TRPV6
Description
The TRPV6 (transient receptor potential cation channel subfamily V member 6) is a protein-coding gene located on chromosome 7.
TRPV6 is a membrane calcium (Ca2+) channel protein which is particularly involved in the first step in Ca2+absorption in the intestine. Transient Receptor Potential Vanilloid subfamily member 6 (TRPV6) is an epithelial Ca2+ channel that belongs to the transient receptor potential family (TRP) of proteins. The TRP family is a group of channel proteins critical for ionic homeostasis and the perception of various physical and chemical stimuli. TRP channels can detect temperature, osmotic pressure, olfaction, taste, and mechanical forces. The human genome encodes for 28 TRP channels, which include six TRPV channels. The high Ca2+-selectivity of TRPV5 and TRPV6 makes these channels distinct from the other four TRPV channels (TRPV1-TRPV4). TRPV5 and TRPV6 are involved in Ca2+ transport, whereas TRPV1 through TRPV3 are heat sensors with different temperature threshold for activation, and TRPV4 is involved in sensing osmolarity. Genetic defects in TRPV6 gene are linked to transient neonatal hyperparathyroidism and early-onset chronic pancreatitis. Dysregulation of TRPV6 is also involved in hypercalciuria, kidney stone formation, bone disorders, defects in keratinocyte differentiation, skeletal deformities, osteoarthritis, male sterility, Pendred syndrome, and certain sub-types of Cancer. Peng et al identified TRPV6 in 1999 from rat duodenum in an effort to search for Ca2+ transporting proteins involved in Ca2+absorption.
TRPV6 is a calcium-selective ion channel that plays a crucial role in calcium uptake in various tissues, including the intestine. It is essential for maintaining normal calcium levels in the body, impacting bone and skin health. The channel is activated by low intracellular calcium levels, likely including depletion of intracellular calcium stores, and exhibits inward rectification. Inactivation occurs through both rapid calcium-dependent and slower calcium-calmodulin-dependent mechanisms, with the latter potentially regulated by phosphorylation. In vitro, it is slowly inhibited by magnesium in a voltage-independent manner. Heteromeric assembly with TRPV5 appears to alter channel properties, with TRPV5-TRPV6 heteromultimeric concatemers demonstrating voltage-dependent gating.
TRPV6 is also known as ABP/ZF, CAT1, CATL, ECAC2, HRPTTN, HSA277909, LP6728, ZFAB.
