Maturation and degradation of beta-galactosidase in the post-Golgi compartment are regulated by cathepsin B and a non-cysteine protease.

Abstract:

:Lysosomal beta-galactosidase precursor is processed to a mature form and associated with protective protein in lysosomes. In this study we used two cysteine protease proinhibitors, E64-d for cathepsins B, S, H, and L, and CA074Me for cathepsin B. They are converted intracellularly to active forms, E-64c and CA074, respectively. Both active compounds inhibited maturation of the exogenous beta-galactosidase precursor, but E-64c did not inhibit further degradation to an inactive 50-kDa product. We concluded that cathepsin B participated exclusively in maturation of beta-galactosidase, and a non-cysteine protease was involved in further degradation and inactivation of the enzyme molecule.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Okamura-Oho Y,Zhang S,Callahan JW,Murata M,Oshima A,Suzuki Y

doi

10.1016/s0014-5793(97)01461-0

subject

Has Abstract

pub_date

1997-12-15 00:00:00

pages

231-4

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)01461-0

journal_volume

419

pub_type

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