Spanish as a World Language: The Interplay of Globalized Localization and Localized Globalization.

This article argues that two movements in constant interplay operate within the historical trajectory of the Spanish language: the localization that becomes globalized and the globalization that becomes localized. Equally, this article illustrates how, at the same time that Spanish is expanding in the world, new idiosyncratic and localized forms of the language are emerging. This article deals with the issues of standardization and language ideology, language contact, and redefinition of identities. The article focuses on three geographic loci: Spain, where Spanish opposes Catalan, Basque, and Galician; the United States, where migrants' Spanish dialects converge and confront English and each other; and finally, Latin America, where Spanish is in contact with Portuguese, indigenous, and Afro-Hispanic languages. The concepts that structure the discussion explain both language expansion and contraction as well as the conflict and constant negotiation between a language's standardized forms and its regional and social varieties.

Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases

OBJECTIVE: Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet aggregation, blood coagulation, and thrombus formation. In this study, we examined the synthesis and trafficking of thiol isomerases in megakaryocytes, determined their subcellular localization in platelets, and identified the cellular events responsible for their movement to the platelet surface on activation. APPROACH AND RESULTS: Immunofluorescence microscopy imaging was used to localize protein disulfide isomerase and ERp57 in murine and human megakaryocytes at various developmental stages. Immunofluorescence microscopy and subcellular fractionation analysis were used to localize these proteins in platelets to a compartment distinct from known secretory vesicles that overlaps with an inner cell-surface membrane region defined by the endoplasmic/sarcoplasmic reticulum proteins calnexin and sarco/endoplasmic reticulum calcium ATPase 3. Immunofluorescence microscopy and flow cytometry were used to monitor thiol isomerase mobilization in activated platelets in the presence and absence of actin polymerization (inhibited by latrunculin) and in the presence or absence of membrane fusion mediated by Munc13-4 (absent in platelets from Unc13dJinx mice). CONCLUSIONS: Platelet-borne thiol isomerases are trafficked independently of secretory granule contents in megakaryocytes and become concentrated in a subcellular compartment near the inner surface of the platelet outer membrane corresponding to the sarco/endoplasmic reticulum of these cells. Thiol isomerases are mobilized to the surface of activated platelets via a process that requires actin polymerization but not soluble N-ethylmaleimide-sensitive fusion protein attachment receptor/Munc13-4-dependent vesicular-plasma membrane fusion.