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A voltage-gated proton channel (Hv1) is the main pathway for H(+) efflux that allows capacitation in sperm and permits sustained reactive oxygen species production in white blood cells. A designed peptide inhibitor C6 was identified by a phage-display strategy whereby approximately 1 million novel peptides were fabricated on an inhibitor cysteine knot scaffold and sorted on purified Hv1 protein.
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 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.
Trp207 is crucial for slow channel opening, highly temperature-dependent gating kinetics, proton selectivity, and DeltapH-dependent gating.
Our data demonstrated that the expression of Hv1 in pancreatic islet beta-cells regulates insulin secretion through regulating Ca(2+) 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
Salt bridge networks and the hydrophobic plug function as the gate in Hv1 channels; outward movement of the fourth transmembrane segment leads to the opening of this gate.
Results suggest that Hv1 may be used as a potential biomarker for diagnosis and prognosis of colorectal carcinoma, and a potential target for anticancer drugs in colorectal cancer therapy.
inhibition of Hv1 activity via Zn(2+) ions can effectively retard the cancer growth and suppress the cancer metastasis by the decrease of proton extrusion and the down-regulation of gelatinase activity
In the Hv1 voltage-gated channel a highly conserved phenylalanine is found in the charge transfer center.
Two conformational changes are detected in Hv1 channels that are involved in channel opening.
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.
Hv1-dependent reactive oxygen species production is responsible for a substantial fraction of brain damage at early time points after ischemic stroke.
The increase in ROS production in VSOP/Hv1-deficient cells was not observed in macrophages, which suggests microglia have a unique mechanism of VSOP/Hv1-dependent ROS regulation.
This work therefore demonstrates that fully differentiated mammalian muscle fibers do not express functional voltage-gated H(+) channels and consequently can no longer be considered as the only vertebrate excitable cells exhibiting voltage-gated H(+) currents.
loss of Hv1 significantly attenuates STZ-induced beta-cell damage and ROS production in pancreatic beta-cells; results suggest that Hv1 might contribute to development of diabetes through producing ROS.
Hv1 channels therefore differentially regulate the pHp 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.
Data suggest that the biochemical properties of the cytoplasmic coiled-coil domain in the Hv channel depend on the redox condition, which may play a role in redox sensing in the phagosome.
Functional expression of voltage-gated proton (Hv1) channels is characterized, for the first time, in mouse bone marrow-derived dendritic cells.
Review of structural organization and gating of Hv1 channels discusses relationship between gating of Hvcn1 and the gating of ion-conducting pores recently discovered in the voltage-sensing domains of mutant voltage-gated potassium and sodium channels.
HVCN1 -deficieent B cells show a defct in ROS production, which causes less signal transduction through impaired BCR-dependent oxidation of SHP-1.
Hv1 channels truncated just downstream of R2 in the S4 segment retain most channel properties.
VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification.
reported that VSOP, a four-transmembrane protein similar to the voltage-sensor domain of voltage-gated ion channels is a voltage-gated proton channel [VSOP]
VSOP/Hv1 is present in phagosome and plays role in production of reactive oxygen species.
Hv1 expression is required for measurable voltage-gated H(+) current in unstimulated phagocytes.
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