There is little doubt that alcohol-related disorders in humans are genetically based. The influence of environmental factors, however, remains unclear. Given that studies of humans are complicated by a multitude of cultural and day-to-day-living factors, researchers in the March issue of Alcoholism: Clinical & Experimental Research use rhesus monkeys to examine genetic and environmental influences on alcohol consumption. Results indicate that, just as with humans, both genetic and environmental factors contribute to variation in alcohol consumption among the non-human primates.
"Rhesus macaques provide a good model for many human diseases due in part to their phylogenetic closeness," said Joseph G. Lorenz, research associate at the Coriell Institute for Medical Research and corresponding author for the study. "Also, like humans, they are highly social, which is important for diseases like alcoholism where there are social factors affecting alcohol consumption. And, finally, because we can control their social environment and precisely measure their exposure to alcohol, whereas human studies often rely on self-reported consumption patterns."
Researchers examined data drawn from an ongoing longitudinal study of genetic and environmental factors affecting the neurobiology, behavior and alcohol consumption among rhesus macaques. For this particular analysis, study authors investigated factors that may have contributed to variation in alcohol consumption among 156 monkeys during a period of 10 years when they were considered adolescents (between 2 and 4 years of age). All belonged to a single extended pedigree, and received identical early rearing backgrounds and subsequent treatments. Alcohol consumption was measured during unfettered and simultaneous access to both aspartame-sweetened (8.4% v/v) alcohol-water solution as well as water for one hour each day during early afternoon for a period of five to seven weeks.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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