The sugar industry began funding research that cast doubt on sugar’s role in heart disease (by pointing the finger at fat) in the 1960s.
Adam Rifkin stashed this in Nutrition!
Dr Tara Narula video:Â http://cbsnews.com/videos/how-to-lose-the-sweet-tooth-and-curb-added-sugar/
Source of text quoted below: http://cbsnews.com/news/sugar-industry...
Stashed in: Awesome, Heart, Harvard, 1960s, Sugar, Food Industry, Science Studies, Cognitive Bias
The sugar industry began funding research that cast doubt on sugar’s role in heart disease - in part by pointing the finger at fat - as early as the 1960s, according to an analysis of newly uncovered documents.
The analysis published Monday is based on correspondence between a sugar trade group and researchers at Harvard University, and is the latest example showing how food and beverage makers attempt to shape public understanding of nutrition.
In 1964, the group now known as the Sugar Association internally discussed a campaign to address “negative attitudes toward sugar” after studies began emerging linking sugar with heart disease, according to documents dug up from public archives. The following year the group approved “Project 226,” which entailed paying Harvard researchers today’s equivalent of $48,900 for an article reviewing the scientific literature, supplying materials they wanted reviewed, and receiving drafts of the article.
The resulting article published in 1967 concluded there was “no doubt” that reducing cholesterol and saturated fat was the only dietary intervention needed to prevent heart disease. The researchers overstated the consistency of the literature on fat and cholesterol, while downplaying studies on sugar, according to the analysis.
“Let me assure you this is quite what we had in mind and we look forward to its appearance in print,” wrote an employee of the sugar industry group to one of the authors.
The sugar industry’s funding and role were not disclosed when the article was published by the New England Journal of Medicine. The journal, which did not require such disclosures at the time, began requesting author disclosures in 1984.
In an editorial published Monday that accompanied the sugar industry analysis, New York University professor of nutrition Marion Nestle noted that for decades following the study, scientists and health officials focused on reducing saturated fat, not sugar, to prevent heart disease.
While scientists are still working to understand links between diet and heart disease, concern has shifted in recent years to sugar and carbohydrates, and away from fat​, Nestle said.
Wow the Sugar Association is diabolical.
Top Reddit comment:
Sugar biologist here. The role of sugar and carbohydrates in disease has started to gain traction and there is a small, but loud community of us 'glycobiologists' that is increasingly growing in number as time goes by. In fact, MIT once predicted that sugar biology will revolutionize medicine in the 21st century, because it may be a big piece of the puzzle towards our understanding of many complex diseases, the root causes of which we still haven't really understood well nearly 2 decades after we've cracked the genetic code.Â
What do you think of when you think of the word 'sugar'? You're probably thinking of table sugar and high fructose corn syrup, both of which you consume in food. You might also be thinking about glucose, the key energy carrying molecule every cell in your body burns for energy in order to maintain life. For the longest time that's what most people in the scientific community thought when they thought about 'sugars'. But there's a different and an extremely important role sugars play in regulating life. After a huge number of proteins are made that are encoded in your genome, they are modified further by a theoretically massive set of sugars. This entire set of sugars in known as 'the glycome' (akin to the genome, proteome, metabolome, etc.). Just how big is the glycome? Well, many scientists have reported that it is theoretically 'many orders of magnitude more complex than the genome' and that it is 'one of the most complex entities known in nature'. When you think about it, taking the genetic products and modifying them with sugars is almost like a quantum leap in complexity for life. Genetics and DNA would be tantamount to our understanding of classical physics. Just as classical physics can't explain all physical phenomena, we now know that a huge portion of the complexity of life exists outside what can be coded directly in DNA (for example the glycome). The study of sugars, their modifications on proteins, and the functional role that this has could be considered like the quantum revolution that physicists needed to explain the nature of fundamental particles and small scale stuff.Â
But there's one type of modification by sugar that's quite special. Back many decades ago two scientists by the names of Krebs and Fischer discovered that proteins were modified by phosphorylation (phospho groups) to regulate their activity. To simply put it (in reality it isn't this simple), when a protein is phosphorylated it is 'turned on', and when it is dephosphorylated it is 'turned off'. Kinases are enzymes that add phospho groups and phosphatases are enzymes that remove phospho groups from proteins. There are literally hundreds and hundreds, if not thousands, of different kinases and phosphatases that exist in order to regulate the phosphorylation states of all proteins in a cell. For their work, Krebs and Fischer won the Nobel Prize in medicine (to illustrate the importance of protein physiology regulation). However, nearly two decades later after Krebs and Fischer discovered protein phosphorylation, scientists soon discovered that hundreds and thousands of proteins inside of a cell were also modified by a single sugar known as N-acetylglucosamine (GlcNAc for short). This observation was later dubbed 'the O-GlcNAc modificaiton' and 'O-GlcNAc'. After a ton of grunt work, scientists were able to show