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Updated: Aug 15, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
Published on: June 23, 2022
[Lysosomal carboxypeptidase A]
Marek Gacko1, Anna Worowska, Arkadiusz Woźniak
1Department of Vascular Surgery and Transplantation, Medical University of Białystok, 24a M. Skłodowska-Curie St., 15-269 Białystok, Poland. chirnacz@amb.edu.pl
Abstract:
Lysosomal carboxypeptidase A (cathepsin A) is synthetized in the form of preproenzyme, which undergoes to active enzyme as a result of post-translational modification. It splits off C-terminal amino acid residues from peptides and proteins and synergizes with other proteases in degradation of cellular proteins in lysosomes. Lysosomal carboxypeptidase A has an effect on peptide hormones and peptides of biological activity of tissues and body fluids as well. It forms complexes with some glycosidases that protects them against proteolytic degradation. Deficiency of this enzyme induces storage diseases. Lysosomal carboxypeptidase A as multifunctional enzyme plays an important regulatory role in organismal metabolism.
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