TRPV1TRPV6

TRPV1TRPV6 is not a standard name for a single protein in current scientific literature. The term may be used informally to refer to either the TRPV1 and TRPV6 channels separately, or to a hypothetical fusion; there is no widely recognized channel by this name. This article therefore summarizes the two distinct members of the TRPV subfamily and their contrasting roles.

TRPV1, the capsaicin receptor, is a non-selective cation channel that forms tetramers. Each subunit has six transmembrane domains with a pore-forming region between the fifth and sixth segments. TRPV1 is activated by heat (threshold around 43 C), capsaicin, acidic pH, and various endogenous ligands. It conducts Ca2+ and Na+ and plays a central role in nociception and inflammatory pain. Channel activity is modulated by cellular lipids such as PIP2 and by phosphorylation; desensitization occurs with sustained stimulation. TRPV1 is a prominent target for analgesic research, with several agonists used experimentally to probe pain pathways and a range of antagonists studied for pain relief.

TRPV6 is a highly Ca2+-selective channel that forms tetramers and is less permeable to other cations. It shows limited voltage dependence and is regulated mainly by extracellular calcium levels and intracellular Ca2+-dependent feedback, including calmodulin. TRPV6 is important for transcellular calcium absorption in the intestine and for renal calcium handling. Its expression is induced by vitamin D and varies across tissues; it has been studied in the context of calcium homeostasis and, in some cancers, for its potential role in cell proliferation.

Because TRPV1TRPV6 is not a recognized single-channel entity, the article treats them as separate channels with distinct physiological and pharmacological profiles.