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Volume 272, Number 24, Issue of June 13, 1997 pp. 15270-15274
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Secretion of Human Furin into Mouse Milk

(Received for publication, March 18, 1997, and in revised form, April 9, 1997)

Rekha K. Paleyanda , Roman Drews , Timothy K. Lee and Henryk Lubo

From the J. Holland Laboratory, American Red Cross, Rockville, Maryland 20855

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 K_m of 32 µM, 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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