Maastricht University

About: Maastricht University is a education organization based out in Maastricht, Limburg, Netherlands. It is known for research contribution in the topics: Population & Health care. The organization has 19263 authors who have published 53291 publications receiving 2266866 citations. The organization is also known as: Universiteit Maastricht & UM.

Marketing Mass-Customized Products: Striking a Balance Between Utility and Complexity

Abstract: Increasingly, firms allow consumers to mass customize their products. In this study, the authors investigate consumers' evaluations of different mass customization configurations when they are asked to mass customize a product. For example, mass customization configurations may differ in the number of modules that can be mass customized. In the context of mass customization of personal computers, the authors find that mass customization configuration affects the product utility that consumers can achieve in mass customization as well as their perception of mass customization complexity. In turn, product utility and complexity affect the utility that consumers derive from using a certain mass customization configuration. More specifically, product utility has a positive effect and complexity has a negative effect on mass customization utility. The effect of complexity is direct as well as indirect because complexity also lowers product utility. The authors also find that consumers with high levels of product expertise consider mass customization configurations less complex than do consumers with low levels of product expertise and that for more-expert consumers, complexity has a less-negative impact on product utility. The study has important managerial implications for how companies can design their mass customization configuration to increase utility and decrease complexity.

Disrupting functional interactions between platelet chemokines inhibits atherosclerosis in hyperlipidemic mice.

Abstract: Atherosclerosis is characterized by chronic inflammation of the arterial wall due to chemokine-driven mononuclear cell recruitment. Activated platelets can synergize with chemokines to exacerbate atherogenesis; for example, by deposition of the chemokines platelet factor-4 (PF4, also known as CXCL4) and RANTES (CCL5), triggering monocyte arrest on inflamed endothelium. Homo-oligomerization is required for the recruitment functions of CCL5, and chemokine heteromerization has more recently emerged as an additional regulatory mechanism, as evidenced by a mutual modulation of CXCL8 and CXCL4 activities and by enhanced monocyte arrest resulting from CCL5-CXCL4 interactions. The CCL5 antagonist Met-RANTES reduces diet-induced atherosclerosis; however, CCL5 antagonism may not be therapeutically feasible, as suggested by studies using Ccl5-deficient mice which imply that direct CCL5 blockade would severely compromise systemic immune responses, delay macrophage-mediated viral clearance and impair normal T cell functions. Here we determined structural features of CCL5-CXCL4 heteromers and designed stable peptide inhibitors that specifically disrupt proinflammatory CCL5-CXCL4 interactions, thereby attenuating monocyte recruitment and reducing atherosclerosis without the aforementioned side effects. These results establish the in vivo relevance of chemokine heteromers and show the potential of targeting heteromer formation to achieve therapeutic effects.