that what really, really made O-GlcNAc interesting was that O-GlcNAc appeared to modify proteins often times at the same exact sites where proteins were phosphorylated (remember how important that was for Krebs and Fischer?). And what really, really, really, really made the addition of O-GlcNAc super duper special was the discovery that only 2 enzymes regulate the addition and removal of O-GlcNAc to proteins--an enzyme known as OGT (which adds it) and OGA (which removes it). That's it! Contrast that to the hundreds and thousands of different kinases and phosphatases that are needed to regulate the phosphorylation states of the proteome. O-GlcNAc is much more conserved. The importance of O-GlcNAcylation can not be overstated. Think of O-GlcNAc as a 'cap' on the sites of proteins where they are phosphorylated. In order to phosphorylate and turn proteins 'on', you must first remove O-GlcNAc to clear the site for modification by phosphorylation. In otherwords, O-GlcNAc is also a master regulator of the entire physiology of proteins inside of a cell. It is like the yin-to-the-yang of phosphorylation. This observation has now been called the 'Yin-Yang hypothesis'. After 30 years of more work, we are increasingly understanding the importance of O-GlcNAc. For example, nearly every type of protein involved in epigenetic modifications and regulation is now known to be modified by O-GlcNAc. Nearly every type of transcription factor (proteins that help to turn on a gene) are modified by O-GlcNAc. RNA polymerase II, the main protein that decodes your DNA, is heavily O-GlcNAcylated and doesn't work right unless it is coated with sugar. Histones (the proteins that your DNA wraps around) are modified by O-GlcNAc, meaning O-GlcNAc is directly part of the histone code. In fact, if you were to stain your chromatin (basically your DNA) for O-GlcNAc it would light up like a Christmas tree, meaning your DNA mass and all of the proteins on it are absolutely covered in sugar. O-GlcNAc also regulates cytoskeletal structure and dynamics, many proteins inside of the mitochondria, mitochondrial cellular mechanics, modifies the proteins that regulate circadian rhythm.....the list goes on.Â
So what does this have to do with 'sugar consumption' and heart disease? Well, what I didn't discuss yet is where exactly the GlcNAc that is used for the O-GlcNAc modification comes from. When most people think of glucose metabolism, they think about using it for glycolysis and oxidative phoshorylation--i.e. using glucose as fuel for a cell. However, what many scientists outside of glycobiology and biochemistry and the general lay public might not have ever heard of is the fact that roughly 2-5% of all glucose turn over is shunted away from glycolysis and energy production and down a biochemical pathway known as the hexosamine biosynthetic pathway (HBP). The HBP does several transformations to glucose, but ultimately it produces a very special metabolite known as UDP-GlcNAc. UDP-GlcNAc is THE substrate for OGT (remember that's the enzyme that adds O-GlcNAc to proteins). While 2-5% of glucose shunting down the HBP doesn't seem like a lot, it really is because of the massive turn over rate of glucose that exists in a cell. In fact, I've repeatedly been told that next to ATP, UDP-GlcNAc is the next most abundant molecule found in a cell (further illustrating its importance). If you can finally see the big picture here, we are, for the first time linking carbohydrate metabolism, carbohydrate uptake, carbohydrate fluxes, and 'sugar consumption' directly to virtually every single aspect of physiology inside of a cell since the O-GlcNAc modification modifies so many things like what was discussed above. The link is O-GlcNAc and the HBP with glucose. More directly, how is this relevant to heart disease? There are many, many things to discuss on this topic alone, but I will defer to the abstracts posted here to get you started:
Cardiac O-GlcNAc signaling is increased in hypertrophy and heart failure.http://www.ncbi.nlm.nih.gov/pubmed/22128088
O-linked β-N-acetylglucosamine transferase (OGT) is indispensable in the failing heart:
http://www.pnas.org/content/107/41/17797.full
Spliced X-box Binding Protein 1 Couples the Unfolded Protein Response to Hexosamine Biosynthetic Pathway http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3959665/
Protein O-GlcNAcylation and Cardiovascular (Patho)physiology
http://www.jbc.org/content/289/50/34449.full
The point is just to explain to you exactly how sugar might, and is probably involved in the development of heart disease.We've long observed that diabetic patients have higher risks for things like heart disease and cardiomyopathy. What do diabetics have? Of course they have dysregulated sugar metabolism which will probably go on to aversely affect normal O-GlcNAc cycling. Maybe O-GlcNAc is the reason why diabetics are more prone to heart disease. In fact, many major disease that affect millions of people every year such as cancer, diabetes, and even Alzheimer's are all associated with dysregulated sugar metabolism and abnormal patterns of O-GlcNAc. Now you might have some inkling as to how sugar metabolism is, probably, in some way involved in the development and progression of many major diseases.Â
TL; DR: Scientists discovered that sugars play an important role in regulating how proteins work. The sugar that does that comes from glucose and glucose consumption. The links between abnormal 'sugar uptake' and conditions like heart disease are becoming increasingly clear. The science on the molecular level is there!
Appealing to teens' impulse to rebel can curb unhealthy eating. When healthy eating was suggested as a way to take a stand against manipulative and unfair practices of the food industry, 8th graders were more likely to chose healthier food:Â
http://www.medicalnewstoday.com/releases/312894.php
200 Reddit comments:
https://reddit.com/r/science/comments/53a556/appealing_to_teens_impulse_to_rebel_can_curb/
11:25 PM Sep 17 2016