Endoprotease activities other than furin and PACE4 with a role in processing of HIV-I gp160 glycoproteins in CHO-K1 cells (Q28301298)

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J F Sucic

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J M Moehring

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M J Spence

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T J Moehring

Journal of Biological Chemistry

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language of work or name

English

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publication date

10 January 1997

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published in

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volume

272

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page(s)

1344-8

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issue

2

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cites work

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Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus

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Identification of a Second Human Subtilisin-Like Protease Gene in thefes/fpsRegion of Chromosome 15

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cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases

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Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats

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Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarity to PACE4

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Analysis of mutations in alleles of the fur gene from an endoprotease-deficient Chinese hamster ovary cell strain.

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The low-density-lipoprotein receptor-related protein (LRP) is processed by furin in vivo and in vitro.

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Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160

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PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE

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Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1

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A second mutant allele of furin in the processing-incompetent cell line, LoVo. Evidence for involvement of the homo B domain in autocatalytic activation.

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A mutation of furin causes the lack of precursor-processing activity in human colon carcinoma LoVo cells

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Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160.

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Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4

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