Dong-Mook Kang
Sungkyunkwan University · 生化学・遺伝学・分子生物学
研究室紹介
Professor Dong-Mook Kang's research lab focuses on ion channel biology, particularly the molecular mechanisms underlying potassium channel function and its role in human diseases such as autosomal dominant nonsyndromic hearing loss (DFNA2). The lab investigates how genetic mutations in KCNQ4 channels affect channel activity and pharmacological responses, with a strong emphasis on the regulatory role of phospholipids like PIP2. Additionally, the lab explores bioelectromechanical systems, including engineered hybrid muscles using functionalized carbon nanotubes and C2C12 cells, for biomimetic actuation. A parallel line of inquiry examines host-microbe interactions in Drosophila, particularly the role of Duox-derived reactive oxygen species and TRPA1 channels in gut immunity and defecation regulation.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15Pathogen expulsion from the gut is an important defense strategy against infection, but little is known about how interaction between the intestinal microbiome and host immunity modulates defecation. In Drosophila melanogaster, dual oxidase (Duox) kills pathogenic microbes by generating the microbicidal reactive oxygen species (ROS), hypochlorous acid (HOCl) in response to bacterially excreted uracil. The physiological function of enzymatically generated HOCl in the gut is, however, unknown asid
There has been continuous progress in the development for biomedical engineering systems of hybrid muscle generated by combining skeletal muscle and artificial structure. The main factor affecting the actuation performance of hybrid muscle relies on the compatibility between living cells and their muscle scaffolds during cell culture. Here, we developed a hybrid muscle powered by C2C12 skeletal muscle cells based on the functionalized multi-walled carbon nanotubes (MWCNT) sheets coated with poly
Abstract Loss-of-function variant in the gene encoding the KCNQ4 potassium channel causes autosomal dominant nonsyndromic hearing loss (DFNA2), and no effective pharmacotherapeutics have been developed to reverse channel activity impairment. Phosphatidylinositol 4,5-bisphosphate (PIP 2 ), an obligatory phospholipid for maintaining KCNQ channel activity, confers differential pharmacological sensitivity of channels to KCNQ openers. Through whole-exome sequencing of DFNA2 families, we identified th
Muscarinic receptor subtypes controlling the nonselective cationic current in response to carbachol (ICCh) were studied in circular smooth muscle cells of the guinea pig gastric antrum using putative muscarinic agonists and antagonists. Both oxotremorine-M (an M2-selective agonist) and CCh dose-dependently activated the cationic current with EC50 values of 0.21 +/- 0.01 microm and 0.97 +/- 0.06 microM, respectively. In contrast, pilocarpine and McN-A 343 (an M1-selective and a putative M4 agonis
Abstract Mutations in potassium voltage-gated channel subfamily Q member 4 ( KCNQ4 ) are etiologically linked to a type of nonsyndromic hearing loss, deafness nonsyndromic autosomal dominant 2 (DFNA2). We performed whole-exome sequencing for 98 families with hearing loss and found mutations in KCNQ4 in five families. In this study, we characterized two novel mutations in KCNQ4 : a missense mutation (c.796G>T; p.Asp266Tyr) and an in-frame deletion mutation (c.259_267del; p.Val87_Asn89del). p.A
We have used ion-selective electrodes (ISEs) to quantify ion fluxes across giant membrane patches by measuring and simulating ion gradients on both membrane sides. Experimental conditions are selected with low concentrations of the ions detected on the membrane side being monitored. For detection from the cytoplasmic (bath) side, the patch pipette is oscillated laterally in front of an ISE. For detection on the extracellular (pipette) side, ISEs are fabricated from flexible quartz capillary tubi
We investigated the properties of carbachol (CCh)-activated nonselective cation channels (NSC(CCh)) at the single channel level in the gastric myocytes of guinea pigs using a magnified whole-cell mode or an outside-out mode. The channel activity (NPo) recorded in a magnified whole-cell mode increased with depolarization (from -120 to -20 mV) and had the half activation potential of -81 mV under the symmetrical 140 mM Cs+ condition. The single channel conductance depended upon the extracellular m