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The secretory proprotein convertases furin, PC5, and PC7 activate VEGF-C to induce tumorigenesis
Geraldine Siegfried, Ajoy Basak, James A. Cromlish, Suzanne Benjannet, Jadwiga Marcinkiewicz, Michel Chrétien, Nabil G. Seidah, Abdel-Majid Khatib
Published in Volume 111, Issue 11
J Clin Invest. 2003; 111(11):1723–1732 doi:10.1172/JCI17220
This article Copyright © 2003, The American Society for Clinical Investigation
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Figure 2

In vitro digestions of Q-h-VEGF-C with recombinant furin, PC5, and PC7. (a) RP-HPLC chromatogram of the crude digest following 4 hours of incubation at 37°C of 20 μg of QVEGF-C with furin, PC5, or PC7 in 25 mM Tris, 25 mM Mes, and 2.5 mM CaCl2, pH 7.4. The elution of the peaks was monitored on-line by UV absorbance at 214 nm as well as by fluorescence detectors (λex, 320 nm; λem, 420 nm). (b) MALDI-ToF mass spectra of the crude digests following 24 hours of incubation at 37°C of 20 μg of QVEGF-C with furin, PC5, and PC7 in 25 mM Tris, 25 mM Mes, and 2.5 mM CaCl2, pH 7.4. Note the absence of the peak at m/z 1,703 suggesting complete cleavage of QVEGF-C. The peaks at m/z 1,129 and 595 were attributed to the highly fluorescent N-terminal (NT) (Abz-Q-VHSIIRR-OH) and the nonfluorescent C-terminal (CT) [SLP(NO2)-A-CONH2] fragments, respectively. The peaks at m/z 972 and 663 are not PC-dependent since they are also present in the crude digest of QVEGF-C by wild-type medium (data not shown). NT-R, the N-terminal sequence without Arginine residue.

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