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Replicating different roles of intent across moral domains.

ABSTRACT: Whether moral cognition is underpinned by distinct mental systems that process different domains of moral information (moral pluralism) is an important question for moral cognition research. The reduced importance of intent (intentional versus accidental action) when judging purity (e.g. incest), when compared with harm (e.g. poisoning), moral violations is, arguably, some of the strongest experimental evidence for distinct moral systems or 'foundations'. The experiment presented here is a replication attempt of these experimental findings. A pre-registered replication of Experiment 1B from the original article documenting this effect was conducted in a sample of N = 400 participants. Findings from this successful replication are discussed in terms of theoretical and methodological implications for approaches to moral cognition.

SUBMITTER: Sweetman J

PROVIDER: S-EPMC7277250 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Replicating different roles of intent across moral domains.

Sweetman Joseph J Newman George A GA

Royal Society open science 20200527 5

Whether moral cognition is underpinned by distinct mental systems that process different domains of moral information (moral pluralism) is an important question for moral cognition research. The reduced importance of intent (intentional versus accidental action) when judging purity (e.g. incest), when compared with harm (e.g. poisoning), moral violations is, arguably, some of the strongest experimental evidence for distinct moral systems or 'foundations'. The experiment presented here is a repli ...[more]

PMID: 32537185

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Project description:BackgroundThe transcription factor Pax6 functions in the specification and maintenance of the differentiated cell lineages in the endocrine pancreas. It has two DNA binding domains, the paired domain and the homeodomain, in addition to a C-terminal transactivation domain. The phenotype of Pax6-/- knockout mice suggests non-redundant functions of the transcription factor in the development of glucagon-expressing alpha-cells as this cell type is absent in the mutants. We ask the question of how the differentiation of pancreatic endocrine cells, in particular that of alpha-cells, is affected by selective inactivation of either one of the three major domains of Pax6.ResultsThe Pax6Aey18 mutant mouse line, in which the paired domain is inactivated, showed a phenotype similar to that of Pax6-/- knockout mice with a near complete absence of glucagon-positive alpha-cells (0-4 cells/section; < or =1% of wt), reduced beta-cell area (74% of wt) and disorganized islets. The proportion of ghrelin-positive epsilon-cells was expanded. In Pax6Sey-Neu mutants, which lack the transactivation domain, alpha-and beta-cells where reduced to 25 and 40% of wt, respectively. We also studied two mouse lines with mutations in the homeodomain, Pax64Neu and Pax6132-14Neu. Neighboring amino acids are affected in the two lines and both point mutations abolish DNA binding of the classical P3 homeodomain target sequence. The pancreatic phenotype of the two mutants however was divergent. While Pax64Neu homozygotes showed a reduction of alpha- and beta-cells to 59 and 61%, respectively, pancreatic endocrine development was unaltered in the Pax6132-14Neu mutant strain.ConclusionsWe show that inactivation of the Pax6 paired domain leads to a more severe phenotype with regards to the differentiation of pancreatic alpha-cells than the loss of the transactivation domain. The analysis of two different homeodomain mutants suggests that the binding of Pax6 to P3 homeodomain consensus sequences is not required for alpha-cell development. It rather seems that the homeodomain has a modulating role in Pax6 function, possibly by facilitating a PH0-like binding confirmation on paired domain target genes like proglucagon. This function is differentially affected by the two homeodomain mutations analyzed in this study.

Dataset Information

Replicating different roles of intent across moral domains.

Publications

Replicating different roles of intent across moral domains.

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