Wow! It seems that all the exciting sience news today are coming from my school:
North Carolina State University researchers have gleaned insight into the genes involved in resistance to nicotine in the lab rat of many gene studies – Drosophila melanogaster, the fruit fly. The research team led by Dr. Greg Gibson, William Neal Reynolds Professor of Genetics, and his graduate student, Gisele Passador-Gurgel, found that regulation of levels of a certain enzyme – ornithine amino transferase – plays an important role in establishing how long flies can tolerate nicotine. Gibson says that the amount of enzyme seems to do two things – it influences flies’ ability to strip away toxins, and it helps establish how much the drug stimulates them.
An interesting sidelight in the study was the observation that flies from North Carolina are more resistant to nicotine than flies from California. The researchers found that 30 percent of the North Carolina flies lived longer after exposure to nicotine – thus were more resistant to nicotine – than all but one California fly.
Gibson isn’t sure why, although he has a few theories. North Carolina flies may garner resistance from living near tobacco fields. California flies may have genetically lost their ability to resist nicotine. Many pesticides are nicotine-based, too, so the flies could have evolved some response to insecticides.
Researchers at North Carolina State University have discovered that repetitive flexing movements increase the speed and depth at which tiny particles are absorbed through the skin, a finding that could have major implications in medical, consumer and industrial fields. Dr. Nancy Monteiro-Riviere, professor of investigative dermatology and toxicology at NC State’s College of Veterinary Medicine, and graduate student Jillian Rouse, working with Dr. Andrew R. Barron, professor of chemistry and materials science at Rice University, made the discovery by exposing the tiny particles – the soccer-ball shaped materials known as fullerenes or buckyballs which are much smaller than the head of a pin – to pig skin.
For the first time, experimental results indicate that it is possible to use a resin filter to remove harmful prion proteins from the blood of an infected animal, a finding that has major implications for the removal of infectious prion proteins – the agents associated with variant Creutzfeldt-Jakob disease, mad cow disease, scrapie and other prion diseases in animals – during blood transfusions.Dr. Ruben Carbonell, Frank Hawkins Kenan Professor of Chemical and Biomolecular Engineering and director of the Kenan Institute for Engineering, Technology and Science at North Carolina State University, and scientists from the University of Maryland at Baltimore’s VA Medical Center, the American Red Cross and ProMetic BioSciences, a biotechnology company, developed small resin beads with molecules that are able to bind to harmful prion proteins. The beads serve as an adsorption filter, capturing the bad proteins and allowing other blood components to be effectively cleansed of the prion-disease-causing agents.
Reports of blue crabs exhibiting both male and female sex characteristics in the Chesapeake Bay and other water systems raise a red flag about the environment in which the crabs live, says Dr. Gerald A. LeBlanc, professor of environmental and molecular toxicology at North Carolina State University.