Year: 2001
Type: article
Abstract: Surface plasmon resonance (SPR) allows examination of protein-protein interactions in real time, from which both binding affinities and kinetics can be directly determined. We have used the SPR technique to search for proteins in heart tissue that would be candidate binding partners for the cardiac gap junction protein, connexin43 (Cx43). Heart lysate showed a strong, pH-dependent binding to the carboxyl terminus (CT) of Cx43 (amino acids 254-382) covalently linked to an SPR cuvette. Binding was inhibited by the presence of v-src transfected 3T3 cell lysate, suggesting that binding partners in these two lysates may compete for overlapping epitopes on Cx43CT. The combined application of proteomic and functional studies is expected to identify which proteins within heart tissue interact with Cx43 and what roles they may play in gap junction function.
Source: Cell Communication & Adhesion
Language: English
Topic: Connexins and lens biology
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Awards: G1193154975, G1404856315, A gap junction-independent role for Connexin43 in cardiac electrophysiology, G2264610468, G2575637574, Molecular Neuropathology, G3508417182, G3591254803, Intercellular Communication and Impulse Propagation, LENS GAP JUNCTIONS--IDENTITY AND PROPERTIES, The Astrocyte Nexus: CX43-Protein Interactions, Liver Cell Membrane Protein-Expression and Function, GAP JUNCTIONS AND SCHWANN CELLS, G882646002
OpenAlex ID: W2114180381