What’s cellular protein got to do with it? A whole lot! Turns out, you can influence it with food. In order to drum up more money for research and drugs, researchers also kind of have to admit the power of food.
Below, I’d like to show two recent, similar but unrelated studies about how cells deal with protein production and disease. One of them demonstrates a type of protective protein and how nutrients from superfoods influence it to keep watch over cells.
With all of this information one can see some patterns: a tipping point that leads to disease manifestation, either a clogging of or lack of protein at the cellular level, and how nutrient dense foods play a role in rebalancing the cell.
From Study Number #1
Cells put off protein production during times of [cellular] stress – High error rate on production line triggers slowdown
Living cells are like miniature factories, responsible for the production of more than 25,000 different proteins with very specific 3-D shapes. And just as an overwhelmed assembly line can begin making mistakes, a stressed cell can end up producing misshapen proteins that are unfolded or misfolded.
Now Duke University researchers in North Carolina and Singapore have shown that the cell recognizes the buildup of these misfolded proteins and responds by reshuffling its workload, much like a stressed out employee might temporarily move papers from an overflowing inbox into a junk drawer.
The study, which appears Sept. 11, 2014 in Cell, could lend insight into diseases that result from misfolded proteins piling up, such as Alzheimer’s disease, ALS, Huntington’s disease, Parkinson’s disease, and type 2 diabetes.
Christopher V. Nicchitta, Ph.D said:
We have identified an entirely new mechanism for how the cell responds to stress. Essentially, the cell remodels the organization of its protein production machinery in order to compartmentalize the tasks at hand.
The general architecture and workflow of these cellular factories has been understood for decades. First, DNA’s master blueprint, which is locked tightly in the nucleus of each cell, is transcribed into messenger RNA (mRNA). Then this working copy travels to the ribosomes standing on the surface of a larger accordion-shaped structure called the endoplasmic reticulum (ER). The ribosomes on the ER are tiny assembly lines that translate the mRNAs into proteins.
When a cell gets stressed, either by overheating or starvation, its proteins no longer fold properly. These unfolded proteins can set off an alarm — called the unfolded protein response or UPR – to slow down the assembly line and clean up the improperly folded products. Nicchitta wondered if the stress response might also employ other tactics to deal with the problem.
The researchers found that when the cells were stressed, they quickly moved mRNAs from the endoplasmic reticulum to the cytosol. Once the stress was resolved, the mRNAs went back to their spots on the production floor of the endoplasmic reticulum.
You can slow down protein production, but sometimes slowing down the workflow is not enough. You can activate genes to help chew up the misfolded proteins, but sometimes they are accumulating too quickly. Here we have discovered a mechanism that does one better — it effectively puts everything on hold. Once things get back to normal, the mRNAs are released from the holding pattern.
From Study #2
New superfoods could help key protein keep bodies healthy
A new generation of new superfoods that tackle heart disease and diabetes could be developed following research into a protein that helps keep cells in our bodies healthy.
Researchers at the University of Warwick (UK) found that the protein, called Nrf2, continually moves in and out of the nuclei of human cells to sense the cell’s health and vitality.
When Nrf2 is exposed to threats to the cell’s health it oscillates faster and activates an increase in the cell’s defence mechanism, including raising the levels of antioxidant.
The researchers, from the University’s Warwick Medical School, successfully increased the speed of Nrf2′s movement by artificially introducing health beneficial substances – potential components of new superfoods.
The beneficial substances comprise broccoli-derived sulforaphane and quercetin, which is found in high-levels in onions. [helpful for immunity and fighting allergies]
Published by Antioxidants and Redox Signalling, the research investigated the ways in which compounds in fruit and vegetables keep humans healthy.
The research team are the first to record the continual movement cycle of Nrf2, which sees the protein oscillate in and out of the cell nucleus once every 129 minutes. When stimulated by a health beneficial vegetable-derived substance Nrf2′s cycle sped up to 80 minutes.
Professor Paul Thornalley said:
The health benefit of Nrf2 oscillating at a fast speed is that surveillance of cell health is increased when most needed, that is, when cells are under threat. By understanding how this process works and increasing Nrf2′s speed without putting cells under threat, new strategies for design of healthier foods and improved drugs can be devised. Current designs may have selected substances with suboptimal if not poor health benefits in some cases.
The researchers in study number one wanted more answers and appeared to be interested in ways to artificially manipulate the cell for future use in medicine. The second study’s researchers, while supporting the role of nutrient dense foods, wanted to develop nutraceuticals, drugs and newer, engineered foods.
Dr. Terry Wahls used studies, and scaled the doses of superfoods given to mice to a human of her weight and size in order to reverse her MS. I’m hoping that by having this information one can see not only the magnificence of cells vs. disease, but that the body is actually equipped to heal with the right tools – before succumbing to and becoming dependent to the intended methods presented by the researchers.