NDLI: Proteolytic maturation of protein C upon engineering the mouse mammary gland to express furin.

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Proteolytic maturation of protein C upon engineering the mouse mammary gland to express furin.

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Proteolytic maturation of protein C upon engineering the mouse mammary gland to express furin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Drews, R. Drohan, W. N. Paleyanda, R. K. Chang, R. R. Kaufman, R. J. Lubon, H. Rehemtulla, A. Lee, T. K.
Description	Author Affiliation: Drews R ( Holland Laboratory, American Red Cross, Rockville, MD 20855, USA.);
Abstract	Endoproteolytic processing of the human protein C (HPC) precursor to its mature form involves cleavage of the propeptide after amino acids Lys-2-Arg-1 and removal of a Lys156-Arg157 dipeptide connecting the light and heavy chains. This processing was inefficient in the mammary gland of transgenic mice and pigs. We hypothesized that the protein processing capacity of specific animal organs may be improved by the coexpression of selected processing enzymes. We tested this by targeting expression of the human proprotein processing enzyme, named paired basic amino acid cleaving enzyme (PACE)/furin, or an enzymatically inactive mutant, PACEM, to the mouse mammary gland. In contrast to mice expressing HPC alone, or to HPC/PACEM bigenic mice, coexpression of PACE with HPC resulted in efficient conversion of the precursor to mature protein, with cleavage at the appropriate sites. These results suggest the involvement of PACE in the processing of HPC in vivo and represent an example of the engineering of animal organs into bioreactors with enhanced protein processing capacity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Mammary Glands, Animal Metabolism Membrane Proteins Protein C Protein Processing, Post-Translational Subtilisins Amino Acid Sequence Animals Furin Mice Mice, Transgenic Chemistry Milk Proteins Molecular Sequence Data Genetics Protein Engineering Protein Precursors Recombinant Proteins Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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