External Bioenergy Increases Intracellular Free Calcium Concentration and Reduces Cellular Response to Heat Stress

Background External bioenergy (energy emitted from the body) can influence a variety of biological activities. It has been shown to enhance immunity, promote normal cell proliferation, increase tumor cell death, and accelerate bone fracture recovery. In this study, we investigated whether external bioenergy could alter intracellular calcium concentration ([Ca2+]i, an important factor in signal transduction) and regulate the cellular response to heat stress in cultured human lymphoid Jurkat T cells. Methods A practitioner emitted bioenergy toward tubes of cultured Jurkat cells for one 15-minute period. [Ca2+]i was measured spectrofluorometrically using the fluorescent probe indo-1. The heat shock protein 72 kd was detected using35 S-methionine prepulse and Western blot analysis. Results The resting [Ca2+]i in Jurkat T cells was 90±3 nM in the presence of external calcium. The removal of external calcium decreased the resting [Ca2+]i to 54±2 nM, indicating that Ca2+ entry from the external source is important for maintaining the basal level of [Ca2+]i. In the presence of external Ca2+, treatment of Jurkat T cells with external bioenergy for 15 minutes increased [Ca2+]i by 22±3%. [Ca2+]i remained elevated in these cells for 2 hours. Surprisingly, we also observed that [Ca2+]i increased by 11±1% if cells were simply placed in the area where external bioenergy had been used. This lingering effect of external bioenergy dissipated within 24 hours. Treatment with external bioenergy reduced cellular responses to heat stress and did not induce the production of heat shock protein 72 kd, which is known to provide cytoprotection. Conclusions These results suggest that externally applied bioenergy can upregulate [Ca2+]i and downregulate the cellular response to stress. The association between the external bioenergy and increases in [Ca2+]i may be a good index for detecting presence of bioenergy.

[1]  J. Kiang,et al.  HSP-72 synthesis is promoted by increase in [Ca2+]i or activation of G proteins but not pHi or cAMP. , 1994, The American journal of physiology.

[2]  J. Kiang,et al.  Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. , 1998, Pharmacology & therapeutics.

[3]  X. Ding,et al.  Thermotolerance attenuates heat-induced increases in [Ca2+]i and HSP-72 synthesis but not heat-induced intracellular acidification in human A-431 cells. , 1996, Journal of investigative medicine : the official publication of the American Federation for Clinical Research.

[4]  J. Kiang,et al.  Biochemical requirements for the expression of heat shock protein 72 kDa in human breast cancer MCF-7 cells , 1999, Molecular and Cellular Biochemistry.

[5]  J. Meldolesi,et al.  Pathways of Ca2+ influx at the plasma membrane: voltage-, receptor-, and second messenger-operated channels. , 1987, Experimental cell research.

[6]  J. Kiang,et al.  Regulation of heat shock protein 72 kDa and 90 kDa in human breast cancer MDA-MB-231 cells , 2004, Molecular and Cellular Biochemistry.

[7]  Hui Lin,et al.  Structure and property changes in certain materials influenced by the external qi of qigong , 1999 .

[8]  J. Kiang,et al.  Effect of heat shock, [Ca2+]i, and cAMP on inositol trisphosphate in human epidermoid A-431 cells. , 1993, The American journal of physiology.

[9]  W. Cao,et al.  Protective effect of XY99-5038 on hydrogen peroxide induced cell death in cultured retinal neurons. , 2001, Life sciences.

[10]  J. Kiang,et al.  Cytoprotection and regulation of heat shock proteins induced by heat shock in human breast cancer T47‐D cells: role of [Ca2+]i and protein kinases , 1998, The FASEB Journal.

[11]  X. Ding,et al.  Overexpression of HSP-70 attenuates increases in [Ca2+]i and protects human epidermoid A-431 cells after chemical hypoxia. , 1998, Toxicology and applied pharmacology.

[12]  Michael J. Berridge,et al.  Inositol phosphates and cell signalling , 1989, Nature.