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Volume 272, Number 2, Issue of January 10, 1997 pp. 1344-1348
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Endoprotease Activities Other Than Furin and PACE4 with a Role in Processing of HIV-I gp160 Glycoproteins in CHO-K1 Cells

(Received for publication, July 3, 1996, and in revised form, October 24, 1996)

Noel M. Inocencio , Joseph F. Sucic , Joan M. Moehring , Michael J. Spence and Thomas J. Moehring

From the Department of Microbiology and Molecular Genetics, Markey Center for Molecular Genetics, and  Vermont Cancer Center, University of Vermont, Burlington, Vermont 05405

We addressed the question of whether furin is the endoprotease primarily responsible for processing the human immunodeficiency virus type I (HIV-I) envelope protein gp160 in mammalian cells. The furin-deficient Chinese hamster ovary (CHO)-K1 strain RPE.40 processed gp160 as efficiently as wild-type CHO-K1 cells in vivo. Although furin can process gp160 in vitro, this processing is probably not physiologically relevent, because it occurs with very low efficiency. PACE4, a furin homologue, allowed processing of gp160 when both were expressed in RPE.40 cells. Further, PACE4 participated in the activation of a calcium-independent protease activity in RPE.40 cells, which efficiently processed the gp160 precursor in vitro. This calcium-independent protease activity was not found in another furin-deficient cell strain, 7.P15, selected from the monkey kidney cell line COS-7.

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