KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D. Jha, S. K., Rauniyar, K., Chronowska, E., Mattonet, K., Maina, E. W., Koistinen, H., Stenman, U., Alitalo, K., & Jeltsch, M. eLife, 8:e44478, May, 2019. ![KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Vascular endothelial growth factor-C (VEGF-C) acts primarily on endothelial cells, but also on non-vascular targets, e.g. in the CNS and immune system. Here we describe a novel, unique VEGF-C form in the human reproductive system produced via cleavage by kallikrein-related peptidase 3 (KLK3), aka prostate-specific antigen (PSA). KLK3 activated VEGF-C specifically and efficiently through cleavage at a novel N-terminal site. We detected VEGF-C in seminal plasma, and sperm liquefaction occurred concurrently with VEGF-C activation, which was enhanced by collagen and calcium binding EGF domains 1 (CCBE1). After plasmin and ADAMTS3, KLK3 is the third protease shown to activate VEGF-C. Since differently activated VEGF-Cs are characterized by successively shorter N-terminal helices, we created an even shorter hypothetical form, which showed preferential binding to VEGFR-3. Using mass spectrometric analysis of the isolated VEGF-C-cleaving activity from human saliva, we identified cathepsin D as a protease that can activate VEGF-C as well as VEGF-D.
@article{jha_klk3/psa_2019,
title = {{KLK3}/{PSA} and cathepsin {D} activate {VEGF}-{C} and {VEGF}-{D}},
volume = {8},
issn = {2050-084X},
url = {https://elifesciences.org/articles/44478},
doi = {10.7554/eLife.44478},
abstract = {Vascular endothelial growth factor-C (VEGF-C) acts primarily on endothelial cells, but also on non-vascular targets, e.g. in the CNS and immune system. Here we describe a novel, unique VEGF-C form in the human reproductive system produced via cleavage by kallikrein-related peptidase 3 (KLK3), aka prostate-specific antigen (PSA). KLK3 activated VEGF-C specifically and efficiently through cleavage at a novel N-terminal site. We detected VEGF-C in seminal plasma, and sperm liquefaction occurred concurrently with VEGF-C activation, which was enhanced by collagen and calcium binding EGF domains 1 (CCBE1). After plasmin and ADAMTS3, KLK3 is the third protease shown to activate VEGF-C. Since differently activated VEGF-Cs are characterized by successively shorter N-terminal helices, we created an even shorter hypothetical form, which showed preferential binding to VEGFR-3. Using mass spectrometric analysis of the isolated VEGF-C-cleaving activity from human saliva, we identified cathepsin D as a protease that can activate VEGF-C as well as VEGF-D.},
language = {en},
urldate = {2019-05-18},
journal = {eLife},
author = {Jha, Sawan Kumar and Rauniyar, Khushbu and Chronowska, Ewa and Mattonet, Kenny and Maina, Eunice Wairimu and Koistinen, Hannu and Stenman, Ulf-Håkan and Alitalo, Kari and Jeltsch, Michael},
month = may,
year = {2019},
pages = {e44478},
}
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