Effects of Different Visual Flow Velocities on Psychophysiological Responses During Virtual Reality Cycling.

Introduction: Virtual reality cycling (VRC) is simulated outdoor cycling with changes in scenery in virtual reality (VR) with rotating ergometer pedals. The speed at which the scenery changes, which is the visual flow velocity, can shift according to the same pedal rotation speed.

Objectives: This study investigated the effects of different visual flow velocities on the psychophysiological responses of cyclists using the VRC.

Accumulation of ACE inhibitory tripeptides, Val-Pro-Pro and Ile-Pro-Pro, in vascular endothelial cells.

The antihypertensive peptides, Val-Pro-Pro and Ile-Pro-Pro, were successfully detected in the aorta of spontaneously hypertensive rats after orally administering these peptides by a guanidine-thiocyanate treatment to prevent proteolysis. Cy3-labeled versions of both peptides were localized in the endothelial cells of arterial vessels in the rats. The accumulation of both peptides in the endothelial cells suggested in vivo inhibitory activity of the angiotensin I-converting enzyme.

Study of the mechanism of antihypertensive peptides VPP and IPP in spontaneously hypertensive rats by DNA microarray analysis.

Many antihypertensive effects of angiotensin-I-converting enzyme (ACE) inhibitory peptides have been studied in spontaneously hypertensive rats (SHRs) and human, however, the mild actions of these peptides expressed by these consecutive uptakes are still not clear. Here, to understand the in vivo antihypertensive effects of well-characterized two peptides, Val-Pro-Pro (VPP) and Ile-Pro-Pro (IPP), DNA microarray was used to analyze gene expression in SHRs fed these peptides for 5 days. By using an Affymetrix analyzer, gene profiling was performed in a target organ, the aorta, of SHRs after repeated administration of VPP and IPP for 5 days.

Structural properties of the DNA-bound form of a novel tandem repeat DNA-binding domain, STPR.

Fibroin-modulator-binding protein 1 (FMBP-1) is a predicted transcription factor of the silkworm fibroin gene. The DNA-binding domain of FMBP-1 consists of four almost perfect tandem repeats of 23 amino acids each (R1-R4), and is referred to as the score and three amino acid peptide repeat (STPR) domain. This characteristic domain is conserved in eukaryotes, but the DNA-binding mode is not known.

Structural approach to a novel tandem repeat DNA-binding domain, STPR, by CD and NMR.

Fibroin-modulator-binding protein 1 (FMBP-1) is a factor that binds the transcriptional activation elements of the fibroin gene. It has a novel structure, consisting of four tandem repeats (R1-R4) of 23 amino acids each in the C-terminal half. This region is referred to as the STPR (score and three amino acid peptide repeat) domain and acts as a DNA-binding domain in FMBP-1.