ADAM17-dependent proteolysis of L-selectin promotes early clonal expansion of cytotoxic T cells View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Rebar N. Mohammed, Sophie C. Wehenkel, Elena V. Galkina, Emma-Kate Yates, Graham Preece, Andrew Newman, H. Angharad Watson, Julia Ohme, John S. Bridgeman, Ruban R. P. Durairaj, Owen R. Moon, Kristin Ladell, Kelly L. Miners, Garry Dolton, Linda Troeberg, Masahide Kashiwagi, Gillian Murphy, Hideaki Nagase, David A. Price, R. James Matthews, Vera Knäuper, Ann Ager

ABSTRACT

L-selectin on T-cells is best known as an adhesion molecule that supports recruitment of blood-borne naïve and central memory cells into lymph nodes. Proteolytic shedding of the ectodomain is thought to redirect activated T-cells from lymph nodes to sites of infection. However, we have shown that activated T-cells re-express L-selectin before lymph node egress and use L-selectin to locate to virus-infected tissues. Therefore, we considered other roles for L-selectin proteolysis during T cell activation. In this study, we used T cells expressing cleavable or non-cleavable L-selectin and determined the impact of L-selectin proteolysis on T cell activation in virus-infected mice. We confirm an essential and non-redundant role for ADAM17 in TCR-induced proteolysis of L-selectin in mouse and human T cells and show that L-selectin cleavage does not regulate T cell activation measured by CD69 or TCR internalisation. Following virus infection of mice, L-selectin proteolysis promoted early clonal expansion of cytotoxic T cells resulting in an 8-fold increase over T cells unable to cleave L-selectin. T cells unable to cleave L-selectin showed delayed proliferation in vitro which correlated with lower CD25 expression. Based on these results, we propose that ADAM17-dependent proteolysis of L-selectin should be considered a regulator of T-cell activation at sites of immune activity. More... »

PAGES

5487

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-019-41811-z

DOI

http://dx.doi.org/10.1038/s41598-019-41811-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1113174612

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30940840


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