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

摘要: The low-density-lipoprotein receptor-related protein (LRP) is a multifunctional receptor involved in the clearance of large number diverse ligands, including proteases, protease-inhibitor complexes and lipoproteins. mature composed 515 kDa 85 subunit generated by proteolytic cleavage from 600 precursor polypeptide trans-Golgi compartment. Proteolytic processing occurs C-terminal to tetrabasic amino acid sequence RHRR, consensus recognition site for endoproteases or convertases. In this study we have identified furin, subtilisin-type protease, be necessary efficient LRP cells. Furin-deficient RPE.40 cells exhibited an impaired endogenous recombinant soluble form containing site. defect could complemented expression furin transfected cDNA cultured purified vitro. maturation did not affect its intracellular transport, correlated with slight but consistent reduction endocytosis LRP-specific ligands. These data suggest that trafficking might required normal activity.