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Biological 'Fountain Of Youth' Found In New World Bat Caves

On Thu, 02 Jul 2009 00:30:02 GMT, "Dave Saum" <...@infiltec.com
http://www.sciencedaily.com/releases/2009/06/090630101229.htm
Science News
Biological 'Fountain Of Youth' Found In New World Bat Caves
ScienceDaily (July 1, 2009) Scientists from Texas are batty over a new
discovery which could lead to the single most important medical breakthrough
in human historysignificantly longer lifespans. The discovery, featured on
the cover of the July 2009 print issue of The FASEB Journal, shows that
proper protein folding over time in long-lived bats explains why they live
significantly longer than other mammals of comparable size, such as mice.

"Ultimately we are trying to discover what underlying mechanisms allow for
some animal species to live a very long time with the hope that we might be
able to develop therapies that allow people to age more slowly," said Asish
Chaudhuri, Professor of Biochemistry, VA Medical Center, San Antonio, Texas
and the senior researcher involved in the work.

Asish and colleagues made their discovery by extracting proteins from the
livers of two long-lived bat species (Tadarida brasiliensis and Myotis
velifer) and young adult mice and exposed them to chemicals known to cause
protein misfolding. After examining the proteins, the scientists found that
the bat proteins exhibited less damage than those of the mice, indicating
that bats have a mechanism for maintaining proper structure under extreme
stress.

"Maybe Juan Ponce De Len wasn't too far off the mark when he searched
Florida for the Fountain of Youth," said Gerald Weissmann, M.D.,
Editor-in-Chief of The FASEB Journal. "As it turns out, one of these bat
species lives out its long life in Florida. Since bats are rodents with
wings, this chemical clue as to why bats beat out mice in the aging game
should point scientists to the source of this elusive fountain."

--------------------------------------------------------------------------------

Journal reference:

1.. Salmon et al. The long lifespan of two bat species is correlated with
resistance to protein oxidation and enhanced protein homeostasis. The FASEB
Journal, 2009; 23 (7): 2317 DOI: 10.1096/fj.08-122523
Adapted from materials provided by Federation of American Societies for
Experimental Biology, via EurekAlert!, a service of AAAS.



On Wed, 1 Jul 2009 18:21:50 -0700 (PDT), Taka <...@gmail.com
The long lifespan of two bat species is correlated with resistance to
protein oxidation and enhanced protein homeostasis

Altered structure, and hence function, of cellular macromolecules
caused by oxidation can contribute to loss of physiological function
with age. Here, we tested whether the lifespan of bats, which
generally live far longer than predicted by their size, could be
explained by reduced protein damage relative to short-lived mice. We
show significantly lower protein oxidation (carbonylation) in Mexican
free-tailed bats (Tadarida brasiliensis) relative to mice, and a trend
for lower oxidation in samples from cave myotis bats (Myotis velifer)
relative to mice. Both species of bat show in vivo and in vitro
resistance to protein oxidation under conditions of acute oxidative
stress. These bat species also show low levels of protein
ubiquitination in total protein lysates along with reduced proteasome
activity, suggesting diminished protein damage and removal in bats.
Lastly, we show that bat-derived protein fractions are resistant to
urea-induced protein unfolding relative to the level of unfolding
detected in fractions from mice. Together, these data suggest that
long lifespan in some bat species might be regulated by very efficient
maintenance of protein homeostasis.

-----------------------

"protein oxidation (carbonylation)" ... by oxidized PUFAs. And the
targets are cysteines so I bet these proteins are low in them. Also
the bat's proteins should withstand wider temperature fluctuations
because they are naked (no body hair) so this makes them less prone to
denaturation by urea.

Taka

On Wed, 1 Jul 2009 18:42:49 -0700 (PDT), Eighthman <...@yahoo.com
Isn't this yet another reason to carefully examine and try to
duplicate Oden's famous (or infamous) study? Given that DNA/RNA may
control/regulate or strongly influence protein synthesis, could the
Oden results be real?

On Thu, 2 Jul 2009 15:44:22 -0700 (PDT), Paul Antonik Wakfer <...@morelife.org
On Jul 1, 8:30 pm, "Dave Saum" <...@infiltec.com
After reading the full paper http://pmid.us/19244163, I was amazed and
disappointed by the above rather silly remark from no less than the
Editor-in-Chief of the journal. Perhaps it merely shows once again
that MD's are not scientists.

The study was a comparison of protein homeostasis between two Florida
bat species with maximum lifespans of at least 12 yrs and wild mice in
captivity with maximum lifespans of 4 years. Note that maximum
lifespans of bats in the wild are only known from limited recaptures
and are almost certainly longer than the oldest recordings, and
furthermore are lifespans of only those bats with the full
functionality required for continued existence in the wild rather than
in protected lab environments. Also note that the numbers of animals
of each species assayed were very small (3-5).

The results found are briefly as follows:

1) Oxidatively damaged proteins (measured by both soluble and
insoluble carbonyl levels) were much lower in one bat specie (~40%)
and slightly lower in the other compared with mouse,
2) Protein carbonyl levels following oxidative stress in vivo (gamma
radiation) were much lower (~50% and 40%) in bat species than mouse.
3) Protein carbonyl levels following oxidative stress in vitro (iron
ascorbate) were much lower relative to their starting values in bats
than mouse.
4) Proteins marked for disposal by ubiquitination were drastically
lower (~20% and 30%) in bats compared with mouse.
5) Proteosome (the recycler of ubiquitinated proteins) activity was
drastically reduced in bats compared with mouse, even though the
proteosome content was similar.
6) Both in vitro and invivo, both in situ and fully separated from
their cells, bat proteins were more resistant to an unfolding stressor
(urea) than were mouse proteins.

After the hype of the headlines, I found these results to be highly
disappointing because of having no practical near-term value to me.
For an already healthy person, antioxidant supplementation has been
shown to have limited benefit toward reducing protein damage. A human
individual can do nothing about the genetic makeup of hir proteins.
Perhaps there are some methods to upregulate protein protection
mechanisms. However, in my view the most practical approach is
actually to continue doing what the bats did *not* show, which is to
increase ubiquitination and proteosomal recycling of proteins by a
combination of mild calorie restriction, intermittent fasting and
ingestion of certain autophagy enhancing chemicals.

--Paul Wakfer

MoreLife for the rational - http://morelife.org
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