The identification of α-galactosidase B from human liver as an α-acetylgalactosaminidase

Dean, Kenneth J.; Sung, Sun‐Sang J.; Sweeley, Charles C.

doi:10.1016/s0006-291x(77)80136-8

Cited by 53 publications

(21 citation statements)

References 15 publications

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“…Immunochemical analysis showed no cross-reactivity between the A and B forms (29,34,35). Independently, Dean et al (36) and Schram et al (37) identified a-galactosidase B as an a-N-acetyl-D--galactosaminidase.…”

Section: A Wgalactosidasesmentioning

confidence: 94%

Glycolipid and Glycoprotein Degradation

Conzelmann

Sandhoff

1987

Advances in Enzymology - And Related Areas of Molecular Biology

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Section: A Wgalactosidasesmentioning

confidence: 94%

Glycolipid and Glycoprotein Degradation

Conzelmann

Sandhoff

1987

Advances in Enzymology - And Related Areas of Molecular Biology

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“…a-gal A activity was measured as published. 23 Quantitative analysis revealed significantly increased amount of some proteins with molecular weights about 30 kDa in AFD patients. This finding was then confirmed by software Phoretix 2D expression 2005.…”

Section: Changes In Proteinsmentioning

confidence: 95%

Study of urinary proteomes in Anderson-Fabry disease

et al. 2010

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Background: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient a-galactosidase A activity. The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease. Material and methods: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects. The proteins were separated using isoelectric focusing method followed by SDS-PAGE. The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Results: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa. The concentration of some proteins was more than three times higher in the AFD samples, compared to the controls. The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 D-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III. Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 D-isomerase was detected. Conclusions: AFD urinary proteomics revealed increased secretion of several proteins. We postulate that the observed difference in the amount of prostaglandin H2 D-isomerase and its position on twodimensional gels might be related to different glycosylation in AFD subjects.

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“…The observed relatively high residual activity toward glycolipid B-6-2 was probably contributed by some other enzyme. The most likely candidate is ␣-NAGA, which is known to accept also ␣-galactosides as substrate, albeit with a high K m value (32,33). [The enzyme was indeed initially purified as ␣-galactosidase B (34)].…”

Section: Downloaded Frommentioning

confidence: 99%

Defects in degradation of blood group A and B glycosphingolipids in Schindler and Fabry diseases

Asfaw

Ledvinová

Dobrovolný

et al. 2002

Journal of Lipid Research

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Skin fibroblast cultures from patients with inherited lysosomal enzymopathies, ␣ -N -acetylgalactosaminidase ( ␣ -NAGA) and ␣ -galactosidase A deficiencies (Schindler and Fabry disease, respectively), and from normal controls were used to study in situ degradation of blood group A and B glycosphingolipids. Glycosphingolipids A-6-2 (Gal N AcCer, globotetraosylceramide) were tritium labeled in their ceramide moiety and used as natural substrates. The degradation rate of glycolipid A-6-2 was very low in fibroblasts of all the ␣ -NAGA-deficient patients (less than 7% of controls), despite very heterogeneous clinical pictures, ruling out different residual enzyme activities as an explanation for the clinical heterogeneity. Strongly elevated urinary excretion of blood group A glycolipids was detected in one patient with blood group A, secretor status (five times higher than upper limit of controls), in support of the notion that blood group A-active glycolipids may contribute as storage compounds in blood group A patients. When glycolipid B-6-2 was fed to ␣ -galactosidase A-deficient cells, the degradation rate was surprisingly high (50% of controls), while that of globotriaosylceramide was reduced to less than 15% of control average, presumably reflecting differences in the lysosomal enzymology of polar glycolipids versus less-polar ones.Relatively

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The identification of α-galactosidase B from human liver as an α-acetylgalactosaminidase

Cited by 53 publications

References 15 publications

Glycolipid and Glycoprotein Degradation

Glycolipid and Glycoprotein Degradation

Study of urinary proteomes in Anderson-Fabry disease

Defects in degradation of blood group A and B glycosphingolipids in Schindler and Fabry diseases

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