β-Galactosidase Deficiency

Johnson, William G.

doi:10.1016/b978-0-12-410529-4.00034-6

Cited by 4 publications

(1 citation statement)

References 51 publications

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“…GM1 gangliosidosis is a rare, fatal, neurodegenerative genetic disease caused by mutations in the GLB1 gene, resulting in deficiency of β-galactosidase enzyme activity and accumulation of glycoconjugates with a terminal β-galactose, including gangliosides GM1 and GA1, oligosaccharides, glycopeptides, and keratan sulfate. 1 , 2 , 3 GM1 gangliosidosis is estimated to affect 1 in 100,000–200,0000 live births. 2 , 3 , 4 The major clinical signs are progressive motor and cognitive decline, visual defects, and premature death.…”

Section: Introductionmentioning

confidence: 99%

A pentasaccharide for monitoring pharmacodynamic response to gene therapy in GM1 gangliosidosis

Kell¹,

Sidhu²,

Mei³

et al. 2023

eBioMedicine

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Section: Introductionmentioning

confidence: 99%

A pentasaccharide for monitoring pharmacodynamic response to gene therapy in GM1 gangliosidosis

Kell¹,

Sidhu²,

Mei³

et al. 2023

eBioMedicine

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Molecular insights into β-Galactosidase enzyme for its potential application in food industry

Thatikonda,

Battula,

Syed

et al. 2024

Journal of the Indian Chemical Society

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Enzyme-responsive polymersomes ameliorate autophagic failure in a cellular model of GM1 gangliosidosis

Paruchuri

Smith²,

Larsen³

2022

Front. Chem. Eng.

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GM1 gangliosidosis is a lysosomal storage disorder caused by deficiency of β-galactosidase (βgal) and subsequent accumulation of GM1 ganglioside in lysosomes. One of the pathological aspects of GM1 gangliosidosis, and other storage disorders, is impaired autophagy, i.e., a reduced fusion of autophagosomes and lysosomes to degrade cellular waste. Enzyme replacement therapy (ERT) can effectively treat systemic deficiency but is limited by immunogenicity and shortened half-life of intravenously administered enzyme. In this paper, we report a hyaluronic acid-b-polylactic acid (HA-PLA) polymersome delivery system that can achieve an enzyme-responsive and sustained delivery of βgal to promote the cell’s self-healing process of autophagy. HA-PLA polymersomes have an average diameter of 138.0 ± 17.6 nm and encapsulate βgal with an efficiency of 77.7 ± 3.4%. In the presence of model enzyme Hyaluronidase, HA-PLA polymersomes demonstrate a two-fold higher release of encapsulant than without enzyme. We also identified reduced autophagy in a cellular model of GM1 Gangliosidosis (GM1SV3) compared to healthy cells, illustrated using immunofluorescence. Enhanced autophagy was reported in GM1SV3 cells treated with βgal-loaded polymersomes. Most notably, the fusion of lysosomes and autophagosomes in GM1SV3 cells returned to normal levels of healthy cells after 24 h of polymersome treatment. The HA-PLA polymersomes described here can provide a promising delivery system to treat GM1 Gangliosidosis.

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β-Galactosidase Deficiency

Cited by 4 publications

References 51 publications

A pentasaccharide for monitoring pharmacodynamic response to gene therapy in GM1 gangliosidosis

A pentasaccharide for monitoring pharmacodynamic response to gene therapy in GM1 gangliosidosis

Molecular insights into β-Galactosidase enzyme for its potential application in food industry

Enzyme-responsive polymersomes ameliorate autophagic failure in a cellular model of GM1 gangliosidosis

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