Isolation and characterization of the human gene encodingI to: further diversity by alternative mRNA splicing
W Kong, S Po, T Yamagishi… - American Journal …, 1998 - journals.physiology.org
W Kong, S Po, T Yamagishi, MD Ashen, G Stetten, GF Tomaselli
American Journal of Physiology-Heart and Circulatory Physiology, 1998•journals.physiology.orgThe transient outward K+ current (I to) in the heart is responsible for the initial phase of
repolarization and for setting the plateau voltage of the ventricular action potential. Recently,
Kv4. 3 has emerged as the leading candidate α-subunit gene that underlies I to in larger
mammals such as dogs and humans. We have cloned the human Kv4. 3 homolog and
describe a carboxyl-terminal splice variant that inserts 19 amino acids with a consensus
protein kinase C (PKC) phosphorylation site into the protein after the last membrane …
repolarization and for setting the plateau voltage of the ventricular action potential. Recently,
Kv4. 3 has emerged as the leading candidate α-subunit gene that underlies I to in larger
mammals such as dogs and humans. We have cloned the human Kv4. 3 homolog and
describe a carboxyl-terminal splice variant that inserts 19 amino acids with a consensus
protein kinase C (PKC) phosphorylation site into the protein after the last membrane …
The transient outward K+ current (I to) in the heart is responsible for the initial phase of repolarization and for setting the plateau voltage of the ventricular action potential. Recently, Kv4.3 has emerged as the leading candidate α-subunit gene that underliesI to in larger mammals such as dogs and humans. We have cloned the human Kv4.3 homolog and describe a carboxyl-terminal splice variant that inserts 19 amino acids with a consensus protein kinase C (PKC) phosphorylation site into the protein after the last membrane-spanning segment. The coding region of Kv4.3 is comprised of at least five exons and is located on chromosome 1p13.3. In the basal state the basic biophysical properties of both of the splice variants are identical.
American Physiological Society