A series of participative budgeting experiments has examined the effect of incentive structures and/or information environments on employees' reporting and production decisions. We analyze the previous experiments in terms of the insights they offer regarding agency theory. We expand the previous analyses of the incentive contracting experiments in three ways. First, we classify the earliest set of participative budgeting experiments based on the type of incentive and information structures examined in each study. Second, from the 21 papers we review, we identify eight specific cases for which the experimental evidence contradicts an agency theory prediction (i.e., anomalies). Third, we develop a classification scheme that can be used to organize hypotheses in terms of whether they rely on an agency theory prediction, a competing behavioral prediction, or a combination of the two. We use this classification to illustrate why we believe that studies that test both an agency theory prediction and a competing behavioral prediction are more likely to advance the development of theory than those that do not.

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These results identify CVS-3983 as a potent inhibitor of AI prostate cancer cell invasion in vitro and established xenograft tumor growth in vivo.

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Human alpha-1-proteinase inhibitor (AlPI) deficiency, associated with the Z-variant AlPI (AlPI/Z) gene, results from defective secretion of the inhibitor from the liver. The AlPI/Z gene exhibits two point mutations which specify amino acid substitutions, Val-213 to Ala and Glu-342 to Lys. The functional importance of these substitutions in AlPI deficiency was investigated by studying the secretion of AlPI synthesized in COS cells transfected with AlPI genes altered by site-directed mutagenesis. This model system correctly duplicates the secretion defect seen in individuals homozygous for the AlPI/Z allele and shows that the substitution of Lys for Glu-342 alone causes defective secretion of AlPI. The substitution of Lys for eliminates the possibility for a salt bridge between residues 342 and 290, which may decrease the conformational stability of the molecule and thus account for the secretion defect. However, when we removed the potential to form a salt bridge from the wild-type inhibitor by changing Lys-290 to Glu (AIPI/SB-290Glu), secretion was not reduced to the 19% of normal level seen for AlPI/Z-342Lys; in fact, 75% of normal secretion was observed. When the potential for salt bridge formation was returned to AlPI/Z-342Lys by changing Lys-290 to Glu, only 46% of normal secretion was seen. These data indicate that the amino acid substitution at position 342, rather than the potential to form the 290-342 salt bridge, is the critical alteration leading to the defect in AlPI secretion.Alpha-1-proteinase inhibitor (AlPI), an inhibitor of serine proteases, is one of the major serum glycoproteins synthesized in and secreted by the liver. Individuals homozygous for the Z-variant AlPI (AlPI/Z) gene have about 15% of the normal circulating level of this protease inhibitor and as a result are predisposed to pulmonary emphysema and hepatic cirrhosis (6). The decreased serum levels of AlPI in affected individuals are caused by impaired secretion of AlPI from the liver rather than by defective synthesis of the protein (5). This conclusion is supported by the observations that the levels of AiPI mRNA in affected and normal livers are essentially the same (30), the efficiencies of translation of these mRNAs are not significantly different (1,25,30), and AlPI/Z accumulates in the endoplasmic reticulum (ER) of the liver (4). The only demonstrated differences between the normal (AlPI/M) and variant (AlPI/Z) forms of this protein are two changes in the primary sequence. In A1PI/Z, alanine is substituted for valine at position 213 (23, 27) and lysine is stibstituted for glutamic acid at position 342 (13). These substitutions do not appear to cause major changes in the conformation of A1PI/Z, since the specific trypsin-inhibitory capacities, circulating half-lives, sedimentation coefficients (1, 21), immunological activities (34), and oligosaccharide structures (1, 35) of the serum forms of AlPI/Z and AlPI/M appear to be identical. Furthermore, after solubilization, the AlPI/Z that accumulates in inclusion bodies in the ER of...