French bakery manufacturer Bridor has expanded its organic range with new additions in bread and Viennese pastries. Now featuring in the Pure Organic Range is a 140g baguettine; a 280g baguette; a 55g pavé; a 55g grain and cereal Purepavé; a 70g croissant; and a 75g pain au chocolat. All are supplied frozen.The products in this range, certified Ecocert, are made with a minimum of 95% of organic raw materials. Bridor has also taken out any Datems (emulsifiers for Viennese pastries) and vanilline (synthetic flavouring) which has been replaced by a natural vanilla flavouring.Bridor’s ’Eclat du Terroir’ range of artisanal French Viennese pastries are made with an all butter recipe. New to its Prestige range is 130g Eclat du Terroir pain aux raisins and 80g Eclat du Terroir pain au chocolat.The Eclat du Terroir pain au chocolat contains 15% chocolate, whereas the market average is just 12%,” said the firm.It has also launched a new Viennese pastry range called Success, which comprises a 70g croissant and a 80g pain au chocolat both are supplied frozen uncooked.
Harvard researchers are using one of the most comprehensive fungal “family trees” ever created to unlock evolutionary secrets.As reported in PLoS ONE on July 18, Associate Professor of Organismic and Evolutionary Biology Anne Pringle and Ben Wolfe, a postdoctoral fellow at the Faculty of Arts and Sciences (FAS) Center for Systems Biology, studied the genetics of more than 100 species of Amanita mushrooms — about one-sixth of the genus’s total diversity — to create an elaborate phylogeny showing how they are related.Amanita mushrooms have appeared in popular culture ranging from “Fantasia” to the Super Mario Bros. video games. Although it includes a number of edible species, such as the Amanita caesarea, the group is probably best known for its many toxic species, including the death-cap mushroom.Armed with the Amanita family tree, Pringle and Wolfe were able to determine that Amanita evolution has largely been away from species that help decompose organic material and toward those that live symbiotically on trees and their roots. More interestingly, they found that the transition came at a steep price — the loss of the genes associated with breaking down cellulose.“There had been earlier suggestions that this type of gene loss might be taking place, but our study is the first precise test of that hypothesis,” Pringle said. “The idea makes sense: If you’re going to actively form a cooperative relationship with a tree, you probably shouldn’t simultaneously be trying to break it apart and eat it. But it’s a very tricky dance to form these kinds of tight, cooperative interactions, and I think this work shows there is a cost associated with that. You have to change, you have to commit, and it can become a sort of gilded cage — these mushrooms are very successful, but they’re stuck where they are.”Amanita, however, isn’t the only mushroom to form such partnerships.“A number of mushrooms — truffles, chanterelles, and porcini — have figured out how to form these symbiotic relationships with trees,” Wolfe said. “The current thinking is that gene loss is a hallmark of the transition to symbiosis. Amanita is simply the first group we’ve been able to make that determination in because we have a phylogeny with this level of resolution.”That resolution was largely the result of Wolfe’s dedicated collecting work. In addition to many species housed in the Farlow Herbarium, at the Harvard University Herbaria, Wolfe spent months on the road tracking rare species.“Because we wanted to make sure we had a well-sampled family history, I spent a lot of time in the field collecting samples,” said Wolfe, whose stops included London and Hawaii. “The tricky part is that many Amanita mushrooms are extremely rare — in some cases, these species had only been collected once or twice in the last 50 or 60 years — and there are relatively few people with the expertise to distinguish one species from another.”Luckily, Wolfe was able to turn to one such expert — retired Bell Labs engineer Rod Tulloss, now an independent researcher and expert on Amanita mushrooms. Tulloss, whose collection of thousands of Amanita samples is stored in his New Jersey garage, which he years ago converted into a herbarium, is a co-author of the paper. As part of the research, he provided a number of crucial samples to fill out Wolfe and Pringle’s phylogeny.After extracting DNA from the samples, Wolfe used the codes of four different genes to determine how the various species are related. He then used a process called ancestral state reconstruction to show that the mushrooms have switched from being decomposers to being symbiotic with trees only once in their evolutionary history. Once the mushrooms switched to this new symbiotic lifestyle, they didn’t go back to their free-living past.Going forward, research will include studies of the entire genome of several Amanita species in an effort to better understand how symbiosis emerged, and how the mushrooms and trees maintain their partnership.Ultimately, Pringle said, the paper highlights one reason she finds such symbiotic partnerships “intrinsically interesting” — for all their apparent benefits, the cost can be high.“I think the really interesting thing is this idea that once you become symbiotic, some of your machinery is lost,” she said. “It seems like a dead end in some ways — you have to make this change to enter this niche, but once you’re there, you can’t go back — you’ve lost the capacity to be free-living.”
