Role for caspase-2 during pore-forming toxin-mediated apoptosis

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Role for caspase-2 during pore-forming toxin-mediated apoptosis

Pore-forming toxins (PFT) form the largest family of secreted toxins from pathogenic bacteria. Staphylococcus aureus produces different hemolysins, and α-hemolysin is one of the well-studied PFTs for which the X-ray structure of the pore is available. These toxins form heptameric pores of 1–2 nm in size in cell membranes, leading to various outcomes, including apoptotic cell death, in the host ...

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Caspase-2 is an initiator caspase responsible for pore-forming toxin-mediated apoptosis.

Bacterial pathogens modulate host cell apoptosis to establish a successful infection. Pore-forming toxins (PFTs) secreted by pathogenic bacteria are major virulence factors and have been shown to induce various forms of cell death in infected cells. Here we demonstrate that the highly conserved caspase-2 is required for PFT-mediated apoptosis. Despite being the second mammalian caspase to be id...

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Lysenin: a sphingomyelin specific pore-forming toxin.

Sphingomyelin is a major sphingolipid in mammalian cells. Recent results indicate that sphingomyelin is a reservoir of lipid second messengers, ceramide and sphingosine-1-phosphate. Sphingomyelin is also a major component of sphingolipid and cholesterol-rich membrane domains (lipid rafts). Lysenin is a pore-forming toxin that specifically binds sphingomyelin. The binding of lysenin to sphingomy...

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Pore Formation Mechanism of Staphylococcal Pore- forming Toxin

Y. Tanaka and M. Yao (Hokkaido Univ.) Pathogenic bacteria express pore-forming toxins (PFTs) to attack host cells. PFTs are expressed as soluble monomeric proteins, which assemble to prepore oligomer on the target cells. After forming prepore, conformational change occurs, and then the pore is formed. Although the crystal structures of monomer and pore have been determined, the detailed mechani...

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Pore-forming activity of alpha-toxin is essential for clostridium septicum-mediated myonecrosis.

Clostridium septicum alpha-toxin is a beta-barrel pore-forming cytolysin that is functionally similar to aerolysin. Residues important in receptor binding, oligomerization, and pore formation have been identified; however, little is known about the activity of the toxin in an infection, although it is essential for disease. We have now shown that deletion of a small portion of the transmembrane...

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ژورنال

عنوان ژورنال: Cell Cycle

سال: 2012

ISSN: 1538-4101,1551-4005

DOI: 10.4161/cc.22046