Stress, whatever its cause - nutritional, biochemical, bacteriological, viral, thermal, psychological or environmental - constantly assaults our cells and threatens our equilibrium. To enable the survival of cells subjected to a state of shock, our organism has developed a mechanism of protection against the various stresses, by expressing proteins known as "heat shock proteins" or "HSPs".
HSPs are proteins whose role is to repair proteins damaged by cellular stress, thus allowing them to function properly.
PHYSIOMANCE HSP COMPLEX is ideal for nutritional support in situations of cellular stress, cellular aggression and shock.
PHYSIOMANCE HSP COMPLEX provides for 3 tablets:
- 200.0 mg of ETASTM asparagus stem extract, inducing the synthesis of HSPs;
- 200.0 mg of HMB*, one of the metabolites of leucine which themselves modulate the synthesis of HSPs;
- 15 mg of zinc, in the form of bisglycinate, inducing the expression of HSPs 70.
*HMB : calcium beta-hydroxy-beta-methylbutyrate
Why choose PHYSIOMANCE HSP COMPLEX from Laboratoire THERASCIENCE?
- For its formula combining 2 bio-actives (ETASTM and HMB) and a trace element (zinc) with synergistic actions on the induction of HSPs;
- For its ETASTM asparagus extract, a registered active ingredient, benefiting from numerous clinical studies on the induction of HSPs.
ETAS™ is a registred trademark of Amino Up Co., Ltd., JAPAN
Did you know it ?
Scientific discoveries are sometimes made by chance. In 1962, during an experiment on Drosophila larvae (small flies), the incorrect setting of an incubator at a high temperature induced the expression of proteins that had never been observed before and that ensured the survival of these larvae. Because of their expression after exposure to heat, these proteins were then named "Heat Shock Proteins" (HSP). Other experiments then demonstrated the induction of these proteins by different types of stress (exposure to heavy metals, UV, oxidative stress, etc.). The understanding of the expression of HSPs following stimulation by different stresses (biological, chemical, physical, psychological, etc.) gave rise to the concept of "stress proteins" that can be activated during cellular stress. HSPs are so-called "chaperone" proteins, i.e. they intervene in the folding of damaged proteins following exposure to these different stresses and take charge of their reconfiguration to ensure the continuity of biological functions. If, however, repair of these proteins proves impossible, HSPs transport them to degradation systems in order to avoid the accumulation of non-functional proteins likely to aggregate and completely disrupt the proper functioning of cells.