ArticleThe Journal of biological chemistry2014
Proteolytic activation of human cathepsin A.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- The pathogenesis of cerebral small vessel disease and vascular cognitive impairment.Physiological reviews · 2025Review
- Novel CTSA Variant Identified in a Thai Family With Late-Infantile Galactosialidosis.Annals of human genetics · 2025Article
- α/β Hydrolases: Toward Unraveling Entangled Classification.Proteins · 2025Article
- Regulation of Human Hydrolases and Its Implications in Pharmacokinetics and Pharmacodynamics.Drug metabolism and disposition: the biological fate of chemicals · 2024Review
- Structure of the immunoregulatory sialidase NEU1.Science advances · 2023Article
- In Silico Structural Analysis of Serine CarboxypeptidaseInternational journal of molecular sciences · 2022Article
- Functional Protein Composition in Femoral Glands of Sand Lizards (Molecules (Basel, Switzerland) · 2022Article
- Article
- Structure of the murine lysosomal multienzyme complex core.Science advances · 2021Article
- Galactosialidosis: preclinical enzyme replacement therapy in a mouse model of the disease, a proof of concept.Molecular therapy. Methods & clinical development · 2021Article
- Cathepsin A knockdown decreases the proliferation and invasion of A549 lung adenocarcinoma cells.Molecular medicine reports · 2020Article
- An In Silico Target Fishing Approach to Identify Novel Ochratoxin A Hydrolyzing Enzyme.Toxins · 2020Article
- Carboxypeptidase Y activity and maintenance is modulated by a large helical structure.FEBS open bio · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Galactosialidosis is a human lysosomal storage disease caused by deficiency in the multifunctional lysosomal protease cathepsin A (also known as protective protein/cathepsin A, PPCA, catA, HPP, and CTSA; EC 3.4.16.5). Previous structural work on the inactive precursor human cathepsin A (zymogen) led to a two-stage model for activation, where proteolysis of a 1.6-kDa excision peptide is followed by a conformational change in a blocking peptide occluding the active site. Here we present evidence for an alternate model of activation of human cathepsin A, needing only cleavage of a 3.3-kDa excision peptide to yield full enzymatic activity, with no conformational change required. We present x-ray crystallographic, mass spectrometric, amino acid sequencing, enzymatic, and cellular data to support the cleavage-only activation model. The results clarify a longstanding question about the mechanism of cathepsin A activation and point to new avenues for the design of mechanism-based inhibitors of the enzyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.