carol Otey; Anna Huttenlocher Cell migration requires the regulated and dynamic turnover of adhesive complexes. We have previously demonstrated that the calcium-dependent protease, calpain, regulates the organization of adhesive complexes and cell detachment during cell...

.... In the adhesive regime where rear detachment limits the rate of cell migration, cell speed has an inverse relationship to the amount of integrin released at the rear of the cell. At high cell-substratum adhesiveness, calpain, a Ca 2+ -dependent protease, is also involved in release of cytoskeletal linkages during...

..., since calpain inhibitors I and II both inhibit neuronal death and suppress actin fragmentation. In contrast, caspase (ICE family) inhibitors, though effective in delaying neuronal death, do not prevent actin cleavage or DNA fragmentation. These results indicate a key role for calpain-like proteases...

...Sassan M. Azarian; Cassandra L. Schlamp; David S. Williams ABSTRACT Calpain II was purified to apparent homogeneity from bovine neural retinas. It was found to be biochemically similar to brain calpain II, purified by the same procedure, with respect to: subunit mobility in SDS-polyacrylamide gel...