Heat Shock Proteins
[FASEBJ/Heat Shock Protein Overexpression
via Hsp22 extends Drosophila life span 30%..,
Books/heat shock proteins,
LibCong,
Links/aging and heat shock proteins,
Images,
Papers,
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LifeExtension,
Wikipedia;
Index/HSP90],
[24s].
According to the
Geron
European Patent
(A' alternate-source version
Compositions and Methods for
Increasing Telomerase Activity,
or A''),
heat
shock proteins mediate the assembly of telomerase and
can be
used to increase telomerase levels in the cell.
(White). Many heat shock proteins, such as
HSP60,
HSP70, and
HSP90,
are chaparonins mediating
protein folding.
Astragalosides seem to be treated like
nuclear superfamily
transcription factors complexed with the 90 kDa
heat shock protein Hsp90
[Wikipedia,
Links,
Images,
Papers,
Books,
Amazon]
before tranfer into the nucleus of the cell.
(Perhaps astragalosides are all stripped down to cycloastragenol, the common
alglycone
of the astragalosides,
prior to transport into the nucleus.)
It may accelerate matters to
improve Hsp90 expression
by some means, perhaps by raising
Interleukin 6 levels via exercise.
We might pump up just before taking our
astragalus root extract with
Chitosan to facilite its march into the
nucleus complexed with Hsp90
elevated by the exercise session.
HSP90 maintains
cellular steroid receptors
and transcription factors vital for
protein synthesis.
[See Iron Man,
Sept.2009, for the Jerry Brainum article on
heat shock proteins, summarized and expanded below.] "HSP90 is necessary for telomerase activity,
as is p23."
(Cong, Wright, and Shay, 2002).
Heat shock proteins (stress proteins)
maintain proper
protein folding and
transport
proteins across cellular membranes.
HSPs
were discovered in 1962, when DNP
(dinitrophenol)
was used to increase body heat in fruit flies.
HSPs
help maintain protein shapes degraded by stress,
including stress from infections, inflammation, toxins like alcohol,
trace metals like cadmium or lead, and from UV light.
Starvation, too little oxygen, dehydration and exercise all
induce HSP release.
We will consider HSP20,
HSP22,
HSP25,
HSP60,
HSP70,
HSP72, and
HSP90.
Ubiquitin,
which helps degrade certain muscle-associated proteins, acts like a small HSP.
HSPs
may signal immune cells.
HSPs may
monitor
cell proteins, taking them to a place in the cell to make way for newly synthesized proteins.
HSP20
prevents aggregation of platelets,
clotting,
the immediate cause of heart attacks and
strokes, and
protects
against ischemia and reperfusion injuries.
HSPs are involved in
anticatabolic
insulin metabolism.
ROS (Reactive Oxygen Species)
stimulate HSP release, so HSPs
are released better during exercise in the absence of
antioxidants which counteract
ROS.
Antioxidants
should be taken well after exercise if HSPs are to be abundantly available from a workout.
HSPs boost glutathione,
a major endogenous antioxidant.
HSPs such as
HSP70
blunt the release and activity of TNF-α, a major agent of
muscle catabolism.
The presence of TNF-α
stimulates HSP70 release.
HSP70 also inhibits NFκB,
an inflammatory mediator
partially responsible for
muscle atrophy. In addition,
HSP70 prevents foxo3 transcription.
HSPs and NO interact, dialating
bronchial tubes, dimenishing exercise-induced asthma.
High intensity resistance exercises seem to be required
to much boost HSP production
from exercise.
Note that HSP60 is released during
contractions not causing much muscle injury, and is
concentrated in mitochondria,
helping to protect them.
HSP60
also helps to maintain IGF-1 cell receptors, which has
anti-aging benefits.
HSP70 is produced during high-intensity contractions
and helps damaged muscle proteins function again via refolding.
Higher levels of
HSP70 give better
cardiovascular protection.
HSP72 is boosted by
anabolic steroids
such as Deca-Durabolin,
allowing more high-intensity training.
HSP release
is also stimulated by testosterone and
catecholamines
(stress hormones)
including epinephrine and
norepinephrine,
which can be released by taking caffeine.
Caffeine boosts HSP72 production
during workouts. Perhaps the most effective HSP blocker during exercise is gamma tocopherol
(abundant in peanuts), and so perhaps
gamma tocopherol should be taken
well after workouts if HSP production is to be emphasized.
Another activator of HSPs
in muscle cells is lipoic acid, and a combination of
carnosine
and zinc can also activate HSPs.
Unfortunately,overexpression of certain HSPs
can
initiate cancer [Index/Cancer] in some cells by
deactivating
p53, a tumor-suppressing protein.
From an anti-aging point of view, I believe I prefer to keep antioxidant
protection high at all times, and rely on HGH,
IGF-1, and
NO from exercise more than on heat shock proteins
from exercise for anti-aging benefits.
On the other hand, lipoic acid and a combination of
carnosine and
zinc
to activate HSPs looks attractive.
Otherwise, regarding
Hsp22,
[Hytest/Human
Heat Shock Protein Hsp22, Hsp22 extends the life span of Drosophila 30%.
(Ben Best, also
FASEB Journal,
Genevive Morrow, Milanie Samson, et.al.)
Also see
elevating
Hsp22 with Trichostatin A,
[Books/heat shock proteins,
Links,
Wikipedia,
LibCong/Heat
Shock Proteins,
LifeExtension]
[24s].
Resveratrol activates SIRT1,
which stress-inducibly regulates
Heat Shock Factor
(HSF1,
HSF2, and
HSF4),
a transcription factor
regulating the expression of Heat Shock Proteins.
In fact, Heat Shock Factor 1 (HSF1)
regulates life span.
Tex OE
[Links,
Papers,
Books],
an extract
of the skin of prickly pear cactus fruit, is taken
2 hours prior to stress exposure such as bodybuilding exercise to raise levels of
HSP70 and
HSP27, and can increase
HSPs by 200%. HSP70 blocks muscle atrophy.
TEX OE is also used for hangovers.
Supplements [Links/HSP supplements,
Links/HSP activators]
include HSPactive.
