lafora disease/carbohydrate

Lafora disease (progressive myoclonus epilepsy of Lafora type) is an autosomal recessive neurodegenerative disorder resulting from defects in the EPM2A gene. EPM2A encodes a 331-amino acid protein containing a carboxyl-terminal phosphatase catalytic domain. We demonstrate that the EPM2A gene product

The progressive myoclonus epilepsy of Lafora disease (LD) is a fatal form of neurodegenerative disorder associated with progressive intellectual decline and ataxia in addition to epilepsy. The disease can be caused by defects in the EPM2A gene encoding laforin phosphatase or the NHLRC1 gene encoding

Lafora's disease (LD) is an autosomal recessive and fatal form of epilepsy with onset in late childhood or adolescence. One of the characteristic features of LD pathology is the presence of periodic acid-Schiff (PAS) positive Lafora inclusion bodies. Lafora bodies are present primarily in neurons,

Lafora bodies are described in the retina of a 16 year old female who died five years after the onset of a typical familial progressive myoclonus epilepsy which was diagnosed as Lafora disease by brain biopsy and by autopsy findings. The patient was the offspring of consanguinous parents who had

Lafora disease in man is an autosomal recessive defect which affects carbohydrate metabolism and results in a progressive, ultimately fatal neurological condition. It is characterized histologically by intraneuronal cytoplasmic polyglucosan inclusions (Lafora bodies). Similar inclusions have been

Lafora disease (LD) is a fatal autosomal recessive form of progressive myoclonus epilepsy. Patients manifest myoclonus and tonic-clonic seizures, visual hallucinations, intellectual, and progressive neurologic deterioration beginning in adolescence. The two genes known to be involved in Lafora

Lafora disease is a progressive myoclonus epilepsy with an early fatal issue. Two genes were identified thus far, the mutations of which cause the disease. The first one, EPM2A, encodes the consensus sequence of a protein tyrosine phosphatase. Its product, laforin, is the object of the present work.

Laforin is a human dual-specificity phosphatase (DSP) involved in glycogen metabolism regulation containing a carbohydrate-binding module (CBM). Mutations in the gene coding for laforin are responsible for the development of Lafora disease, a progressive fatal myoclonus epilepsy with early onset,

Lafora disease (LD) is an autosomal recessive, progressive form of myoclonus epilepsy which affects worldwide. LD occurs mainly in countries like southern Europe, northern Africa, South India, and in the Middle East. LD occurs with its onset mainly in teenagers and leads to decline and death within

Lafora disease is an autosomal recessive and progressive degenerative disorder of the central nervous system (CNS). The pathogenic mechanism has been presumed to be an inborn error of carbohydrate metabolism, although this has never been proved. In a case of proven Lafora disease, pyruvate

Lafora disease is an inborn error of carbohydrate metabolism with storage of a polyglucosan in various tissues including brain and liver. Recently, distinctive histopathological changes in liver have been emphasized, and the diagnosis has been confirmed by the relatively simple procedure of

Lafora Disease (LD) is a fatal neurodegenerative epileptic disorder that presents as a neurological deterioration with the accumulation of insoluble, intracellular, hyperphosphorylated carbohydrates called Lafora bodies (LBs). LD is caused by mutations in either the gene encoding laforin or malin.

Progressive Myoclonus Epilepsy (PME) of the Lafora type is an autosomal recessive disease, which presents in teenage years with myoclonia and generalized seizures leading to death within a decade of onset. It is characterized by pathognomonic inclusions, Lafora bodies (LB), in neurons and other cell

Lafora disease (LD) is a progressive myoclonic epilepsy resulting in severe neurodegeneration followed by death. A hallmark of LD is the accumulation of insoluble polyglucosans called Lafora bodies (LBs). LD is caused by mutations in the gene encoding the phosphatase laforin, which reportedly exists

Laforin is the only phosphatase in the animal kingdom that contains a carbohydrate-binding module. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder, which is diagnosed by the presence of intracellular deposits of insoluble