Secretion of human furin into mouse milk.

The Journal of Biological Chemistry
R K PaleyandaH Lubon

Abstract

We have previously described the expression of the human proprotein convertase furin or paired basic amino acid-cleaving enzyme, in mice transgenic for paired basic amino acid-cleaving enzyme and human Protein C (HPC). Here we show 100-fold or higher expression of furin in the mammary gland, compared with endogenous furin. Furin and recombinant HPC were detected in the same regions of the mammary gland and regulated similar to the endogenous whey acidic protein. In addition to the expected intracellular localization, furin was secreted into the milk as an 80-kDa form lacking the transmembrane and cytoplasmic domains. Furin present at levels of up to 40,000 units/ml milk cleaved the t-butoxycarbonyl-RVRR-AMC substrate with a Km of 32 microM, and processed the recombinant HPC precursor at the appropriate sites. Surprisingly, the expression of an active protease was not toxic to the mammary gland. This is a rare example of an animal model secreting active truncated forms of a processing endoprotease into a bodily fluid.

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Citations

Apr 28, 2009·Transgenic Research·Yaroslav GurskyElena Sadchikova
Apr 23, 2003·Experimental Cell Research·Franck PeirettiGilles Nalbone
Jul 20, 2007·Reproduction : the Official Journal of the Society for the Study of Fertility·C FreyerG Nie
Mar 10, 2015·International Journal of Molecular Sciences·Chae-Won ParkKwan-Sik Min
Dec 13, 2006·Anatomia, histologia, embryologia·S DraginP Chrenek
Apr 15, 2006·Brain Pathology·Fiona PickfordEileen McGowan
Jun 2, 2000·Protein Expression and Purification·J B DenaultR Leduc
Dec 28, 2016·Biomedit︠s︡inskai︠a︡ khimii︠a︡·N I SolovyevaE V Kugaevskaya
Apr 26, 2018·Biotechnology Progress·Martin VanderlaanKevin E Van Cott

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