Calcium Transients Closely Reflect Prolonged Action Potentials in iPSC Models of Inherited Cardiac Arrhythmia

Autor: Craig T. January, Kevin E. Healy, Jianhua Zhang, Ethan A. Hua, Marie A.F. Sears, Jonathan C. Makielski, Julianne Wojciak, Melvin M. Scheinman, Paweena Lizarraga, Chi-cheng Fu, Kenta Nakamura, Sadguna Y. Balijepalli, Yohei Hayashi, Shiro Baba, Shinya Yamanaka, C. Ian Spencer, Kiichiro Tomoda, Timothy J. Kamp, Bruce R. Conklin, Katriina Aalto-Setälä

Publikováno v: Stem cell reports, vol 3, iss 2
Stem Cell Reports
Stem Cell Reports, Vol 3, Iss 2, Pp 269-281 (2014)
Spencer, CI; Baba, S; Nakamura, K; Hua, EA; Sears, MAF; Fu, CC; et al.(2014). Calcium transients closely reflect prolonged action potentials in iPSC models of inherited cardiac arrhythmia. Stem Cell Reports, 3(2), 269-281. doi: 10.1016/j.stemcr.2014.06.003. UCSF: Retrieved from: http://www.escholarship.org/uc/item/9720z7s2

Summary Long-QT syndrome mutations can cause syncope and sudden death by prolonging the cardiac action potential (AP). Ion channels affected by mutations are various, and the influences of cellular calcium cycling on LQTS cardiac events are unknown.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5ebbd4c5318efa324a08bf6727d5553

Rat Brain Thioltransferase : Regional Distribution, Immunological Characterization, and Localization by Fluorescent In Situ Hybridization

Autor: K. V. Swamy, Padmashree S. Tirumalai, Vijayalakshmi Ravindranath, Michael R. Boyd, John J. Mieyal, Sadguna Y. Balijepalli

Publikováno v: Journal of Neurochemistry. 72:1170-1178

Thioltransferase (TTase) is a member of the family of thiol-disulfide oxidoreductases that are involved in the maintenance of sulfhydryl homeostasis in cells by catalyzing thiol-disulfide interchange reactions. One of the major consequences of oxidat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4da25ad73c08b92e3b1d4622aec4fc59
https://doi.org/10.1046/j.1471-4159.1999.0721170.x

Mouse ERG K(+) channel clones reveal differences in protein trafficking and function

Autor: John W. Kyle, Craig T. January, Sarah P. Concannon, Corey L. Anderson, Sadguna Y. Balijepalli, Jonathan C. Makielski, Evi Lim, Eric C. Lin, Brooke M. Moungey

Publikováno v: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

Background The mouse ether‐a‐go‐go‐related gene 1a ( mERG 1a, mKCNH 2 ) encodes mERG K + channels in mouse cardiomyocytes. The mERG channels and their human analogue, hERG channels, conduct I Kr . Mutations in hERG channels reduce I Kr to cau

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb02da9b69fba4985ac25ca5fc0da55b
https://pubmed.ncbi.nlm.nih.gov/25497881

Mechanism of Loss of Kv11.1 K+ Current in Mutant T421M-Kv11.1 Expressing Rat Ventricular Myocytes: Interaction of Trafficking and Gating

Autor: David J. Tester, Craig T. January, Chen L. Chew, Sadguna Y. Balijepalli, Kassandra E. Holzem, Sarah P. Concannon, Brian P. Delisle, Michael J. Ackerman, Ravi C. Balijepalli, Evi Lim

Background— Type 2 long QT syndrome involves mutations in the human ether a-go-go–related gene ( hERG or KCNH2 ). T421M, an S1 domain mutation in the Kv11.1 channel protein, was identified in a resuscitated patient. We assessed its biophysical, p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad185b9da9386bdee4e9c1f926d1c1f2
https://europepmc.org/articles/PMC3530382/

Rescue of mutated cardiac ion channels in inherited arrhythmia syndromes

Autor: Eric C. Lin, Corey L. Anderson, Craig T. January, Sadguna Y. Balijepalli

Publikováno v: Journal of cardiovascular pharmacology. 56(2)

Inherited arrhythmia syndromes comprise an increasingly complex group of diseases involving mutations in multiple genes encoding ion channels, ion channel accessory subunits and channel interacting proteins, and various regulatory elements. These mut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4daa12691e093bfb8658178f65a8d67d
https://pubmed.ncbi.nlm.nih.gov/20224422