Chapter title |
Boyden Chamber Assay to Study of Cell Migration Induced by Metalloprotease Cleaved-CD95L
|
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Chapter number | 12 |
Book title |
CD95
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6780-3_12 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6778-0, 978-1-4939-6780-3
|
Authors |
Amanda Poissonnier, Patrick Legembre |
Editors |
Patrick Legembre |
Abstract |
CD95 receptor, also called Fas or Apo-1, is a member of the tumor necrosis factor receptors (TNF-R) superfamily (Itoh and Nagata, J Biol Chem 268:10932-10937, 1993). Its cognate ligand, CD95L, is a transmembrane cytokine, which can be cleaved by metalloproteases (Matsuno et al., J Rheumatol 28:22-28, 2001; Vargo-Gogola et al., Arch Biochem Biophys 408:155-161, 2002; Kiaei et al., Exp Neurol 205:74-81, 2007; Schulte et al., Cell Death Differ 14:1040-1049, 2007) releasing a soluble ligand into the bloodstream. Recent work has shown that this metalloprotease-cleaved CD95L (cl-CD95L) is involved in carcinogenesis (Malleter et al., Cancer Res 73:6711-6721, 2013). Cl-CD95L also fuels the inflammatory process in patients affected by systemic lupus erythematosus by promoting the accumulation of activated T lymphocytes in enflamed organs (Tauzin et al., PLoS Biol 9:e1001090, 2011). This chapter aims at describing the methodology used to measure the chemoattractive effect of cl-CD95L on human cancer cells and lymphocytes. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Master | 1 | 20% |
Professor | 1 | 20% |
Student > Ph. D. Student | 1 | 20% |
Student > Bachelor | 1 | 20% |
Unknown | 1 | 20% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 3 | 60% |
Medicine and Dentistry | 1 | 20% |
Unknown | 1 | 20% |