Space Shuttle Solid Rocket Booster Lightweight Recovery System

The cancellation of the Advanced Solid Rocket Booster Project and the earth-to-orbit payload requirements for the Space Station dictated that the National Aeronautics and Space Administration (NASA) look at performance enhancements from all Space Transportation System (STS) elements (Orbiter Project, Space Shuttle Main Engine Project, External Tank Project, Solid Rocket Motor Project, & Solid Rocket Booster Project). The manifest for launching of Space Station components indicated that an additional 12-13000 pound lift capability was required on 10 missions and 15-20,000 pound additional lift capability is required on two missions. Trade studies conducted by all STS elements indicate that by deleting the parachute Recovery System (and associated hardware) from the Solid Rocket Boosters (SRBS) and going to a lightweight External Tank (ET) the 20,000 pound additional lift capability can be realized for the two missions. The deletion of the parachute Recovery System means the loss of four SRBs and this option is two expensive (loss of reusable hardware) to be used on the other 10 Space Station missions. Accordingly, each STS element looked at potential methods of weight savings, increased performance, etc. As the SRB and ET projects are non-propulsive (i.e. does not have launch thrust elements) their only contribution to overall payload enhancement can be achieved by the saving of weight while maintaining adequate safety factors and margins. The enhancement factor for the SRB project is 1:10. That is for each 10 pounds saved on the two SRBS; approximately 1 additional pound of payload in the orbiter bay can be placed into orbit. The SRB project decided early that the SRB recovery system was a prime candidate for weight reduction as it was designed in the early 1970s and weight optimization had never been a primary criteria

Cultural and serological analysis of the salmonella status of Australian pig production

The microbiological quality of food of animal origin is receiving widespread scrutiny as outbreaks of food-borne disease are increasingly reported in developed countries. In Australia, the pig industry has embarked on a national program to define and enhance the quality, including microbiological quality, of pig meat. The National Pig Meat Hygiene Program (PMHP) is part of this initiative, and aims to develop baseline data for microorganisms on pig meat, including public health pathogens, and to develop and implement management strategies to enhance the microbial quality of Australia\u27s pig meat production. The study reported here measured salmonella contamination on pig meat and carcases sampled nationwide, and adapted and validated an enzyme linked immunosorbent assay (ELISA) for evaluating the salmonella infection status of pig herds

MHC-IIB Filament Assembly and Cellular Localization Are Governed by the Rod Net Charge

Actin-dependent myosin II molecular motors form an integral part of the cell cytoskeleton. Myosin II molecules contain a long coiled-coil rod that mediates filament assembly required for myosin II to exert its full activity. The exact mechanisms orchestrating filament assembly are not fully understood., negatively-charged regions of the coiled-coil were found to play an important role by controlling the intracellular localization of native MHC-IIB. The entire positively-charged region is also important for intracellular localization of native MHC-IIB.A correct distribution of positive and negative charges along myosin II rod is a necessary component in proper filament assembly and intracellular localization of MHC-IIB

Proteomics analysis of serum protein profiling in pancreatic cancer patients by DIGE: up-regulation of mannose-binding lectin 2 and myosin light chain kinase 2

<p>Abstract</p> <p>Background</p> <p>Pancreatic cancer has significant morbidity and mortality worldwide. Good prognosis relies on an early diagnosis. The purpose of this study was to develop techniques for identifying cancer biomarkers in the serum of patients with pancreatic cancer.</p> <p>Methods</p> <p>Serum samples from five individuals with pancreatic cancer and five individuals without cancer were compared. Highly abundant serum proteins were depleted by immuno-affinity column. Differential protein analysis was performed using 2-dimensional differential in-gel electrophoresis (2D-DIGE).</p> <p>Results</p> <p>Among these protein spots, we found that 16 protein spots were differently expressed between the two mixtures; 8 of these were up-regulated and 8 were down-regulated in cancer. Mass spectrometry and database searching allowed the identification of the proteins corresponding to the gel spots. Up-regulation of mannose-binding lectin 2 and myosin light chain kinase 2, which have not previously been implicated in pancreatic cancer, were observed. In an independent series of serum samples from 16 patients with pancreatic cancer and 16 non-cancer-bearing controls, increased levels of mannose-binding lectin 2 and myosin light chain kinase 2 were confirmed by western blot.</p> <p>Conclusions</p> <p>These results suggest that affinity column enrichment and DIGE can be used to identify proteins differentially expressed in serum from pancreatic cancer patients. These two proteins 'mannose-binding lectin 2 and myosin light chain kinase 2' might be potential biomarkers for the diagnosis of the pancreatic cancer.</p

Myosin II Motor Proteins with Different Functions Determine the Fate of Lamellipodia Extension during Cell Spreading

Non-muscle cells express multiple myosin-II motor proteins myosin IIA, myosin IIB and myosin IIC transcribed from different loci in the human genome. Due to a significant homology in their sequences, these ubiquitously expressed myosin II motor proteins are believed to have overlapping cellular functions, but the mechanistic details are not elucidated. The present study uncovered a mechanism that coordinates the distinctly localized myosin IIA and myosin IIB with unexpected opposite mechanical roles in maneuvering lamellipodia extension, a critical step in the initiation of cell invasion, spreading, and migration. Myosin IIB motor protein by localizing at the front drives lamellipodia extension during cell spreading. On the other hand, myosin IIA localizes next to myosin IIB and attenuates or retracts lamellipodia extension. Myosin IIA and IIB increase cell adhesion by regulating focal contacts formation in the spreading margins and central part of the spreading cell, respectively. Spreading cells expressing both myosin IIA and myosin IIB motor proteins display an organized actin network consisting of retrograde filaments, arcs and central filaments attached to focal contacts. This organized actin network especially arcs and focal contacts formation in the spreading margins were lost in myosin IIÂ cells. Surprisingly, myosin IIB̂ cells displayed long parallel actin filaments connected to focal contacts in the spreading margins. Thus, with different roles in the regulation of the actin network and focal contacts formation, both myosin IIA and IIB determine the fate of lamellipodia extension during cell spreading

Cortical Mechanics and Meiosis II Completion in Mammalian Oocytes Are Mediated by Myosin-II and Ezrin-Radixin-Moesin (ERM) Proteins

Analysis of mouse oocyte mechanics shows that effective tension drops 6-fold from prophase I to metaphase II; the metaphase II egg has a 2.5-fold tension differential between the cortex over the spindle and the opposite cortex. Manipulation of actin, myosin-II, or ERMs alters tension levels and induces spindle abnormalities during meiosis II