scholarly journals STUDIES IN MYOCLONUS EPILEPSY III. THE EFFECTS OF AMYLOLYTIC ENZYMES ON THE ULTRASTRUCTURE OF LAFORA BODIES

1971 ◽  
Vol 19 (6) ◽  
pp. 382-385 ◽  
Author(s):  
TORU NIKAIDO ◽  
JAMES AUSTIN ◽  
HANS STUKENBROK
Keyword(s):  
Staining Intensity ◽  
Ultrastructural Changes ◽  
Corpora Amylacea ◽  
Amylolytic Enzymes ◽  
Lafora Bodies ◽  
Myoclonus Epilepsy

Sections containing Lafora bodies were exposed to the action of amylolytic enzymes. These enzymes split the glucose linkages of glucose polymers (polyglucosans). The following ultrastructural changes were observed: ( a) the fibrils of Lafora bodies were greatly reduced in number; ( b) the staining intensity of the fibrils was reduced; ( c) the amorphous densities were no longer seen. The evidence suggests that the fibrils and amorphous densities of Lafora bodies are both polyglucosan in nature. Lafora bodies resemble corpora amylacea in this respect.

scholarly journals Gys1 antisense therapy rescues neuropathological bases of murine Lafora disease

2021 ◽  
Author(s):  
Saija Ahonen ◽  
Silvia Nitschke ◽  
Tamar R. Grossman ◽  
Holly Kordasiewicz ◽  
Peixiang Wang ◽  
...  
Keyword(s):  
Antisense Oligonucleotide ◽  
Glycogen Synthase ◽  
Lafora Disease ◽  
Neuroinflammatory Response ◽  
Glycogen Accumulation ◽  
Body Formation ◽  
Lafora Bodies ◽  
Progressive Myoclonus Epilepsy ◽  
Myoclonus Epilepsy ◽  
Lafora Body

AbstractLafora disease is a fatal progressive myoclonus epilepsy. At root, it is due to constant acquisition of branches that are too long in a subgroup of glycogen molecules, leading them to precipitate and accumulate into Lafora bodies, which drive a neuroinflammatory response and neurodegeneration. As a potential therapy, we aimed to downregulate glycogen synthase, the enzyme responsible for glycogen branch elongation, in the disease’s mouse models. We synthesized an antisense oligonucleotide (Gys1-ASO) that targets the mRNA of the brain-expressed glycogen synthase 1 gene (Gys1). We administered Gys1-ASO by intracerebroventricular injection and analyzed the pathological hallmarks of Lafora disease, namely glycogen accumulation, Lafora body formation, and neuroinflammation. Gys1-ASO prevented Lafora body formation in young mice that had not yet formed them. In older mice that already exhibited Lafora bodies, Gys1-ASO inhibited further accumulation, markedly preventing large Lafora bodies characteristic of advanced disease. Inhibition of Lafora body formation was associated with prevention of astrogliosis and strong trends towards correction of dysregulated expression of disease immune and neuroinflammatory markers. Lafora disease manifests gradually in previously healthy teenagers. Our work provides proof of principle that an antisense oligonucleotide targeting the GYS1 mRNA could prevent, and halt progression of, this catastrophic epilepsy.

Transient Effect of L-Tryptophan in Progressive Myoclonus Epilepsy Without Lafora Bodies: Clinical and Electrophysiological Study

Epilepsia ◽  
1980 ◽  
Vol 21 (4) ◽  
pp. 351-357 ◽  
Author(s):  
Marjaleena Koskiniemi ◽  
Markku Hyyppä ◽  
Kimmo Sainio ◽  
Tapani Salmi ◽  
Seppo Sarna ◽  
...  
Keyword(s):  
Electrophysiological Study ◽  
Transient Effect ◽  
Lafora Bodies ◽  
Progressive Myoclonus Epilepsy ◽  
Myoclonus Epilepsy

scholarly journals Myoclonus epilepsy with cerebellar Lafora bodies: Report of a case

1976 ◽  
Vol 39 (4) ◽  
pp. 357-361 ◽  
Author(s):  
R. Scelsi ◽  
G. L. Mazzella ◽  
M. Lombardi
Keyword(s):  
Lafora Bodies ◽  
Myoclonus Epilepsy
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