Comparing the alpha-galactosidase A biochemical properties from healthy individuals and Fabry disease patients

Daitx, Vanessa Vitcoski; Mezzalira, J. C.; Moraes, Vitória da Costa; Breier, Ana Carolina; Cé, Jaqueline; Coelho, Janice Carneiro

doi:10.1016/j.cca.2015.03.014

Cited by 4 publications

(2 citation statements)

References 29 publications

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“…The α‐Gal A activity in blood cells lysate was measured using the fluorogenic substrate 4‐methylumbelliferyl‐α‐D‐galactopyranoside, and normalized to the total protein, as described elsewhere (Daitx et al, ). The normal activity in control subjects is ranging from 20 to 60 nmol mg −1 hr −1 in our laboratory.…”

Section: Methodsmentioning

confidence: 99%

Strong increase of leukocyte apha‐galactosidase A activity in two male patients with Fabry disease following oral chaperone therapy

Lamari

Mauhin

Koraichi³

et al. 2019

Molec Gen & Gen Med

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Background Fabry disease (OMIM 301500) is an X‐linked disorder caused by alpha‐galactosidase A (α‐Gal A) deficiency. The administration of a pharmacologic chaperone (migalastat) in Fabry patients with amenable mutations has been reported to improve or stabilize organ damages and reduce lyso‐Gb3 plasma level. An increase of α‐Gal A activity has been observed in vitro in cells expressing amenable GLA mutations when incubated with migalastat. The impact of the drug on α‐Gal A in vivo activity has been poorly studied. Methods We conducted a retrospective analysis of two unrelated male Fabry patients with p.Asn215Ser (p.N215S) variant. Results We report the important increase of α‐Gal A activity in blood leukocytes reaching normal ranges of activity after about 1 year of treatment with migalastat. Cardiac parameters improved or stabilized with the treatment. Conclusion We confirm in vivo the effects of migalastat that have been observed in N215S carriers in vitro. The increase of α‐Gal A activity may be the strongest marker for biochemical efficacy. The normalization of enzyme activity could become the new therapeutic target to achieve.

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Section: Methodsmentioning

confidence: 99%

Strong increase of leukocyte apha‐galactosidase A activity in two male patients with Fabry disease following oral chaperone therapy

Lamari

Mauhin

Koraichi³

et al. 2019

Molec Gen & Gen Med

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“…They catalyze the hydrolysis of α-linked terminal non-reducing galactose residues from galactose oligosaccharides, galactomannans and galactolipids. α-Galactosidases have find various industrial applications such as in su-gar industry to increase the yield of crystallized sugar, in feed industry as an animal feed additive to improve nutritional value, in pulp and paper industry to improve pulp bleaching and also in clinical applications such as for the treatment of Fabry's disease by enzyme replacement therapy and to convert B blood group to O blood group [20][21][22]. α-Galactosidases have been purified from different microbial sources with a number of purification protocols including salting-out, ion-exchange, affinity chromatography etc [23][24][25].…”

Section: Introductionmentioning

confidence: 99%

Three-Phase Partitioning of α-Galactosidase from Aspergillus lentulus: Optimization of System and Characterization of Enzyme

Çamurlu

Bayraktar

Özdemir

et al. 2020

Hacettepe Journal of Biology and Chemistry

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Ü çlü-faz ayırma (TPP) tekniği α-galaktozidazın Aspergillus lentulus'dan tek adımda kısmi saflaştırılması için ilk kez başarıyla kullanıldı. Yüksek aktivite ve saflaştırma katı elde etmek için enzimin ekstraksiyon etkinliğine amonyum sülfat konsantrasyonu, ekstrakt t-butanol oranı ve pH etkisi araştırıldı. Sistemin optimum saflaştırma parametreleri %55(w/v) amonyum sülfat konsantrasyonu, 1:1 (v/v) ham ekstrakt t-butanol oranı ve pH 5.5 olarak belirlendi. Bu optimize TPP sistemi α-galaktosidaz için 5.3 saflaştırma katı ile %178 aktivite verimi oluşturdu. pH 6.5 ve 50°C'de maksimum aktivite gözlendi. α-Galaktozidaz 25-60°C sıcaklık aralığında ve pH 2.6-5.5 aralığında oldukça iyi bir kararlılık gösterdi. KM ve Vmax değerleri sırasıyla 0.365 mM ve 0.093 U olarak belirlendi. Metal iyonları ve şekerler arasında Na 2 CO 3 ve galaktoz enzim aktivitesi üzerinde kuvvetli inhibitor etkisi gösterdi. TPP ile A. lentulus'dan farklı biyokimyasal özelliklere sahip yeni bir α-galaktozidazın elde edilmesi onun çeşitli biyoteknolojik uygulamaları açısından ilgi çekici olacaktır.Anahtar Kelimeler α-galaktozidaz, biyoayırım, üçlü-faz ayırma (TPP), enzim saflaştırma, enzim karakterizasyonu.

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α-Galactosidases

Anisha¹

2017

Current Developments in Biotechnology and Bioengineering

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Comparing the alpha-galactosidase A biochemical properties from healthy individuals and Fabry disease patients

Cited by 4 publications

References 29 publications

Strong increase of leukocyte apha‐galactosidase A activity in two male patients with Fabry disease following oral chaperone therapy

Strong increase of leukocyte apha‐galactosidase A activity in two male patients with Fabry disease following oral chaperone therapy

Three-Phase Partitioning of α-Galactosidase from Aspergillus lentulus: Optimization of System and Characterization of Enzyme

α-Galactosidases

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