Neuronal glycogen synthesis contributes to physiological aging

Glycogen is a branched polymer of glucose and the carbohydrate energy store for animal cells. In the brain, it is essentially found in glial cells, although it is also present in minute amounts in neurons. In humans, loss-of-function mutations in laforin and malin, proteins involved in suppressing glycogen synthesis, induce the presence of high numbers of insoluble polyglucosan bodies in neuronal cells. Known as Lafora bodies (LBs), these deposits result in the aggressive neurodegeneration seen in Lafora's disease. Polysaccharide-based aggregates, called corpora amylacea (CA), are also present in the neurons of aged human brains. Despite the similarity of CA to LBs, the mechanisms and functional consequences of CA formation are yet unknown. Here, we show that wild-type laboratory mice also accumulate glycogen-based aggregates in the brain as they age. These structures are immunopositive for an array of metabolic and stress-response proteins, some of which were previously shown to aggregate in correlation with age in the human brain and are also present in LBs. Remarkably, these structures and their associated protein aggregates are not present in the aged mouse brain upon genetic ablation of glycogen synthase. Similar genetic intervention in Drosophila prevents the accumulation of glycogen clusters in the neuronal processes of aged flies. Most interestingly, targeted reduction of Drosophila glycogen synthase in neurons improves neurological function with age and extends lifespan. These results demonstrate that neuronal glycogen accumulation contributes to physiological aging and may therefore constitute a key factor regulating age-related neurological decline in humans

Les societats científiques: la Confederació de Societats Científiques d'Espanya o "la unió fa la força"

Les societats científiques haurien d'actuar com a grups de pressió per al foment de la investigació, millorar l'ensenyança de les ciències, difondre l'esperit científic i promoure l'apreciació social de la ciència. En aquest escrit es descriuen les accions dutes a terme per la Confederación de Sociedades Científicas de España (COSCE), una plataforma única que engloba més de setanta societats científiques i més de trenta mil investigadors provinents de diferents disciplines que ha demostrat ser una eina molt útil per dur a terme aquests objectius.The scientific societies. The confederations of Spanish scientific societies or "United we stand, divided we fall". Scientific societies serve as lobby groups to strengthen research, improve science education, disseminate the scientific spirit and promote public appreciation of science. This text describes the activities undertaken by the Confederación de Sociedades Científicas de España (COSCE) (Spanish Confederation of Scientific Societies). Representing more than 70 scientific societies and over 30,000 researchers from diverse disciplines, COSCE has proved highly effective in achieving its objectives

Les societats científiques: la Confederació de Societats Científiques d'Espanya o "la unió fa la força"

Les societats científiques haurien d'actuar com a grups de pressió per al foment de la investigació, millorar l'ensenyança de les ciències, difondre l'esperit científic i promoure l'apreciació social de la ciència. En aquest escrit es descriuen les accions dutes a terme per la Confederación de Sociedades Científicas de España (COSCE), una plataforma única que engloba més de setanta societats científiques i més de trenta mil investigadors provinents de diferents disciplines que ha demostrat ser una eina molt útil per dur a terme aquests objectius.The scientific societies. The confederations of Spanish scientific societies or "United we stand, divided we fall". Scientific societies serve as lobby groups to strengthen research, improve science education, disseminate the scientific spirit and promote public appreciation of science. This text describes the activities undertaken by the Confederación de Sociedades Científicas de España (COSCE) (Spanish Confederation of Scientific Societies). Representing more than 70 scientific societies and over 30,000 researchers from diverse disciplines, COSCE has proved highly effective in achieving its objectives

Neuronal glycogen synthesis contributes to physiological aging

Glycogen is a branched polymer of glucose and the carbohydrate energy store for animal cells. In the brain, it is essentially found in glial cells, although it is also present in minute amounts in neurons. In humans, loss-of-function mutations in laforin and malin, proteins involved in suppressing glycogen synthesis, induce the presence of high numbers of insoluble polyglucosan bodies in neuronal cells. Known as Lafora bodies (LBs), these deposits result in the aggressive neurodegeneration seen in Lafora's disease. Polysaccharide-based aggregates, called corpora amylacea (CA), are also present in the neurons of aged human brains. Despite the similarity of CA to LBs, the mechanisms and functional consequences of CA formation are yet unknown. Here, we show that wild-type laboratory mice also accumulate glycogen-based aggregates in the brain as they age. These structures are immunopositive for an array of metabolic and stress-response proteins, some of which were previously shown to aggregate in correlation with age in the human brain and are also present in LBs. Remarkably, these structures and their associated protein aggregates are not present in the aged mouse brain upon genetic ablation of glycogen synthase. Similar genetic intervention in Drosophila prevents the accumulation of glycogen clusters in the neuronal processes of aged flies. Most interestingly, targeted reduction of Drosophila glycogen synthase in neurons improves neurological function with age and extends lifespan. These results demonstrate that neuronal glycogen accumulation contributes to physiological aging and may therefore constitute a key factor regulating age-related neurological decline in humans