Validating the response surface method in entrepreneurship management research.

This study adapts an existing methodology in psychology to assess congruence relationships in entrepreneurship management. More specifically, it describes the application of a response surface method to examine the congruence effect of two predictor variables on an outcome variable. The study presents both visual and text presentations to serve as a guideline that can aid management researchers in adapting the method. The paper underscores three strengths of using the response surface method as a robust analytical approach to evaluating congruent and incongruent relationships.•The response surface method can be used to examine congruency and incongruency between variables in the field of management in general and entrepreneurship management in particular.•The results can be visualized as two- and three-dimensional graphs.•Compared with a traditional approach, the response surface method offers a clearer visual representation of a focal relationship.

LPS-induced galectin-3 oligomerization results in enhancement of neutrophil activation.

Galectin-3 (Gal 3) is a glycan-binding protein that can be secreted by activated macrophages and mast cells at inflammation sites and plays an important role in inflammatory diseases caused by Bacteria and their products, such as lipopolysaccharides (LPS). Although it is well established that Gal 3 can interact with LPS, the pathophysiological importance of LPS/Gal 3 interactions is not fully understood. Data presented herein demonstrate for the first time that the interaction of Gal 3, either via its carbohydrate binding C-terminal domain or via its N-terminal part, with LPS from different bacterial strains, enhances the LPS-mediated neutrophil activation in vitro. Gal 3 allowed low LPS concentrations (1 µg/mL without serum, 1 ng/mL with serum) to upregulate CD11b expression and reactive oxygen species (ROS) generation on human neutrophils in vitro and drastically enhanced the binding efficiency of LPS to the neutrophil surface. These effects required LPS preincubation with Gal 3, before neutrophil stimulation and involved specific Gal 3/LPS interaction. A C-terminal Gal-3 fragment, which retains the lectin domain but lacks the N-terminal part, was still able to bind both to Escherichia coli LPS and to neutrophils, but had lost the ability to enhance neutrophil response to LPS. This result emphasizes the importance of an N-terminus-mediated Gal 3 oligomerization induced by its interaction with LPS. Finally we demonstrated that Balb/C mice were more susceptible to LPS-mediated shock when LPS was pretreated with Gal 3. Altogether, these results suggest that multimeric interactions between Gal 3 oligomers and LPS potentiate its pro-inflammatory effects on neutrophils.