The Environmental Protection Agency (EPA) and California Air Resources Board (CARB) requirements for high mileage durability of emission components make it necessary to ensure the mechanical robustness of metallic catalytic converters. In addition, the robustness of design features must be assessed in the early design development phase without resorting to vehicle fleet testing. By following established reliability methods, a new approach for time and cost efficient accelerated durability testing was developed, which can account for the combined effects of critical stressors of a metallic catalytic converter. This paper describes the methodology used to determine the critical stressors and their levels in actual operating conditions which were determined by analyzing a broad range of vehicle test information. This information was used to develop a temperature profile and a high vibration load profile for the new life test method. Finally, this paper describes the combination and superimposed introduction of all stressors in a hot vibration/ thermal cycling component bench test. The new time and cost efficient highly accelerated test method can reproduce metallic converter failure modes and can be used to develop the robustness o f mechanical designs for metallic catalytic converters.
GABA A receptor activity is directly modulated by glyceraldehyde 3-phosphate dehydrogenase (GAPDH), a protein with many nonglycolytic moonlighting functions. In addition to playing a role in the phosphorylation of the receptor, GAPDH may also participate in proper receptor trafficking to the plasma membrane. We previously showed that volatile anesthetics affect GAPDH structure and function that may contribute to the manner by which GAPDH modulates the GABA A receptor. In the current study, GAPDH interacted with engineered phospholipid-containing vesicles, preferring association with phosphatidylserine over phosphatidylcholine. Phosphatidyl-serine is known to participate in membrane trafficking of transport proteins and to play a role in GABA A receptor stability and function. We observed that GAPDH promoted the self-association and fusion of phosphatidylserine-rich vesicles as well as decreased membrane fluidity. Isoflurane enhanced each of these GAPDH-mediated events. Isoflurane also increased the binding of GAPDH to the cytoplasmic loop of the GABA A receptor. These observations are consistent with the working model of isoflurane playing a role in the trafficking of membrane proteins. This study is the first to implicate GAPDH and isoflurane in the regulation of GABA A receptor localization, providing insight into the mechanism of action of anesthesia.
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