EDITORIAL

Healthy Brains and Healthy Bodies

The proteins upon which life depends share an attribute with
paper airplanes: Unless folded properly, they just won’t fly.

— From “Life’s Secrets Are Locked Away in
Folded Proteins,” R&D, June 12, 2008

ne thing is certain: the future will be much faster than the present. The recently announced USB 3.0 standard—supported by computer industry leaders such as Intel and Microsoft—portends impressive data transfer features, such as a staggering rated speed of 4.8 Gbit/s. (Where will competitors such as Firewire come in?) Additionally, USB 3.0 offers room for smart power control that can effectively lower your electricity draw. More for less. But the real question is: Will you be able to keep up?

The answer depends on whether you’re up and running efficiently in the 2010s, with a healthy brain in a healthy body. It is for this reason that Life Enhancement exists. We are committed to help you be as robust and vigorous as possible. And this is why we continue to push the envelope.

A Great Leap Forward in Health

In this issue, we are introducing what must be thought of as “a great leap forward”: the first practical answer to an acknowledged—but hitherto unaddressed—aspect of the aging process. For decades, scientists have lamented the decline in functionality associated with the failure of our proteins to refold themselves properly when they become misfolded. By losing this ability to restore their correct shape, these molecules stop serving life’s functions, contributing instead to dysfunction and degradation. Addressing this problem, for the first time with a proposed solution, life extension scientists Durk Pearson and Sandy Shaw call their approach “The Origami of Aging: How Small Molecules Help Maintain Proper Protein Folding for Better Health and Longevity.” (See their article on page 4.)

Improperly folded proteins tend to aggregate and are associated with a variety of age-related diseases, such as Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis, and, quite probably, other neurodegenerative conditions. Moreover, improperly folded proteins are also associated with cancer, emphysema, cystic fibrosis, liver disease, and mad cow disease (and other prion diseases). They are even associated with chronic pain and cataracts.

Folding Correctly Is a Key Step for Cellular Health



Dr. Judith Frydman
Judith Frydman, an associate professor of biology at Stanford University and one of two senior authors of a paper published recently in Nature Structural and Molecular Biology,1 has said that “Folding is one of the key steps for the health of the cell.” If they are not properly folded, as virtually all proteins require—often with the help of a type of molecule called a chaperone or chaperonin—they will not function properly. According to Frydman, “Many of the proteins that have these complex folds are the most important ones for life. . . . The proteins that control the cell cycle, tumor suppressors, and the proteins that control the shape of the cell are dependent on chaperonins to get to the folded state. . . . If the chaperones don’t work well, then all these proteins that have been made become toxic.”

The Protein Good News

Fortunately, the study of protein misfolding and aggregation is heating up, and a growing body of scientific information now points to a group of nutrients called osmolytes, which can help refold misfolded proteins correctly. Osmolytes are found naturally and abundantly in living tissue and have been used safely in substantial amounts as supplements or as components of foods for long periods of time.

According to researchers working at the University of Massachusetts and the Max Planck Institute for Biochemistry in Germany, “. . . the osmolyte proline may be protective against biomedically important protein aggregates that are hallmarks of several late-onset neurodegenerative diseases, including Huntington’s, Alzheimer’s, and Parkinson’s. . . . We propose that proline is aggregation-protective because of its ability to suppress the earliest aberrant protein interactions that trigger pathogenic aggregation.”2

As Durk and Sandy said, upon deciding to start supplementing with proline and other osmoprotectants, “There’s no time to waste—proteins are aggregating right now under above our noses.”

References

  1. Booth CR, Meyer AS, Cong Y, Topf M, Sali A, Ludtke SJ, Chiu W, Frydman J. Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol 2008 Jul;15(7):746-53.
  2. Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci USA 2006;103(36): 13357-61.

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