@article {693,
	title = {KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D},
	journal = {eLife},
	volume = {8},
	year = {2019},
	month = {2019/05/17/},
	pages = {e44478},
	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.},
	keywords = {cancer biology, Cathepsin D, kallikrein-related peptidases, KLK3/PSA, Lymphangiogenesis, mouse, VEGF-C, VEGF-D},
	isbn = {2050-084X},
	url = {https://elifesciences.org/articles/44478},
	author = {Jha, Sawan Kumar and Rauniyar, Khushbu and Chronowska, Ewa and Mattonet, Kenny and Maina, Eunice Wairimu and Koistinen, Hannu and Stenman, Ulf-H{\r a}kan and Alitalo, Kari and Jeltsch, Michael}
}
@article {589,
	title = {Efficient activation of the lymphangiogenic growth factor VEGF-C requires the C-terminal domain of VEGF-C and the N-terminal domain of CCBE1},
	journal = {Scientific Reports},
	volume = {7},
	year = {2017},
	month = {2017/07/07/},
	pages = {4916},
	doi = {10.1038/s41598-017-04982-1},
	url = {https://www.nature.com/articles/s41598-017-04982-1}
}
