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The authors now report that R1H mutation is sufficient to reconstitute resting-state H(+) 'shuttle' conductance in Hv1 without abrogating the intrinsic 'aqueous' H(+) conductance.
We suggest that cleavage and heterodimerization of Hv1 represents an adaptation to the specific requirements of pH control in sperm.
Inhibition of Hv1 channels by Zn(2+).
CREBBP (show CREBBP Proteins) mutations were associated with inferior progression-free survival (PFS), whereas mutations in previously unreported HVCN1, a voltage-gated proton channel-encoding gene and B-cell receptor signaling modulator, were associated with improved PFS.
Our data demonstrated that the expression of Hv1 in pancreatic islet beta-cells regulates insulin (show INS Proteins) secretion through regulating Ca(2 (show CA2 Proteins)+) homeostasis.
The main properties of the voltage-gated proton channel (HV1) are described in this review, along with what is known about how the channel protein structure accomplishes its functions. [review]
Hv1 activity displays hysteresis
A shorter isoform of HVCN1 with enhanced gating is specifically enriched in malignant B cells.
Divalent metal binding causes a conformational change in human the Hv1 c-terminal domain.
analysis of of the C-terminal domain of voltage-gated proton channel HV1 and the thermodynamic characteristics of Zn(2) binding to this domain
loss of Hv1 significantly attenuates STZ-induced beta-cell damage and ROS (show ROS1 Proteins) production in pancreatic beta-cells; results suggest that Hv1 might contribute to development of diabetes through producing ROS (show ROS1 Proteins).
Hv1 channels therefore differentially regulate the pHp (show FXYD6 Proteins) in neutrophils and macrophages, sustaining rapid acidification in macrophage phagosomes and maintaining a neutral pH in neutrophil phagosomes.
microglial Hv1 proton channel is a unique target for modulation of microglial M1/M2 polarization in the pathogenesis of ischemic stroke
Alkalinity of neutrophil phagocytic vacuoles is modulated by HVCN1.
The voltage-gated proton channel Hv1/VSOP inhibits neutrophil granule release
Eosinophils require proton channel HVCN1 for optimal reactive oxygen species generation and prevention of activation-induced cell death.
Functional expression of voltage-gated proton (Hv1) channels is characterized, for the first time, in mouse bone marrow-derived dendritic cells.
inhibition of Hv1 function via knockdown of Hv1 expression can effectively retard cancer growth
Hv1 channels maintain a physiological membrane potential during the respiratory burst of neutrophils by providing a compensating charge for the electrons transferred by NOX2 from NADPH to superoxide.
This gene encodes a voltage-gated protein channel protein expressed more highly in certain cells of the immune system. Phagocytic cells produce superoxide anions which require this channel protein, and in B cells this same process facilitates antibody production. This same channel protein, however, can also regulate functions in other cells including spermatozoa. Multiple transcript variants encoding different isoforms have been found for this gene.
, voltage-gated hydrogen channel 1
, hydrogen voltage-gated channel 1
, voltage sensor domain-only protein