It is already well known that exercise has many salutary effects, but the researchers said the new findings hint at the possibility that exercise and fasting could also help reduce the risk of developing conditions associated with the accumulation of misfolded proteins, such as Alzheimer’s and Parkinson’s. That possibility, however, remains to be explored, the team noted.In their experiments, the researchers analyzed the effects of exercise on cells obtained from the thigh muscles of four human volunteers before and after vigorous biking. Following exercise, the proteasomes of these cells showed dramatically more molecular marks of enhanced protein degradation, including greater levels of cAMP. The same changes were observed in the muscles of anesthetized rats whose hind legs were stimulated to contract repeatedly.Fasting — even for brief periods — produced a similar effect on the cells’ protein-breakdown machinery. Fasting increased proteasome activity in the muscle and liver cells of mice deprived of food for 12 hours, the equivalent of an overnight fast.In another round of experiments, the researchers exposed the liver cells of mice to glucago, the hormone that stimulates production of glucose as fuel for cells and tissues during periods of food deprivation or whenever blood sugar levels drop. The researchers observed that glucagon exposure stimulated proteasome activity and enhanced the cells’ capacity to destroy misfolded proteins.Exposure to the fight-or-flight hormone epinephrine produced a similar effect. Epinephrine, also known as adrenaline, is responsible for stimulating the liver and muscle to mobilize energy reserves to boost heart rate and muscle strength during periods of physiologic stress. Liver cells treated with epinephrine showed marked increases in cAMP, as well as enhanced 26S proteasome activity and protein degradation. Epinephrine exposure also boosted proteasome activity — a marker of protein degradation — in the hearts of living rats. Similarly, when researchers exposed mouse kidney cells to vasopressin — the antidiuretic hormone that helps the body retain water and prevents dehydration — they observed higher levels of protein degradation as well.Taken together, these findings demonstrate that the rate of protein degradation can rise and fall swiftly in a variety of tissues in response to shifting conditions, and that such changes are mediated by fluctuations in hormone levels. This response was surprisingly rapid and short-lived, the scientists noted. For example, exposure to the antidiuretic hormone triggered protein breakdown in kidney cells within five minutes and subsided to pre-exposure levels within an hour, the experiments showed. The findings show that the diverse set of hormones that stimulate cAMP appear to share a common mechanism that alters the composition of cells. These have long been known to modify gene expression, but this latest research reveals they also play a critical role in cellular housecleaning by disposing of proteins that are no longer needed.A new twist on a classic conceptThe new findings build on observations about the physiologic effects of hormones first made by HMS physician Walter Cannon nearly a century ago and elegantly captured in his book “The Wisdom of the Body” (1932). Some of Cannon’s most notable work includes defining the mechanism of action of epinephrine and its role in the fight-or-flight response. Epinephrine is one of the hormones whose action on the protein-disposal machinery is now illuminated by Goldberg’s latest work. In a symbolic coincidence, Goldberg’s lab occupies the very space where Cannon made his observations on the same hormone a hundred years ago.