Vertical integration or specialisation: producing and commercialising cotton goods (1815-1913)

This article describes the ways in which cotton goods were commercialised during the nineteenth century and the first third of the twentieth. Several national cases are analysed: Britain, as the Workshop of the World; France, Germany, Switzerland and the US, as core economies; and Italy and Spain as countries on the European periphery. The main question that we address is why some cotton industries vertically integrated their production and commercialisation processes, but others did not. We present a model that combines industrial district size and product differentiation to explain why vertical integration was present in most cases and why there was vertical specialisation in Lancashire and Lowell.

[4 phot. des monuments élevés par Jean Joseph de La Borde dans le parc de son château de Méréville (Seine-et-Oise), à la fin du XVIIIe siècle, à la mémoire de ses deux fils, de La Borde-Marchainville et de La Borde-Boutervilliers, officiers de l'Astrolabe, péris avec La Pérouse en 1786, ainsi qu'à la mémoire du capitaine Cook, don du prince Roland Bonaparte en 1896. Voir les CR. des séances de la S.G., 1896, p. 319-321]

Donateur : Bonaparte, Roland (1858-1924)

Calpastatin-mediated inhibition of calpains in the mouse brain prevents mutant ataxin 3 proteolysis, nuclear localization and aggregation, relieving Machado-Joseph disease.

Machado-Joseph disease is the most frequently found dominantly-inherited cerebellar ataxia. Over-repetition of a CAG trinucleotide in the MJD1 gene translates into a polyglutamine tract within the ataxin 3 protein, which upon proteolysis may trigger Machado-Joseph disease. We investigated the role of calpains in the generation of toxic ataxin 3 fragments and pathogenesis of Machado-Joseph disease. For this purpose, we inhibited calpain activity in mouse models of Machado-Joseph disease by overexpressing the endogenous calpain-inhibitor calpastatin. Calpain blockage reduced the size and number of mutant ataxin 3 inclusions, neuronal dysfunction and neurodegeneration. By reducing fragmentation of ataxin 3, calpastatin overexpression modified the subcellular localization of mutant ataxin 3 restraining the protein in the cytoplasm, reducing aggregation and nuclear toxicity and overcoming calpastatin depletion observed upon mutant ataxin 3 expression. Our findings are the first in vivo proof that mutant ataxin 3 proteolysis by calpains mediates its translocation to the nucleus, aggregation and toxicity and that inhibition of calpains may provide an effective therapy for Machado-Joseph disease.