Quantifying the Effect of Flexibility and Information Sharing in Transportation Planning

In this paper, we analyze the effect of information sharing between a wholesaler and a transport company in the Norwegian grocery supply chain. The planning process of each company is formulated as a set covering problem, where the input data of the transport company depends on the optimal solution of the wholesaler model. Information sharing is modeled through controlling which information from the wholesaler model is sent to the transport company model. We define three different cases of information sharing and introduce two types of flexibility, namely the abilities to deviate from the planned delivery date and selected routes. We use real-world data to calculate the effect of information sharing for the different cases. Our results indicate that the benefits from information sharing are limited if there is no flexibility in the system

Furin-dependent Intracellular Activation Of The Human Stromelysin-3 Zymogen

HUMAN stromelysin-3, a new member of the matrix metalloproteinase family, is expressed in tissues undergoing the active remodelling associated with embryonic development, wound healing and tumour invasion(1-3). But like all other members of the matrix metalloproteinase gene family, stromelysin3 is synthesized as an inactive precursor that must be processed to its mature form in order to express enzymic activity(4,5). Here we identify stromelysin-3 as the first matrix metalloproteinase to be discovered that can be processed directly to its enzymically active form by an obligate intracellular proteolytic event that occurs within the constitutive secretory pathway. Intracellular activation is regulated by an unusual 10-amino-acid insert sandwiched between the pro- and catalytic-domains of stromelysin-3, which is encrypted with an Arg-X-Arg-X-Lys-Arg recognition motif for the Golgi-associated proteinase, furin, a mammalian homologue of the yeast Kex2 pheromone convertase(6,7). A furin-stromelysin-3 processing axis not only differentiates the regulation of this enzyme from all previously characterized matrix metalloproteinases, but also identifies pro-protein convertases as potential targets for therapeutic intervention in matrix-destructive disease states.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/62522/1/375244a0.pd