Skip to: site menu | section menu | main content

Currently viewing: Gender Physiology » Return Home

 

Menu:

 
Return to Member's page

Tzyh-Chang (TC) Hwang, PhD

Associate Professor, Department of Medical Pharmacology and Physiology, Dalton Investigator

 

Medical Pharmacology and Physiology
222C Dalton Cardiovascular Research Center
Columbia, MO 65211
573-882-2181
HwangT@health.missouri.edu

Cystic fibrosis, the most common lethal genetic disease in Caucasians, is caused by mutations that reduce chloride channel activity of the CFTR protein. The CFTR chloride channel is activated by protein kinase A (PKA)-dependent phosphorylation. ATP binding/ hydrolysis in two nucleotide binding domains (NBD1 and NBD2) of CFTRis coupled to the opening and closing of the phosphorylated channel. The most common CF- associated mutation, F508, causes an abnormal retention of the mutant protein in the endoplasmic reticulum. A small portion of F508 CFTR proteins can reach the plasma membrane and function as chloride channels. However, kinetic studies of these mutant CFTR channels in cell-attached patches indicate a lower open probability in response to cAMP stimulation compared to the wild-type channels. Genistein, a plant isoflavone that is abundant in legumes, can dramatically enhance F508 CFTR channel currents activated via the cAMP pathway. This effect of genistein appears to be caused by a direct binding of genistein to the CFTR. Current studies are focused on understanding the molecular nature of genistein binding site(s) and on the kinetic mechanism of genistein's action. Their work on CFTR modulation could potentially provide information useful for drug design and therapeutic intervention for cystic fibrosis.

 

More information on Dr. Hwang and his lab can be found here.

Research Areas of Interest

Biological physics
Biomedical engineering
Cardiovascular biology/ research
Cell biology
Cellular signaling
Child health
Electrophysiology
Genetics
Hormone action
Membrane transport
Molecular biology
Molecular genetics
Neuroscience
Protein biology
Protein phosphorylation
Protein structure/function
Pulmonary