Expression and function of native potassium channel (K V α1) subunits in terminal arterioles of rabbit
Autor: | Alexandra M. Dedman, Alex Cheong, David J. Beech |
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Rok vydání: | 2001 |
Předmět: |
Male
medicine.medical_specialty Potassium Channels Physiology Xenopus Scorpion Venoms Muscle Smooth Vascular Cell membrane Kv1.5 Potassium Channel Xenopus laevis Cerebral circulation Internal medicine Kv1.2 Potassium Channel Potassium Channel Blockers medicine Animals Tissue Distribution 4-Aminopyridine biology Chemistry Cell Membrane Electric Conductivity Potassium channel blocker Depolarization Original Articles biology.organism_classification Molecular biology Triterpenes Potassium channel Arterioles medicine.anatomical_structure Endocrinology Potassium Channels Voltage-Gated Cerebrovascular Circulation Oocytes Endothelium Vascular Rabbits Amifampridine medicine.symptom Vasoconstriction Delayed Rectifier Potassium Channels medicine.drug |
Zdroj: | The Journal of Physiology. 534:691-700 |
ISSN: | 1469-7793 0022-3751 |
DOI: | 10.1111/j.1469-7793.2001.00691.x |
Popis: | 1. In this study we investigated the expression and function of the K(V)alpha1 subfamily of voltage-gated K(+) channels in terminal arterioles from rabbit cerebral circulation. 2. K(+) current was measured from smooth muscle cells within intact freshly isolated arteriolar fragments. Current activated on depolarisation positive of about -45 mV and a large fraction of this current was blocked by 3,4-diaminopyridine (3,4-DAP) or 4-aminopyridine (4-AP), inhibitors of K(V) channels. Expression of cRNA encoding K(V)1.6 in Xenopus oocytes also generated a 4-AP-sensitive K(+) current with a threshold for activation near -45 mV. 3. Immunofluorescence labelling revealed K(V)1.2 to be specifically localised to endothelial cells, and K(V)1.5 and K(V)1.6 to plasma membranes of smooth muscle cells. 4. K(V) channel current in arteriolar fragments was blocked by correolide (which is specific for the K(V)alpha1 family of K(V) channels) but was resistant to recombinant agitoxin-2 (rAgTX2; which inhibits K(V)1.6 but not K(V)1.5). Heterologously expressed K(V)2.1 was resistant to correolide, and K(V)1.6 was blocked by rAgTX2. 5. Arterioles that were mildly preconstricted and depolarised by 0.1-0.3 nM endothelin-1 constricted further in response to 3,4-DAP, 4-AP or correolide, but not to rAgTX2. 6. We suggest that K(V)alpha1 channels are expressed in smooth muscle cells of terminal arterioles, underlie a major part of the voltage-dependent K(+) current, and have a physiological function to oppose vasoconstriction. K(V)alpha1 complexes without K(V)1.5 appear to be uncommon. |
Databáze: | OpenAIRE |
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