Biochem Biophys Res Commun. 1993 Sep 15;195(2):1019-26.

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

Takahashi S, Kasai K, Hatsuzawa K, Kitamura N, Misumi Y, Ikehara Y, Murakami K, Nakayama K.

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Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.

Abstract

Furin has been proposed to be the endoprotease responsible for precursor cleavage at Arg-X-Lys/Arg-Arg (RXK/RR) sites within the constitutive secretory pathway. However, there was a possibility that other protease(s) is involved in this cleavage. We here characterized furin in human colon carcinoma LoVo cells, since these cells lacked the endogenous processing activity toward RXK/RR sites and recovered the activity by transfection of furin cDNA. Furin cDNA cloned from LoVo cells had one nucleotide deletion in the region covering the homo B domain which is essential for the endoproteolytic activity. LoVo cells transfected with a furin construct with the mutation showed no activity. Based on these data, we conclude that furin is the endoprotease that is involved in the precursor cleavage at RXK/RR sites within the constitutive secretory pathway.

PMID:: 7690548; [PubMed - indexed for MEDLINE]

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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. [J Biol Chem. 1995]
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A mutation of furin causes the lack of precursor-processing activity in human co...
A mutation of furin causes the lack of precursor-processing activity in human colon carcinoma LoVo cells.
Biochem Biophys Res Commun. 1993 Sep 15 ;195(2):1019-26.

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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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