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1.
Group Processes & Intergroup Relations ; : 1, 2021.
Article in English | Academic Search Complete | ID: covidwho-1477188

ABSTRACT

How do global citizens respond to a global health emergency? The present research examined the association between global citizen identification and prosociality using two cross-national datasets—the World Values Survey (Study 1, N = 93,338 from 60 countries and regions) and data collected in 11 countries at the start of the COVID-19 pandemic (Study 2, N = 5,427). Results showed that individuals who identified more strongly as global citizens reported greater prosociality both generally (Study 1) and more specifically in the COVID-19 global health emergency (Study 2). Notably, global citizen identification was a stronger predictor of prosociality in response to COVID-19 than national identification (Study 2). Moreover, analyses revealed that shared ingroup identity accounted for the positive association between global citizen identification and prosociality (Study 2). Overall, these findings highlight global citizenship as a unique and promising direction in promoting prosociality and solidarity, especially in the fight against COVID-19. [ABSTRACT FROM AUTHOR] Copyright of Group Processes & Intergroup Relations is the property of Sage Publications, Ltd. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

2.
J Biol Chem ; 295(36): 12686-12696, 2020 09 04.
Article in English | MEDLINE | ID: covidwho-1387615

ABSTRACT

Type II transmembrane serine proteases (TTSPs) are a group of enzymes participating in diverse biological processes. Some members of the TTSP family are implicated in viral infection. TMPRSS11A is a TTSP expressed on the surface of airway epithelial cells, which has been shown to cleave and activate spike proteins of the severe acute respiratory syndrome (SARS) and the Middle East respiratory syndrome coronaviruses (CoVs). In this study, we examined the mechanism underlying the activation cleavage of TMPRSS11A that converts the one-chain zymogen to a two-chain enzyme. By expression in human embryonic kidney 293, esophageal EC9706, and lung epithelial A549 and 16HBE cells, Western blotting, and site-directed mutagenesis, we found that the activation cleavage of human TMPRSS11A was mediated by autocatalysis. Moreover, we found that TMPRSS11A activation cleavage occurred before the protein reached the cell surface, as indicated by studies with trypsin digestion to remove cell surface proteins, treatment with cell organelle-disturbing agents to block intracellular protein trafficking, and analysis of a soluble form of TMPRSS11A without the transmembrane domain. We also showed that TMPRSS11A was able to cleave the SARS-CoV-2 spike protein. These results reveal an intracellular autocleavage mechanism in TMPRSS11A zymogen activation, which differs from the extracellular zymogen activation reported in other TTSPs. These findings provide new insights into the diverse mechanisms in regulating TTSP activation.


Subject(s)
Epithelial Cells/metabolism , Membrane Proteins/metabolism , Proteolysis , Serine Proteases/metabolism , A549 Cells , Cells, Cultured , HEK293 Cells , Humans , Membrane Proteins/chemistry , Membrane Proteins/genetics , Mutation , Protein Domains , Protein Transport , Respiratory Mucosa/cytology , Serine Proteases/chemistry , Serine Proteases/genetics , Spike Glycoprotein, Coronavirus/metabolism , Trypsin/metabolism
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