Are you sure? The relationship between response certainty and performance in visual detection using a perimetry-style task.

Conventional psychophysical methods ignore the degree of confidence associated with each response. We compared the psychometric function for detection with that for "absolute certainty" in a perimetry-style task, to explore how knowledge of response certainty might aid the estimation of detection thresholds. Five healthy subjects performed a temporal 2-AFC detection task, indicating on each trial whether they were "absolutely certain." The method of constant stimuli was used to characterize the shape of the two psychometric functions. Four eccentricities spanning central and peripheral vision were tested. Where possible, conditions approximated those of the Humphrey Field Analyzer (spot size, duration, background luminance, test locations). Based on the empirical data, adaptive runs (ZEST) were simulated to predict the likely improvement in efficiency obtained by collecting certainty information. Compared to detection, threshold for certainty was 0.5 to 1.0 dB worse, and slope was indistinguishable across all eccentricities tested. A simple two-stage model explained the threshold difference; under this model, psychometric functions for detection and for certainty-given-detection are the same. Exploiting this equivalence is predicted to reduce the number of trials required to achieve a given level of accuracy by approximately 30% to 40%. The chances of detecting a spot and the chances of certainty-given-detection were approximately the same in young, healthy subjects. This means, for example, that a spot detected at threshold was labeled as "certainly" detected approximately half the time. The collection of certainty information could be used to improve the efficiency of estimation of detection thresholds.

Identification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis.

Dipeptidyl peptidase 9 (DPP9) is a member of the S9B/DPPIV (DPP4) serine protease family, which cleaves N-terminal dipeptides at an Xaa-Pro consensus motif. Cytoplasmic DPP9 has roles in epidermal growth factor signalling and in antigen processing, whilst the role of the recently discovered nuclear form of DPP9 is unknown. Mice lacking DPP9 proteolytic activity die as neonates. We applied a modified 2D differential in-gel electrophoresis approach to identify novel DPP9 substrates, using mouse embryonic fibroblasts lacking endogenous DPP9 activity. A total of 111 potential new DPP9 substrates were identified, with nine proteins/peptides confirmed as DPP9 substrates by MALDI-TOF or immunoblotting. Moreover, we also identified the dipeptide Val-Ala as a consensus site for DPP9 cleavage that was not recognized by DPP8, suggesting different in vivo roles for these closely related enzymes. The relative kinetics for the cleavage of these nine candidate substrates by DPP9, DPP8 and DPP4 were determined. This is the first identification of DPP9 substrates from cells lacking endogenous DPP9 activity. These data greatly expand the potential roles of DPP9 and suggest different in vivo roles for DPP9 and DPP8.