Is carotid artery stiffness related to endothelial function in young healthy subjects?
Carotid artery elasticity in health is not related to conduit artery FMD, suggesting that endothelial influence on baroreceptor activity is not exerted through changes in barosensory wall elasticity.
The orientation of the Ref-1 peptide in the hTRX-Ref-1 complex is opposite to that found in the previously solved complex of hTRX with the target peptide from the transcription factor NF kappa B. Orientation is determined by three discriminating interactions involving the nature of the residues at the P-2' P-4 and P-5 binding positions. (P0 defines the active cysteine of the peptide, Cys65 for Ref-1 and Cys62 for NF kappa B. Positive and negative numbers indicate residues N-terminal and C-terminal to this residue, respectively, and vice versa for NF kappa B as it binds in the opposite orientation.) The environment surrounding the reactive Cys32 of hTRX, as well as the packing of the P+3 to P-4 residues are essentially the same in the two complexes, despite the opposing orientation of the peptide chains. This versatility in substrate recognition permits hTRX to act as a wide-ranging redox regulator for the cell.