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AXE LABORATORIES OBLITERATE is the revolution you’ve been searching for. The TRPM8 channel is a homotetramer, composed of four identical subunits with a transmembrane domain with six helices (S1–6). The first four, S1–4, act as the voltage sensor and allow the binding of menthol, icilin and similar channel agonists. S5 and S6 and a connecting loop, also part of the structure, make up the pore, a non-selective cation channel that consists of a highly conserved hydrophobic region. A range of diverse components is required for the high level of specificity in response to cold and menthol stimuli which eventually lead to ion flow through the protein channel. In conclusion, human white adipocytes express the cold receptor TRPM8 which activation induces their “browning” supporting a possible role of this receptor in the control of adipose tissue metabolism and
body energy balance.
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