BioAcyl Corp
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Yan, L., Liu, J. J., & Hong, L. (2025). Hv1 channel in immune cells and pharmacology. Pharmacological Research, 219, 107885. Added by: Dr. Enrique Feoli (11/03/2026, 18:40) Last edited by: Dr. Enrique Feoli (11/03/2026, 18:47) |
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| Resource type: Journal Article DOI: 10.1016/j.phrs.2025.107885 ID no. (ISBN etc.): 1043-6618 BibTeX citation key: Yan2025 View all bibliographic details  |
Categories: BioAcyl Corp Subcategories: Extracellular acidity Keywords: Hv1, Immune cells, Immune disorder, inflammation, Ion channel, Pharmacology Creators: Hong, Liu, Yan Collection: Pharmacological Research |
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| Abstract |
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The voltage-gated proton channel Hv1 is a key regulator of immune cell function, crucial for maintaining pH homeostasis, supporting reactive oxygen species (ROS) production, and modulating both innate and adaptive immune responses. By facilitating proton extrusion in response to membrane depolarization, Hv1 helps counteract intracellular acidification during immune cell activation and respiratory burst. Hv1 is highly expressed in diverse immune populations such as neutrophils, monocytes, eosinophils, and B cells, where it plays important roles in microbial defense, inflammatory signaling, antigen presentation, and cellular activation. Emerging evidence shows that dysregulation of Hv1 expression or function alters immune homeostasis and contributes to the pathogenesis of autoimmune diseases, chronic inflammation, and cancers. Given its immunoregulatory functions and disease associations, Hv1 represents a promising therapeutic target for the development of novel treatments for immune and inflammatory diseases.
Added by: Dr. Enrique Feoli Last edited by: Dr. Enrique Feoli |
| Notes |
 Topological organization of the voltage-gated proton channel Hv1. The Hv1 is made of four membrane-spanning segments (S1 through S4). In the S4 segment, there are three positive arginines (R205, R208, and R211 in human Hv1) responsible for the S4 movement to regulate the opening of the Hv1 proton channel. Hv1 forms dimers in which two Hv1 subunits are held together by the C-terminal coiled-coil domain of each subunit. The proton permeation pathway is located in each subunit.
Added by: Dr. Enrique Feoli Last edited by: Dr. Enrique Feoli |