anti-Cathepsin A (CTSA) Antikörper

Arabidopsis thaliana Cathepsin A (CTSA) Interaktionspartner

1. Studies indicate the transcript accumulation of the beta-galactosidases (BGAL) genes AtBGAL1 (At3g13750), AtBGAL2 (At3g52840), AtBGAL3 (At4g36360), AtBGAL4 (At5g56870), AtBGAL5 (At1g45130) and AtBGAL12 (At4g26140) along the plant development, as well as their subcellular location by the construction of transgenic plants producing the enhanced green fluorescent protein (eGFP) fused to the six BGAL proteins.

2. It is shown by dot-immunoblotting that At3g52840 is the gene expressing Gal-2 which is associated with the cell wall in Arabidopsis.

Human Cathepsin A (CTSA) Interaktionspartner

1. CTSA expression in the left atrium in mitral regurgitation patients significantly differed from those in aortic valve disease patients and normal controls.

2. The usefulness of modified U1 snRNA for rescue from exon 7 skipping caused by the IVS7 +3a>g mutation of the CTSA gene.

3. The gene signature of OPA1, CTSA, NDUFA1, STK10 and PRDX1 was able to identify patients post-implant with a sensitivity of 91% and a specificity of 86% in discrimination between post-implant group and healthy controls.

4. Galactosialidosis is a rare lysosomal storage disease caused by a combined deficiency of GM1 beta-galactosidase (beta-gal) and neuraminidase secondary to a defect of a lysosomal enzyme protective protein/cathepsin A (PPCA) and mutation in CTSA gene.

5. Case Report: galactosialidosis with novel mutations of CTSA gene diagnosed using placental pathology.

6. We identified compound heterozygous mutations in the CTSA gene, responsible for causing galactosialidosis

7. correct nomenclature of mutations for this gene is discussed; clinical and mutational analyses of 4 cases with rare infantile form of galactosialidosis; identified 3 novel nucleotide changes, 2 resulting in missense mutations and the third, resulting in the p.Gln406* stop codon; complexity of the clinical phenotypes in GS reflects dual functions of PPCA/CTSA

8. Catalytic function, tissue distribution and substrates of cathepsin A are discussed as well as inhibition of cathepsin A as an emerging strategy for the treatment of heart failure.

9. The Cathepsin C releases the glycosidases from complexes formed with cathepsin A, and reinstates their activity.

10. Our data suggest that CatA is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human APC.

11. mutations in early infantile galactosialidosis in two Dutch patients

12. Increased activity of beta-galactosidase in the peritoneal fluid is associated with gynecologic cancers and pelvic inflammatory disease

13. effects of GLB1, PPCA and NEU1 gene mutations on elastogenesis in skin fibroblasts

14. Results describe the hydrodynamic properties of PPCA, NEU1, and a complex of the two proteins and identified multiple binding sites on both proteins.

Mouse (Murine) Cathepsin A (CTSA) Interaktionspartner

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

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

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.

4. characterization of human PPCA, including N-terminal sequencing of the two cleavage products

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

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.

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.

8. Results indicate a novel role for PPCA/cathepsin A in osteoclastogenesis via down-regulation of NF-kappaB p50/p65 activity and suggest a new function for PPCA as an NF-kappaB-degrading enzyme in addition to its known multifunctional properties.

9. Results describe the hydrodynamic properties of PPCA, NEU1, and a complex of the two proteins and identified multiple binding sites on both proteins.

10. 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

Cow (Bovine) Cathepsin A (CTSA) Interaktionspartner

1. PPGB gene is not responsible for the lysosomal storage disease of Japanese Black cattle.