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. Author manuscript; available in PMC: 2009 Dec 1.
Published in final edited form as: Cell Metab. 2008 Oct 30;8(6):502–511. doi: 10.1016/j.cmet.2008.09.012

Figure 7. Model of matriptase-2 activity on BMP-HJV-hepcidin pathway.

Figure 7

(A) Schematic representation of a model of matriptase-2 activity in iron deficiency. On the left, the serine protease cleaves m-HJV releasing soluble fragments (here simplified by the black boxes). The cleavage sites of matriptase-2 are unknown. The question mark indicates uncertainty on fragments function. The resulting hepcidin inhibition is shown. The complementary effect of s-HJV, produced by furin cleavage, to sequester BMP is shown on the right. (B) Lack of hepcidin inhibition in the presence of matriptase-2 mutations. m-HJV acts as BMP coreceptor and permits hepcidin production in iron deficiency; the effect of s-HJV cannot downregulate hepcidin in the presence of m-HJV.