1. in normal tissues the tandem of serine carboxypeptidases, Scpep1 and CathA likely constitutes an important part of the physiological mechanism responsible for the balanced elimination of heightened levels of ET-1 that otherwise would accumulate in tissues and consequently contribute to development of the hyper-proliferative corneal dystrophy and abnormal skin thickening PMID: 28234994
2. our results define the biological role of mammalian serine carboxypeptidase Scpep1 and suggest that Scpep1 and CathA together participate in the control of ET-1 regulation of vascular tone and hemodynamics PMID: 24586188
3. Loss of the cathepsin A results in the lysosomal storage disease galactosialidosis. However, mice with a catalytically inactive cathepsin A enzyme show no signs of this disease. PMID: 23495688
4. characterization of human PPCA, including N-terminal sequencing of the two cleavage products PMID: 3136930
5. the compromised halo cells, due to PPCA deficiency within their lysosomes, cannot function properly and as a result there is a recruitment of macrophages in the intertubular space PMID: 14579412
6. PPCA deficiency causes structural changes to the blood-epididymal barrier as evidenced by lanthanum nitrate and Cldns expression that affects the luminal environment of the epididymis, resulting in altered sperm motility. PMID: 17522420
7. CathA acts in vivo as an endothelin-1-inactivating enzyme and strongly confirm a crucial role of this enzyme in effective elastic fiber formation. PMID: 18391110
8. Results describe the hydrodynamic properties of PPCA, NEU1, and a complex of the two proteins and identified multiple binding sites on both proteins. PMID: 19666471
9. The N-terminal N-glycan of NEU1 is indispensable for its function, whereas the C-terminal N-glycan appears to be non-essential. The omission of the second N-glycan can be compensated for by upregulating the expression of PPCA PMID: 19714866

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KEGG: mmu:19025

STRING: 10090.ENSMUSP00000017904

UniGene: Mm.359633