The current study examines the construct validity of the Maximization Scale (MS; Schwartz et al., 2002) and the Maximization Tendency Scale (MTS; Diab et al., 2008) as well as the nomological net of the maximizing construct. We find that both scales of maximizing suffer psychometrically, especially in their proposed dimensionality. Using confirmatory factor analysis and item response theory (IRT) we identify and remove three problematic items from the MTS and six problematic items from the MS. Additionally, we find that the MS appears to be measuring difficulty and restlessness with the search for the best alternative, whereas the MTS is more focused on the search for the best option, regardless of choice difficulty. We then examined these revised scales in relation to other psychological constructs in the nomological net for maximizing and found that maximizers may not be unhappy but are generally distressed in the decision-making context. Finally, we suggest that future maximizng research use revised form of the MTS that seems to us to be most consistent with the original concept of maximizing/satisficing.
The chemokines CCL17 (TARC) and CCL22 (MDC) function through the same receptor, CCR4, but have been proposed to differentially affect the immune response. To better understand the role of the individual ligands, a panel of rat anti-mouse CCL17 surrogate antibodies was generated that can be used to differentiate CCL17 and CCL22 function in vitro and in vivo. We have successfully identified a panel of neutralizing antibodies by screening hybridomas for the ability to inhibit CCL17-mediated calcium mobilization. Chemotaxis in response to CCL17 is also inhibited, providing further evidence that the antibodies in this panel are antagonistic. Using a recombinant cell line expressing human CCR4, we show that the antibodies block β-arrestin recruitment as evidence that the antibodies are specifically blocking CCL17 signaling through CCR4. The antibodies within this panel inhibit calcium mobilization with varying potency in the calcium flux assay, having apparent IC50 ranging from approximately 1 to >400 ng/mL. Although both CCL17 and CCL22 function through CCR4, only a single antibody was identified as having detectable binding to CCL22. This panel of CCL17-specific antibodies provides tools that can be used to differentiate CCL17 and CCL22 function through CCR4 interaction in vitro and in vivo.
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