One pathway of apoptosis, observed in animal systems, can be induced by the deprivation of serum from tissue culture cells, leading to the release of cytochrome c from mitochondria. Compartmentalization of caspases and their cofactors suggests that two major apoptotic pathways exist. Caspases are synthesized as zymogens that are activated by proteolytic cleavage at specific aspartic acid residues in the P1 position ( 8). This apoptotic cascade is regulated by both initiators and inhibitors and can be activated by diverse stimuli. Apoptosis is triggered by the sequential activation of cysteine proteases known as caspases, which results in protein cleavage and the breakdown of DNA molecules. Extensive study over the past decade has illuminated the biological and molecular mechanisms of the regulation of apoptosis in animal systems ( 2– 7). This functionally conserved process, known as programmed cell death (PCD) 5 or apoptosis, is genetically regulated and associated with distinct morphological and biochemical characteristics. The current results demonstrated the existence of a novel plant IAP-like protein that prevents caspase activation in Arabidopsis and showed that a plant anti-apoptosis gene functions similarly in plant and animal systems.Īll living organisms use a process of cell suicide to achieve and maintain homeostasis during normal development as well as in response to environmental stress or during pathogen challenge ( 1). Overexpression of AtILP also attenuated effector protein-induced cell death and increased the growth of an avirulent bacterial pathogen. In AtIPL transgenic plants, suppression of cell death was accompanied by inhibition of caspase activation and DNA fragmentation. Transgenic Arabidopsis lines overexpressing AtILP exhibited anti-apoptotic activity when challenged with the fungal toxin fumonisin B1, an agent that induces apoptosis-like cell death in plants. The anti-apoptotic activity of the AtILP N-terminal domain observed in plants was reproduced in an animal system. In contrast to the C-terminal RING domain of AtILP, which did not inhibit the activity of caspase-3, the N-terminal region, despite displaying no homology to known BIR domains, potently inhibited the activity of caspase-3 in vitro and blocked TNF-α/ActD-induced apoptosis. The expression of AtILP in HeLa cells conferred resistance against tumor necrosis factor (TNF)-α/ActD-induced apoptosis through the inactivation of caspase activity. Arabidopsis IAP-like protein (AtILP) contained a C-terminal RING finger domain but lacked a baculovirus IAP repeat (BIR) domain, which is essential for anti-apoptotic activity in other IAP family members. Screw terminals enable the connection of two conductors in a terminal chamber and are characterized by good contact quality with little heating.A novel Arabidopsis thaliana inhibitor of apoptosis was identified by sequence homology to other known inhibitor of apoptosis (IAP) proteins. Depending on the design, for connection cross sections of 0.08 - 4 mm².
The screw terminals are suitable for solid wires and stranded wires with end sleeves. An integrated wire protection or a lift system protect the wire when it is connected. The stripped wire is clamped and contacted directly or indirectly by a screw. The connection technology of the screw terminals, which has been tried and tested a million times, is based on a metallic clamping body that is built into an insulating body. Many of the pluggable terminal block versions have matching THR headers available in tape and reel packaging, making them well suited for automated assembly. Our core offering of direct solder terminal block versions can accommodate wires ranging in size from twenty-eight up to and including twelve gauge. METZ CONNECT offers a variety of screw type terminal blocks for your wire to board connectivity needs.