By Warren J. Gallin, Andrew N. Spencer (auth.), Stephen L. Archer, Nancy J. Rusch (eds.)
Potassium channels (K+) are membrane-spanning proteins which serve many very important capabilities and have gotten a sizzling subject in body structure. K+ channels ascertain or modulate many services of vascular tender muscle, endothelial and inflammatory cells, and therefore are critical to law of arterial tone and regulate of mobile proliferation. also they are promising pursuits for antihypertensive remedies with medications which open and shut particular varieties of K+ channels, making for an energetic box of study. With their skill to manage vascular tone, voltage-gated K+ channels play an important function in either pulmonary and systemic high blood pressure in addition to in cardiac arrhythmias. This booklet will spotlight the most recent discoveries by way of top researchers touching on the function of K+ channels within the center and blood vessels in basic body structure and quite a few ailment states.
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Extra resources for Potassium Channels in Cardiovascular Biology
Sample text
Cardiac Action Potentials and the QT Interval . . . . . . Molecular Genetic Approaches to the Identification of LQTS Genes Molecular Mechanisms of LQTS Mutations . . . . Mutations in KVLQTl, the Gene Encoding the a-Subunit of I Ks Channels Mutations in KvLQT1-Like Channels Also Cause Disease . Mutations in minK, the Gene Encoding the fJ-Subunit of hs Channels Recessive Mutations in KVLQT1 or minK Cause LQTS and Congenital Sensorineural Hearing Loss. .
2. Electrophysiological Alterations in Myocytes from Hypertrophied and Failing Hearts . . . . . . . . . . . . 3. Decreased Expression of Kv4 Subfamily Channel Subunit mRNAs in Hypertrophied and Failing Hearts-a Molecular Mechanism Underlying the Reduction in Ito . . . . . . . . . . 4. Mechanisms for the Decreased Expression of Kv4 Subfamily Channel mRNAs and Ito Channels in Hypertrophied and Failing Hearts .. 5. Region-Specific Expression of Ito and Its Alterations by Hypertrophy and Heart Failure 6.
Cohen, S. , Chait, B. , 1998, Crystal structure and functional analysis of the HERG potassium channel N terminus:A eukaryotic PAS domain, Cell 95:649-655. Papazian, D. , Shao, X. , Seoh, S. , Mock, A. , and Wainstock, D. , 1995, Electrostatic interactions of S4 voltage sensor in Shaker K + channel, Neuron 14:1293-1301. , Jan, Y. , and Jan, L. , 1996, Contributions of a negatively charged residue in the hydrophobic domain of the IRK1 inwardly rectifying K + channel to K +-selective permeation, Biophys.