“We think ours is truly a neoclassical discovery that builds on findings and observations made right here, in this very building, nearly a century ago,” Goldberg said.Study co-investigators included Jinghui Zhao and Sudarsanareddy Lokireddy, who is no longer at Harvard.The research was made possible through tissue samples provided by colleagues in Houston, Copenhagen, and Sydney.The work was supported by grants from the National Institutes of Health’s National Institute of General Medical Sciences under grants R01 GM051923-20 and F32 GM128322, the Cure Alzheimer’s Fund, the Muscular Dystrophy Association (MDA-419143), Genentech, and Project ALS. The body’s ability to adapt to changing conditions and shifting physiologic demands is essential to its survival. To ensure cellular performance and the health of the entire organism, each cell must be able to dispose of damaged or unnecessary proteins.Now, a study from the Blavatnik Institute at Harvard Medical School (HMS) shows that intense exercise, fasting, and an array of hormones can activate cells’ built-in protein-disposal systems and enhance their ability to purge defective, toxic, or unneeded proteins.The findings, published Feb. 19 in PNAS, reveal a previously unknown mechanism that is triggered by fluctuations in hormone levels, which signal changes in physiologic conditions.“Our findings show that the body has a built-in mechanism for cranking up the molecular machinery responsible for waste-protein removal that is so critical for the cells’ ability to adapt to new conditions,” said Alfred Goldberg, senior author on the study and professor of cell biology at the Blavatnik Institute.Cellular housecleaning in disease and healthMalfunctions in the cells’ protein-disposal machinery can lead to the accumulation of misfolded proteins, which clog up the cell, interfere with its functions, and, over time, precipitate the development of diseases, including neurodegenerative conditions such as amyotrophic lateral sclerosis and Alzheimer’s.The best-studied biochemical system used by cells to remove junk proteins is the ubiquitin-proteasome pathway. It involves tagging defective or unneeded proteins with ubiquitin molecules — a process known as the “kiss of death” — marking them for destruction by the cell’s protein-disposal unit, known as 26S proteasome. Finding our genomic clockwork Harvard researchers discover a biomarker that can determine both chronological and biological age In pursuit of healthy aging The Daily Gazette Sign up for daily emails to get the latest Harvard news. Harvard study shows how intermittent fasting and manipulating mitochondrial networks may increase lifespan Past research by Goldberg’s lab has shown that this machinery can be activated by pharmacological agents that boost the levels of a molecule known as cAMP, the chemical trigger that initiates the cascade leading to protein degradation inside cells, which in turn switches on the enzyme protein kinase A. The lab’s previous research found that cAMP-stimulating drugs enhanced the destruction of defective or toxic proteins, particularly mutant proteins that can lead to neurodegenerative conditions.The new findings, however, reveal that shifts in physiological states and corresponding changes in hormones can regulate this quality-control process independent of drugs. Goldberg’s lab previously focused on reining in overactive protein breakdown — excessive protein removal that can cause muscle wasting in cancer patients or give rise to several types of muscle atrophy. In fact, a proteasome inhibitor drug Goldberg and his team developed to tamp down protein-disposal activity has been widely used to treat multiple myeloma, a common blood cancer marked by abnormal protein accumulation and overworked proteasomes.The team’s latest work, by contrast, is focused on developing therapies that do just the opposite — invigorate the cell’s protein-disposal machinery when it is too sluggish. These newest findings open the door, at least conceptually, to precisely such treatments.“We believe our findings set the stage for the development of therapies that harness the cells’ natural ability to dispose of proteins and thus enhance the removal of toxic proteins that cause disease,” said study’s lead investigator, Jordan VerPlank, a postdoctoral research fellow in cell biology at the Blavatnik Institute. Such treatments may not necessarily involve the design of new molecules, but instead stimulate the cell’s built-in capacity for quality control.“This is truly a new way of looking at whether we can turn up the cellular vacuum cleaner,” Goldberg said. “We thought this would require the development of new types of molecules, but we hadn’t truly appreciated that our cells continually activate this process.“The beauty and the surprise of it is that such new treatments may involve churning a natural endogenous pathway and harnessing the body’s pre-existing capacity to perform quality control,” he said. Related