Search Results - "Salamino, F"

Changes in calpastatin localization and expression during calpain activation: a new mechanism for the regulation of intracellular Ca(2+)-dependent proteolysis by Averna, M, De Tullio, R, Capini, P, Salamino, F, Pontremoli, S, Melloni, E

“…The amount of calpastatin directly available in cytosol is under the control of [Ca2+] and [cyclic AMP]. Prolonged calpain activation also promotes degradation…”
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Changes in calpastatin localization and expression during calpain activation: a new mechanism for the regulation of intracellular Ca2+-dependent proteolysis by Averna, M, De Tullio, R, Capini, P, Salamino, F, Pontremoli, S, Melloni, E

“…The amount of calpastatin directly available in cytosol is under the control of [Ca^sup 2+^] and [cyclic AMP]. Prolonged calpain activation also promotes…”
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Changes in intracellular calpastatin localization are mediated by reversible phosphorylation by Averna, M, de Tullio, R, Passalacqua, M, Salamino, F, Pontremoli, S, Melloni, E

“…We have previously reported that, in neuroblastoma LAN-5 cells, calpastatin is in an aggregated state, close to the cell nucleus [de Tullio, Passalacqua,…”
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Modulation of the Calpain Autoproteolysis by Calpastatin and Phospholipids by Melloni, E., Michetti, M., Salamino, F., Minafra, R., Pontremoli, S.

“…The Ca-induced autoproteolysis calpain proceedes through the sequential formation of two forms of active enzyme with molecular masses of 78 kD and 75 kD,…”
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In vivo degradation of nitric-oxide synthase isozymes by calpain is regulated by HSP90 by Melloni, E, Averna, M, Stifanese, R, De Tullio, R, Salamino, F, Pontremoli, S

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Interaction with HSP90 protects nitric oxide synthases from proteolytic degradation by calpain by Melloni, E, Averna, M, Stifanese, R, De Tullio, R, Salamino, F, Bertuccio, M, Pontremoli, S

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Reversible Inactivation of Calpain Isoforms by Nitric Oxide by Michetti, M., Salamino, F., Melloni, E., Pontremoli, S.

“…S-nitrosylation by sodium nitroprusside, a nitric oxide-generating agent, inactivates, almost completely at neutral pH, the proteolytic activity of the high Ca…”
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Specific degradation of troponin T and I by mu-calpain and its modulation by substrate phosphorylation by Di Lisa, F, De Tullio, R, Salamino, F, Barbato, R, Melloni, E, Siliprandi, N, Schiaffino, S, Pontremoli, S

“…The degradation of troponin (Tn) subunits by calpain was studied by incubating either isolated cardiac Tns or myocardial cryosections with two different…”
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Is the expression of [-G93A(+)] human SOD1 a model to study neurodegenerations? by Stifanese, R, Averna, M, Pedrazzi, M, De Tullio, R, Salamino, F, Pontremoli, S, Melloni, E

“…To relate the alterations occurring in neurodegenerations with Ca2+ homeostasis dysregulation, we analyzed the functional properties of the Ca2+-dependent…”
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Phosphorylation of rat brain calpastatins by protein kinase C by Averna, M., De Tullio, R., Salamino, F., Melloni, E., Pontremoli, S.

“…Calpastatin, the natural inhibitor of calpain, is present in rat brain in multiple forms, having different molecular masses, due to the presence of one (low Mr…”
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Interplay between Calcium dependent proteolysis and neuronal NO production is involved in neurodegeneration by Salamino, F., Averna, M., Stifanese, R., De Tullio, R., Pedrazzi, M., Pontremoli, S., Melloni, E.

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Isozymes of protein kinase C in human neutrophils and their modification by two endogenous proteinases by PONTREMOLI, S, MELLONI, E, SPARATORE, B, MICHETTI, M, SALAMINO, F, HORECKER, B. L

“…Two major protein kinase C (PKC) isozymes, accounting for approximately 95% of the total activity in human neutrophils, were separated by hydroxyapatite…”
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Modulation of calpastatin specificity in rat tissues by reversible phosphorylation and dephosphorylation by Salamino, F, De Tullio, R, Michetti, M, Mengotti, P, Melloni, E, Pontremoli, S

“…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…”
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The plasma membrane calcium pump is the preferred calpain substrate within the erythrocyte by Salamino, F, Sparatore, B, Melloni, E, Michetti, M, Viotti, P L, Pontremoli, S, Carafoli, E

“…The activation of calpain in normal human erythrocytes incubated in the presence of Ca2+ and the Ca2+ ionophore A23187 led to the decline of the…”
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Isolation and characterization of calpain activator protein from bovine brain by Melloni, E, Michetti, M, Salamino, F, Minafra, R, Sparatore, B, Pontremoli, S

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The calpain-calpastatin system in mammalian cells: properties and possible functions by Melloni, E, Salamino, F, Sparatore, B

“…All mammalian cells contain a calcium-dependent proteolytic system, composed by a proteinase, calpain, and an inhibitor, calpastatin. In some cell types an…”
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Effects of a monoclonal anti-calpain antibody on responses of stimulated human neutrophils. Evidence for a role for proteolytically modified protein kinase C by Pontremoli, S, Melloni, E, Damiani, G, Salamino, F, Sparatore, B, Michetti, M, Horecker, B L

“…A monoclonal antibody directed against the Ca2+-requiring proteinase (calpain) of human neutrophils was employed to assess the role of this proteinase in…”
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Protease removal by means of antiproteases immobilized on supports as a potential tool for hemodialysis or extracorporeal blood circulation by Grano, V, Diano, N, Portaccio, M, De Santo, N, Di Martino, S, Rossi, S, De Santo, L S, Salamino, F, Mattei, A, Mita, D G

“…This work studies protease concentration decrease in aqueous solutions in contact with a modified polyethersulphone graft membrane onto which antiproteases…”
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Modulation of inhibitory efficiency of rat skeletal muscle calpastatin by phosphorylation by Pontremoli, S, Viotti, P L, Michetti, M, Salamino, F, Sparatore, B, Melloni, E

“…Rat skeletal muscle calpastatin form is markedly modified in its inhibitory properties by means of a reverse reaction which involves both phosphorylation and…”
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Identification of the Proteolytically Activated Form of Protein Kinase C in Stimulated Human Neutrophils by Pontremoli, Sandro, Michetti, Mauro, Melloni, Edon, Sparatore, Bianca, Salamino, Franca, Horecker, B. L.

“…The proteolytically activated form of protein kinase C has been identified in human neutrophils by using a monoclonal antibody that recognizes both the native…”
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