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    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.

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

    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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