A new variant of glycogen storage disease type 1: Probably due to a defect in the glucose-6-phosphate transport system

1979 ◽  
Vol 2 (3) ◽  
pp. 45-49 ◽  
Author(s):  
Y. Igarashi ◽  
H. Otomo ◽  
K. Narisawa ◽  
K. Tada
Keyword(s):  
Transport System ◽  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Glycogen Storage Disease Type ◽  
Phosphate Transport ◽  
Glycogen Storage ◽  
Disease Type ◽  
New Variant

scholarly journals Hypogonadotropic Hypogonadism in Males with Glycogen Storage Disease Type 1

2017 ◽  
pp. 79-84 ◽  
Author(s):  
Evelyn M. Wong ◽  
Anna Lehman ◽  
Philip Acott ◽  
Jane Gillis ◽  
Daniel L. Metzger ◽  
...  
Keyword(s):  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Hypogonadotropic Hypogonadism ◽  
Glycogen Storage Disease Type ◽  
Glycogen Storage ◽  
Disease Type

Inhibition of microsomal glucose-6-phosphate transport in human neutrophils results in apoptosis: a potential explanation for neutrophil dysfunction in glycogen storage disease type 1b

Blood ◽  
2003 ◽  
Vol 101 (6) ◽  
pp. 2381-2387 ◽  
Author(s):  
Rosanna Leuzzi ◽  
Gábor Bánhegyi ◽  
Tamás Kardon ◽  
Paola Marcolongo ◽  
Piero-Leopoldo Capecchi ◽  
...  
Keyword(s):  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Glycogen Storage Disease Type ◽  
Phosphate Transport ◽  
Glycogen Storage ◽  
Disease Type ◽  
Jurkat Cells ◽  
Phosphate Transporter ◽  
Disulfonic Acid ◽  
Human Neutrophils

Mutations in the gene of the hepatic glucose-6-phosphate transporter cause glycogen storage disease type 1b. In this disease, the altered glucose homeostasis and liver functions are accompanied by an impairment of neutrophils/monocytes. However, neither the existence of a microsomal glucose-6-phosphate transport, nor the connection between its defect and cell dysfunction has been demonstrated in neutrophils/monocytes. In this study we have characterized the microsomal glucose-6-phosphate transport of human neutrophils and differentiated HL-60 cells. The transport of glucose-6-phosphate was sensitive to the chlorogenic acid derivative S3483,N-ethylmaleimide, and 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid, known inhibitors of the hepatic microsomal glucose-6-phosphate transporter. A glucose-6-phosphate uptake was also present in microsomes from undifferentiated HL-60 and Jurkat cells, but it was insensitive to S3483. The treatment with S3484 of intact human neutrophils and differentiated HL-60 cells mimicked some leukocyte defects of glycogen storage disease type 1b patients (ie, the drug inhibited phorbol myristate acetate–induced superoxide anion production and reduced the size of endoplasmic reticulum Ca2+ stores). Importantly, the treatment with S3484 also resulted in apoptosis of human neutrophils and differentiated HL-60 cells, while undifferentiated HL-60 and Jurkat cells were unaffected by the drug. The proapoptotic effect of S3483 was prevented by the inhibition of nicotinamide adenine dinucleotide phosphate oxidase or by antioxidant treatment. These results suggest that microsomal glucose-6-phosphate transport has a role in the antioxidant protection of neutrophils, and that the genetic defect of the transporter leads to the impairment of cellular functions and apoptosis.

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