Lysosomes degrade and recycle macromolecules that are delivered through the
biosynthetic, endocytic, and autophagic routes. Hydrolysis of the different classes of …

Lysosomal storage disorders comprise a group of more than 30 different diseases. The
common feature of these diseases is the deficiency of a lysosomal protein that is part of a …

Cathepsin D (EC 3.4. 23.5) is a lysosomal protease suspected to play important roles in
protein catabolism, antigen processing, degenerative diseases, and breast cancer …

The acid sphingomyelinase (ASM) gene, which has been implicated in ceramide-mediated
cell signaling and atherogenesis, gives rise to both lysosomal SMase (L-SMase), which is …

In humans, two major β-hexosaminidase isoenzymes exist: Hex A and Hex B. Hex A is a
heterodimer of subunits α and β (60% identity), whereas Hex B is a homodimer of β …

Two crystal structures are described for the lysosomal aspartic protease cathepsin D (EC
3.4. 23.5). The molecular replacement method was used with X‐ray diffraction data to 3 A …

UDP-N-acetylglucosamine: lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase
(GlcNAc-phosphotransferase) catalyzes the initial step in the synthesis of the mannose 6 …

B lymphocytes from patients with I-cell disease (ICD) maintain normal cellular levels of
lysosomal enzymes despite a deficiency of the enzyme UDP-N-acetylglucosamine …

Most newly synthesized soluble lysosomal proteins contain mannose 6-phosphate (Man-6-
P), a specific carbohydrate modification that is recognized by Man-6-P receptors (MPRs) that …

Human β-glucuronidase (GUS) cleaves β-D-glucuronic acid residues from the non-reducing
termini of glycosaminoglycan and its deficiency leads to mucopolysaccharidosis type VII …