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© Research
Publication : FEBS letters

Plasmin cleaves the juxtamembrane domain and releases truncated species of the urokinase receptor (CD87) from human bronchial epithelial cells

Member: Abdelkader Namane
Member: Michel Chignard
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 10 Sep 2004

Beaufort N, Leduc D, Rousselle JC, Namane A, Chignard M, Pidard D

Link to Pubmed [PMID] – 15358545

FEBS Lett. 2004 Sep;574(1-3):89-94

The three-domain (D1D2D3) urokinase receptor (CD87) is highly susceptible to cleavage within the D1-D2 linker sequence, but also within the juxtamembrane region by yet poorly characterized proteinases, allowing the release of D1 and D2D3 species in various (patho)physiological body fluids. Using immunoblot analysis and ELISA applied to a recombinant soluble CD87 and to CD87-expressing epithelial cells, we establish that exogenous or in situ generated plasmin proteolyzes CD87 in the D1-D2 linker and D3 carboxyterminal sequences, producing a major soluble D2D3 species. Mass spectrometry analysis of the fragmentation of CD87-related synthetic peptides, and aminoterminal sequencing of D2D3 reveal Arg83, Arg89, and Arg281 as residues targeted by plasmin within human CD87.