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CTSA encodes a glycoprotein which associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high molecular weight multimers. Additionally we are shipping Cathepsin A Antibodies (126) and Cathepsin A Kits (25) and many more products for this protein.
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Studies indicate the transcript accumulation of the beta-galactosidases (BGAL (show GLB1 Proteins)) 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 (show GLB1 Proteins) proteins.
It is shown by dot-immunoblotting that At3g52840 is the gene expressing Gal-2 (show LGALS2 Proteins) which is associated with the cell wall in Arabidopsis.
The gene signature of OPA1 (show OPA1 Proteins), CTSA, NDUFA1 (show NDUFA1 Proteins), STK10 (show STK10 Proteins) and PRDX1 (show PRDX1 Proteins) 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.
Galactosialidosis is a rare lysosomal storage disease caused by a combined deficiency of GM1 beta-galactosidase (beta-gal (show GLB1 Proteins)) and neuraminidase (show NA Proteins) secondary to a defect of a lysosomal enzyme protective protein/cathepsin A (PPCA) and mutation in CTSA gene.
Case Report: galactosialidosis with novel mutations of CTSA gene diagnosed using placental pathology.
We identified compound heterozygous mutations in the CTSA gene, responsible for causing galactosialidosis
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
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.
The Cathepsin C (show CTSC Proteins) releases the glycosidases from complexes formed with cathepsin A, and reinstates their activity.
Our data suggest that CatA (show CAT Proteins) is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human APC (show APC Proteins).
Increased activity of beta-galactosidase (show GLB1 Proteins) in the peritoneal fluid is associated with gynecologic cancers and pelvic inflammatory disease
effects of GLB1 (show GLB1 Proteins), PPCA and NEU1 (show NEU1 Proteins) gene mutations on elastogenesis in skin fibroblasts
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 (show EDN1 Proteins) that otherwise would accumulate in tissues and consequently contribute to development of the hyper-proliferative corneal dystrophy and abnormal skin thickening
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 (show EDN1 Proteins) regulation of vascular tone and hemodynamics
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.
characterization of human PPCA, including N-terminal sequencing of the two cleavage products
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
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.
CathA acts in vivo as an endothelin-1 (show EDN1 Proteins)-inactivating enzyme and strongly confirm a crucial role of this enzyme in effective elastic fiber formation.
Results indicate a novel role for PPCA/cathepsin A in osteoclastogenesis via down-regulation of NF-kappaB p50 (show NFKB1 Proteins)/p65 (show NFkBP65 Proteins) activity and suggest a new function for PPCA as an NF-kappaB (show NFKB1 Proteins)-degrading enzyme in addition to its known multifunctional properties.
Results describe the hydrodynamic properties of PPCA, NEU1 (show NEURL Proteins), and a complex of the two proteins and identified multiple binding sites on both proteins.
The N-terminal N-glycan of NEU1 (show NEURL Proteins) 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
PPGB gene is not responsible for the lysosomal storage disease of Japanese Black cattle.
This gene encodes a glycoprotein which associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high molecular weight multimers. The formation of this complex provides a protective role for stability and activity. Deficiencies in this gene are linked to multiple forms of galactosialidosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
lysosomal protective protein
, protective protein for beta-galactosidase
, protective protein for beta-galactosidase (galactosialidosis)
, beta-galactosidase 2
, beta-galactosidase protective protein
, carboxypeptidase C
, carboxypeptidase L
, carboxypeptidase Y-like kininase
, lysosomal carboxypeptidase A
, protective protein cathepsin A
, urinary kininase