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Blood-Borne Molecule Helps Regulate Blood-Vessel Integrity
Although maintaining the integrity of blood vessel walls is essential for life, well-controlled temporary leakage of blood contents through the walls of blood vessels into the tissues is a hallmark of inflammation. Although the molecule S1P is known to act on the cells that line blood vessels (endothelial cells) to regulate the permeability of blood vessel walls, the in vivo of SIP in this process remains unknown, and whether it has a role in inflammation has not been determined. In a new study, Shaun Coughlin and colleagues, at UCSF, San Francisco, have shed light on these issues, revealing that mice that lack S1P selectively in plasma (the liquid component of blood) have increased leakage from the blood vessels in response to a variety of stimuli, including inflammatory ones. As the leakage was reversed by treatment with either S1P-containing red blood cells or an agonist for the protein to which SIP binds, the authors conclude that S1P in the blood regulates blood-vessel integrity and prevents potentially lethal decreases in blood volume after exposure to leak-inducing stimuli.
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Published Study Shows VNUS ClosureFAST(TM) System Significantly Superior To Laser For Varicose Vein Treatment
VNUS(R) Medical Technologies, Inc. (Nasdaq: VNUS), a worldwide leader in medical devices for the minimally invasive treatment of venous reflux disease, announced that the Journal of Vascular & Interventional Radiology, the prestigious monthly publication of the Society of Interventional Radiology, has published a study showing the VNUS ClosureFAST(TM) system for radiofrequency (RF) thermal ablation to be "significantly superior" to endovenous laser (EVL) for treating venous reflux, the underlying cause of symptomatic varicose veins. Drugshop to buy zoloft online and other pills.
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Patching Gaps In Global Pneumococcal Vaccination
Since 2000, U.S. infants have been routinely immunized against pneumococcal (Streptococcus pneumoniae) infection, but the existing vaccine"s expense puts it out of reach for most developing countries, where almost one million children die from pneumococcal infections each year. Richard Malley, MD, of the Division of Infectious Diseases at Children"s Hospital Boston, is at work on a pneumococcal vaccine that meets developing countries" needs it can be made cheaply, withstands high temperatures without refrigeration, and can be given without needles, avoiding the need for sterile procedures and medical professionals to administer it. Also, because it is a whole-cell vaccine, it should provide protection against virtually all of the 91 pneumococcal serotypes that infect people worldwide. (The U.S. vaccine covers only seven.)
Medical Devices

New Nanoparticles Could Revolutionise Therapeutic Drug Discovery

A revolutionary new protein stabilisation technique has been developed by scientists funded by the Biotechnology and Biological Sciences Research Council (BBSRC) which could lead to 30 per cent more proteins being available as potential targets for drug development opening up exciting possibilities in drug discovery. Understanding the structure of proteins is a vital first step in developing new drugs, but to date, drug development has been slowed because due to their instability, proteins are difficult to work with in lab conditions. However, using nanoparticles, scientists from the Universities of Birmingham and Warwick have found a way to preserve membrane proteins intact, enabling detailed analysis of their structure and molecular functions. These new findings, which have just been published online in the Journal of the American Chemical Society, will give scientists access to previously ignored proteins deemed too unstable to work with. Professor Michael Overduin, from the University of Birmingham, who led the study, explained: "We have shown how a polymer can wrap around and preserve membrane proteins intact in stable nanoparticles. Membrane proteins are the most valuable but technically challenging targets for drug discovery. Finding a gentle solution that preserves their structure and activity, yet is robust enough for experimental interrogation, has eluded scientists for decades, but is now available." Using a polymer - styrene maleic acid lipid particles (SMALPs), the researchers solubilised a pair of membrane proteins. They found that not only did the proteins maintain their folded structure, binding and enzyme activities in the SMALPs, but also that using the nanoparticles allowed them to be simply and rapidly used for virtually any laboratory analysis. Advantages of SMALPs over traditional ways to solubilise proteins such as detergents include enhanced stability, activity and spectral quality of the protein membranes. Dr Tim Dafforn who jointly ran the study, said: "In the past, studies have concentrated largely on soluble proteins as membrane proteins are so difficult to make. However, the discovery of the SAMLPs removes this barrier and opens up access to membrane proteins - this has exciting clinical implications as it may enable drug discovery on receptors that are currently too difficult to produce or study by current methods." Commenting on the findings, BBSRC Chief Executive Professor Doug Kell, said: "The attrition rate in developing new drugs is phenomenal. Only a tiny fraction make it into the clinic to benefit patients. Research such as this that can help to increase the number of potential targets will mean a larger pipeline for scientists to develop new drugs from and, ultimately more, better drugs for patients. Fundamental bioscience working in coordination with medical research is vital to deliver new, effective drugs." Biotechnology and Biological Sciences Research Council


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