The calpain-calpastatin system in mammalian cells: properties and possible functions

WITHDRAWN: Respiratory exposure to inert particulate matter during pregnancy leads to oxidative stress and cardiac proteome remodeling

“…There was a robust correlation between pregnancy and S100a8 expression; this protein is a key modulator in the inflammatory response with roles in promoting leukocyte recruitment and cytokine secretion ( Figure 2A ) (28). In addition to inflammatory upregulation, we also found an increase in proteins that aid cardiac function during pregnancy such as calpastatin (CAST) and Rad23 homolog b (Rad23b); specifically, CAST, an inhibitor of calpain, was upregulated, thus preventing protein degradation in the cardiac muscle tissue (29–31). To further understand the proteins that were upregulated and downregulated, we generated a volcano plot that indicates the five most significantly upregulated and downregulated proteins during pregnancy ( Figure 2B ).…”

WITHDRAWN: Respiratory exposure to inert particulate matter during pregnancy leads to oxidative stress and cardiac proteome remodeling

“…There was a robust correlation between pregnancy and S100a8 expression; this protein is a key modulator in the inflammatory response with roles in promoting leukocyte recruitment and cytokine secretion ( Figure 2A ) (28). In addition to inflammatory upregulation, we also found an increase in proteins that aid cardiac function during pregnancy such as calpastatin (CAST) and Rad23 homolog b (Rad23b); specifically, CAST, an inhibitor of calpain, was upregulated, thus preventing protein degradation in the cardiac muscle tissue (29–31). To further understand the proteins that were upregulated and downregulated, we generated a volcano plot that indicates the five most significantly upregulated and downregulated proteins during pregnancy ( Figure 2B ).…”

Single Nucleotide Polymorphisms of Leptin and Calpain/Calpastatin in Key Traits of Pork Meat Quality

“…The two common forms of calpain (µ-calpain, m-calpain) share a similar structure [ 95 , 96 , 97 , 98 ]. These forms are heterodimers, each one consisting of a large catalytic subunit (80 kDa) and a smaller regulatory subunit (28 kDa) that undergoes autolysis in the presence of calcium [ 99 ].…”

“…It has similarities with the typical structure of thiol proteinases, including essential amino acid residues like Cys and His/Asn [ 95 , 96 , 97 , 98 ]. Domain III contains amino acid residues that are crucial for interaction with specific ligands [ 98 ]. It is thought to bind to phospholipids, potentially interacting with cell membranes [ 100 ].…”

“…It is thought to bind to phospholipids, potentially interacting with cell membranes [ 100 ]. Domain IV has four calcium-binding sites like calmodulin [ 93 , 98 ]. …”

“…Domain II is the active site. It has similarities with the typical structure of thiol proteinases, including essential amino acid residues like Cys and His/Asn [ 95 , 96 , 97 , 98 ].…”

WITHDRAWN: Respiratory exposure to inert particulate matter during pregnancy leads to oxidative stress and cardiac proteome remodeling

“…There was a robust correlation between pregnancy and S100a8 expression; this protein is a key modulator in the inflammatory response with roles in promoting leukocyte recruitment and cytokine secretion ( Figure 2A ) (28). In addition to inflammatory upregulation, we also found an increase in proteins that aid cardiac function during pregnancy such as calpastatin (CAST) and Rad23 homolog b (Rad23b); specifically, CAST, an inhibitor of calpain, was upregulated, thus preventing protein degradation in the cardiac muscle tissue (29–31). To further understand the proteins that were upregulated and downregulated, we generated a volcano plot that indicates the five most significantly upregulated and downregulated proteins during pregnancy ( Figure 2B ).…”

Single Nucleotide Polymorphisms of Leptin and Calpain/Calpastatin in Key Traits of Pork Meat Quality

“…The two common forms of calpain (µ-calpain, m-calpain) share a similar structure [ 95 , 96 , 97 , 98 ]. These forms are heterodimers, each one consisting of a large catalytic subunit (80 kDa) and a smaller regulatory subunit (28 kDa) that undergoes autolysis in the presence of calcium [ 99 ].…”

“…It has similarities with the typical structure of thiol proteinases, including essential amino acid residues like Cys and His/Asn [ 95 , 96 , 97 , 98 ]. Domain III contains amino acid residues that are crucial for interaction with specific ligands [ 98 ]. It is thought to bind to phospholipids, potentially interacting with cell membranes [ 100 ].…”

“…It is thought to bind to phospholipids, potentially interacting with cell membranes [ 100 ]. Domain IV has four calcium-binding sites like calmodulin [ 93 , 98 ]. …”

“…Domain II is the active site. It has similarities with the typical structure of thiol proteinases, including essential amino acid residues like Cys and His/Asn [ 95 , 96 , 97 , 98 ].…”

WITHDRAWN: Respiratory exposure to inert particulate matter during pregnancy leads to oxidative stress and cardiac proteome remodeling

“…There was a robust correlation between pregnancy and S100a8 expression; this protein is a key modulator in the inflammatory response with roles in promoting leukocyte recruitment and cytokine secretion ( Figure 2A ) (28). In addition to inflammatory upregulation, we also found an increase in proteins that aid cardiac function during pregnancy such as calpastatin (CAST) and Rad23 homolog b (Rad23b); specifically, CAST, an inhibitor of calpain, was upregulated, thus preventing protein degradation in the cardiac muscle tissue (29–31). To further understand the proteins that were upregulated and downregulated, we generated a volcano plot that indicates the five most significantly upregulated and downregulated proteins during pregnancy ( Figure 2B ).…”

Single Nucleotide Polymorphisms of Leptin and Calpain/Calpastatin in Key Traits of Pork Meat Quality

“…The two common forms of calpain (µ-calpain, m-calpain) share a similar structure [ 95 , 96 , 97 , 98 ]. These forms are heterodimers, each one consisting of a large catalytic subunit (80 kDa) and a smaller regulatory subunit (28 kDa) that undergoes autolysis in the presence of calcium [ 99 ].…”

“…It has similarities with the typical structure of thiol proteinases, including essential amino acid residues like Cys and His/Asn [ 95 , 96 , 97 , 98 ]. Domain III contains amino acid residues that are crucial for interaction with specific ligands [ 98 ]. It is thought to bind to phospholipids, potentially interacting with cell membranes [ 100 ].…”

“…It is thought to bind to phospholipids, potentially interacting with cell membranes [ 100 ]. Domain IV has four calcium-binding sites like calmodulin [ 93 , 98 ]. …”

“…Domain II is the active site. It has similarities with the typical structure of thiol proteinases, including essential amino acid residues like Cys and His/Asn [ 95 , 96 , 97 , 98 ].…”