{"date_created":"2024-06-30T13:58:07Z","status":"public","doi":"10.1074/jbc.m109.018945","date_updated":"2024-06-30T13:58:15Z","page":"29024–29040","publication":"Journal of Biological Chemistry","_id":"54944","citation":{"bibtex":"@article{Haerteis_Krueger_Korbmacher_Rauh_2009, title={The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation}, volume={284}, DOI={<a href=\"https://doi.org/10.1074/jbc.m109.018945\">10.1074/jbc.m109.018945</a>}, number={42}, journal={Journal of Biological Chemistry}, publisher={American Society for Biochemistry and Molecular Biology}, author={Haerteis, Silke and Krueger, Bettina and Korbmacher, Christoph and Rauh, Robert}, year={2009}, pages={29024–29040} }","mla":"Haerteis, Silke, et al. “The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation.” <i>Journal of Biological Chemistry</i>, vol. 284, no. 42, American Society for Biochemistry and Molecular Biology, 2009, pp. 29024–29040, doi:<a href=\"https://doi.org/10.1074/jbc.m109.018945\">10.1074/jbc.m109.018945</a>.","short":"S. Haerteis, B. Krueger, C. Korbmacher, R. Rauh, Journal of Biological Chemistry 284 (2009) 29024–29040.","ama":"Haerteis S, Krueger B, Korbmacher C, Rauh R. The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation. <i>Journal of Biological Chemistry</i>. 2009;284(42):29024–29040. doi:<a href=\"https://doi.org/10.1074/jbc.m109.018945\">10.1074/jbc.m109.018945</a>","ieee":"S. Haerteis, B. Krueger, C. Korbmacher, and R. Rauh, “The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation,” <i>Journal of Biological Chemistry</i>, vol. 284, no. 42, pp. 29024–29040, 2009, doi: <a href=\"https://doi.org/10.1074/jbc.m109.018945\">10.1074/jbc.m109.018945</a>.","chicago":"Haerteis, Silke, Bettina Krueger, Christoph Korbmacher, and Robert Rauh. “The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation.” <i>Journal of Biological Chemistry</i> 284, no. 42 (2009): 29024–29040. <a href=\"https://doi.org/10.1074/jbc.m109.018945\">https://doi.org/10.1074/jbc.m109.018945</a>.","apa":"Haerteis, S., Krueger, B., Korbmacher, C., &#38; Rauh, R. (2009). The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation. <i>Journal of Biological Chemistry</i>, <i>284</i>(42), 29024–29040. <a href=\"https://doi.org/10.1074/jbc.m109.018945\">https://doi.org/10.1074/jbc.m109.018945</a>"},"intvolume":"       284","abstract":[{"lang":"eng","text":"The epithelial sodium channel (ENaC) is probably a heterotrimer with three well characterized subunits (alphabetagamma). In humans an additional delta-subunit (delta-hENaC) exists but little is known about its function. Using the Xenopus laevis oocyte expression system, we compared the functional properties of alphabetagamma- and deltabetagamma-hENaC and investigated whether deltabetagamma-hENaC can be proteolytically activated. The amiloride-sensitive ENaC whole-cell current (DeltaI(ami)) was about 11-fold larger in oocytes expressing deltabetagamma-hENaC than in oocytes expressing alphabetagamma-hENaC. The 2-fold larger single-channel Na(+) conductance of deltabetagamma-hENaC cannot explain this difference. Using a chemiluminescence assay, we demonstrated that an increased channel surface expression is also not the cause. Thus, overall channel activity of deltabetagamma-hENaC must be higher than that of alphabetagamma-hENaC. Experiments exploiting the properties of the known betaS520C mutant ENaC confirmed this conclusion. Moreover, chymotrypsin had a reduced stimulatory effect on deltabetagamma-hENaC whole-cell currents compared with its effect on alphabetagamma-hENaC whole-cell currents (2-fold versus 5-fold). This suggests that the cell surface pool of so-called near-silent channels that can be proteolytically activated is smaller for deltabetagamma-hENaC than for alphabetagamma-hENaC. Proteolytic activation of deltabetagamma-hENaC was associated with the appearance of a delta-hENaC cleavage product at the cell surface. Finally, we demonstrated that a short inhibitory 13-mer peptide corresponding to a region of the extracellular loop of human alpha-ENaC inhibited DeltaI(ami) in oocytes expressing alphabetagamma-hENaC but not in those expressing deltabetagamma-hENaC. We conclude that the delta-subunit of ENaC alters proteolytic channel activation and enhances base-line channel activity."}],"user_id":"49428","publisher":"American Society for Biochemistry and Molecular Biology","language":[{"iso":"eng"}],"department":[{"_id":"35"},{"_id":"22"}],"type":"journal_article","author":[{"last_name":"Haerteis","full_name":"Haerteis, Silke","first_name":"Silke"},{"last_name":"Krueger","full_name":"Krueger, Bettina","first_name":"Bettina","id":"49428","orcid":"0000-0001-5351-1785"},{"last_name":"Korbmacher","full_name":"Korbmacher, Christoph","first_name":"Christoph"},{"first_name":"Robert","full_name":"Rauh, Robert","last_name":"Rauh"}],"volume":284,"issue":"42","year":"2009","title":"The $\\delta$-Subunit of the Epithelial Sodium Channel (ENaC) Enhances Channel Activity and Alters Proteolytic ENaC Activation"}