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A review of the potential effect of electroacupuncture and moxibustion on cell repair and survival: the role of heat shock proteins by ProQuest

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In recent years, a considerable amount of research has been focused on the underlying mechanisms of electroacupuncture and moxibustion assisted tissue repair. Intracellular protein denaturation is a significant pathological step of acute conditions such as stroke, myocardial infarction and acute pancreatitis. Protein aggregation can be observed after the protein denaturation step in chronic diseases of the central nervous system like Alzheimer's and Parkinson's disease, and also in other chronic system diseases including cataract formation. Heat shock proteins (HSPs) are fundamental for intracellular protein repair and work by preventing protein aggregation and assisting denaturated proteins to refold. Further, HSPs can also function for extracellular cell signalling. The focus of this review is to analyse the data studying electroacupuncture and moxibustion induced HSPs, and how acupuncture can survive cells from apoptosis under stress.

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                                                                                                        folding and the maturation of large
A review of the potential effect of                                                                     proteins such as cellular receptors in the
                                                                                                        cell (see figure 2).23 Further, it is worth
electroacupuncture and moxibustion on cell                                                              noting that the HSP70 and HSP100
                                                                                                        bichaperone system is able to disentangle
repair and survival: the role of heat shock                                                             polypeptides from aggregates which, in
                                                                                                        turn, results in the disaggregation pro-
proteins                                                                                                cess.24 See figure 1.

Yusuf Ozgur Cakmak                                                                                      Acupuncture and heat shock proteins
                                                                                                        The first study on HSP and acupuncture
In recent years, a considerable amount of research has been focused on the underlying                   related techniques was published in 1995.
                                                                                                        It has been shown that levels of HSP70,
mechanisms of electroacupuncture and moxibustion assisted tissue repair. Intracellular protein
denaturation is a significant pathological step of acute conditions such as stroke, myocardial          HSP85 and HSP100 are increased by
infarction and acute pancreatitis. Protein aggregation can be observed after the protein                moxibustion, in which heat is applied to
                                                                                                        acupuncture points directly or through
denaturation step in chronic diseases of the central nervous system like Alzheimer’s and
Parkinson’s disease, and also in other chronic system diseases including cataract formation. Heat       needles via burning of artemisia vulgaris
shock proteins (HSPs) are fundamental for intracellular protein repair and work by preventing           (mugwort).25 It is not surprising that heat
protein aggregation and assisting denaturated proteins to refold. Further, HSPs can also function for   assisted acupuncture techniques triggers
extracellular cell signalling. The focus of this review is to analyse the data studying                 an increase of HSP levels. However, it is
electroacupuncture and moxibustion induced HSPs, and how acupuncture can survive cells from             worth noting that HSPs act on moxibus-
apoptosis under stress.                                                                                 tion rather than the smoke of mugwort.26
                                                                                                           The first evidence of the relationship
                                                                                                        between HSPs and EA was demonstrated
Heat shock proteins (HSPs), also called             help of HSPs. These active folded proteins          by Zamotrinsky et al in 1997.27
stress proteins, are a group of proteins            can be misfolded when the cell experience           Zamotrinsky et al applied 3Hz auricular
present in all cells in all life forms.             stressful conditions. In such a case, the           EA daily for 10 days to patients with
Although HSPs are named after an inves-             most significant action of HSPs occurs.             coronary artery disease. After the seventh
tigation studying heat exposure in droso-           HSPs stabilise and repair misfolded pro-            and eighth EA no ECG signs of myocardial
philia (fruitfly), they are produced in any         teins and thereby help to protect the cell          ischaemia are observed. The patients
kind of stress when a cell undergoes                against irreversible damage, apoptosis and          could tolerate a bicycle exercise test and
various types of environmental stresses             death. HSPs (especially HSP70 and                   they also could climb 5–7 flights of stairs
such as heat, heavy metal,1 UV-B,2 etha-            HSP60) repair misfolded proteins by                 without requiring sublingual glyceryl tri-
nol,3 oxygen deprivation.4 Experiments              refolding them back to their original size.         nitrate or developing angina. Three days
with bacteria,5 yeast,6 fruitflies,7 plants,8       If these processes are ineffective, proteins        after the final EA session, HSP70
fruits,9 mice10 and humans have shown               are targeted for degradation in the ubiqui-         amounts, whose presence is specific for
that increased production of HSPs can               tin-proteasome pathway. Further, these              ischaemic heart pathology, were not
protect an organism against stress-induced          misfolded or unfolded proteins tend to              detectable in samples of the EA group.27
damage. It is worth noting that even noise          accumulate. If they accumulate they                 This was the first, indirect evidence of
can be a stress factor for cochlear cells and       trigger apoptosis and cell death. Even if           HSP levels increasing with EA and EA
triggers HSP production,11 12 which inhibits        an accumulation occurs, HSPs (HSP100-               assisted tissue repair via HSPs.
the cochlear hair cell death.13–15 The aim of       HSP70) can still help cell survival by                 In 2001, Lin YH et al28 applied local
this review is to clarify the relationship of       stimulating disaggregation. HSPs are                somatothermal stimulation by using
HSPs and mechanisms underlying the                  mandatory molecules for the cells to shift          heated rods on the intersection point of
electroacupuncture (EA) and moxibustion             the apoptosis pathway to the survival               the midclavicular line and right seventh
assisted regeneration.                              pathway. See figure 1.                              intercostal space at the liver ischaemia-
                                                       There are many different subgroups of            reperfusion model of rats. Although the
Protein folding                                     heat shock proteins—each one of them                point at which the heated rod was applied
When harmful substances denature pro-               performs a variety of functions that help           fits with acupuncture point of GB24,
teins and cause them to unfold, the                 the cell in both stressful and non-stressful        according to World Health Organization
proteins lose their original configuration          conditions. HSP40 presents unfolded                 description,29 it has not been indicated in
and are no longer able to function                  (nonfunctional) 
								
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