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Jordi Duran
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Duran, J. Role of Astrocytes in Pathophysiology of Lafora Disease. Encyclopedia. Available online: https://encyclopedia.pub/entry/42475 (accessed on 19 July 2025).
Duran J. Role of Astrocytes in Pathophysiology of Lafora Disease. Encyclopedia. Available at: https://encyclopedia.pub/entry/42475. Accessed July 19, 2025.
Duran, Jordi. "Role of Astrocytes in Pathophysiology of Lafora Disease" Encyclopedia, https://encyclopedia.pub/entry/42475 (accessed July 19, 2025).
Duran, J. (2023, March 23). Role of Astrocytes in Pathophysiology of Lafora Disease. In Encyclopedia. https://encyclopedia.pub/entry/42475
Duran, Jordi. "Role of Astrocytes in Pathophysiology of Lafora Disease." Encyclopedia. Web. 23 March, 2023.
Role of Astrocytes in Pathophysiology of Lafora Disease
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This entry is adapted from the peer-reviewed paper 10.3390/cells12050722

Lafora disease Lafora disease (LD) is a rare disorder caused by loss of function mutations in either the EPM2A or NHLRC1 gene. The initial symptoms of this condition are most commonly epileptic seizures, but the disease progresses rapidly with dementia, neuropsychiatric symptoms, and cognitive deterioration and has a fatal outcome within 5–10 years after onset. The hallmark of the disease is the accumulation of poorly branched glycogen in the form of aggregates known as Lafora bodies in the brain and other tissues. The astrocytic glycogen accumulation drives the neuroinflammatory phenotype of LD but not the increased susceptibility to epilepsy, which might be attributable to neuronal lafora bodies (LBs).

Lafora disease Astrocytes i glycogen

1. Lafora Disease

Despite the key physiological role of glycogen, this polysaccharide can also participate in brain pathology. In some conditions, glycogen abnormally accumulates in the nervous tissue. Lafora disease (LD, OMIM 254780) is probably the most striking example of the consequences of the abnormal buildup of glycogen in the brain. In LD, poorly branched glycogen accumulates in the brain and other tissues in the form of aggregates known as Lafora bodies (LBs). Glycogen in LBs is not accessible to glycogen phosphorylase and glycogen debranching enzyme. Thus, it cannot be degraded and progressively accumulates. Glycogen in LBs also contains high levels of covalently bound phosphate, which had been hypothesized to participate in glycogen insolubility in LD [1]. However, it seems now clear that abnormal glycogen branching, not hyperphosphorylation, underlies glycogen insolubility in LD [2][3]. In addition to poorly branched, hyperphosphorylated glycogen, LBs contain several proteins, including GS, ubiquitin, and the autophagy adaptor p62 [4][5][6][7].
The onset of LD occurs in adolescence, in previously healthy children, normally in the form of epileptic seizures that are difficult to distinguish from idiopathic generalized epilepsies. Seizures escalate over time, together with a rapid decline in cognitive function. The patient develops severe dementia and eventually enters a vegetative state with continuous seizures. Death invariably comes 5 to 10 years after the onset as a consequence of status epilepticus or complications derived from neurodegeneration [8][9][10]. LD is a rare disease with an estimated prevalence of ~4 cases per million individuals in the world [8]. However, the number of undiagnosed cases might be higher, particularly in developing countries. Current treatment remains palliative, with limited success in the modulation of symptoms.
LD is an autosomal recessive disease caused by mutations in two genes: EPM2A, encoding laforin, a dual phosphatase that contains a carbohydrate-binding domain [11][12], and EPM2B/NHLRC1, encoding malin, an E3-ubiquitin ligase [13]. Mutations in either of these genes cause an indistinguishable disease. The exact roles of malin and laforin in glycogen metabolism are not yet fully understood, but it is widely accepted that malin uses laforin as a scaffold to bind to glycogen and ubiquitinate proteins involved in glycogen metabolism [14][15][16]. The accumulation of poorly branched glycogen in LD suggests that malin and laforin form this functional complex to regulate glycogen synthesis and prevent glycogen insolubility [17]. To minimize the toxic consequences of the accumulation of poorly branched glycogen, proteins like the autophagy adaptor p62 promote its compaction in the form of LBs [6] (Figure 1). This protective mechanism is reminiscent of the condensation of ubiquitinated, misfolded proteins into larger structures to be degraded by autophagy [18][19][20].
/media/item_content/202303/641d1cb50c6ffcells-12-00722-g001.png
Figure 1. Brain glycogen metabolism in normal conditions and in LD. In normal conditions, malin and laforin prevent the accumulation of poorly branched glycogen that is generated as a side product of glycogen metabolism. In LD, due to the absence of malin or laforin, poorly branched glycogen accumulates in astrocytes and neurons. Proteins like the autophagy adaptor p62 promote its aggregation in the form of LBs to minimize the toxic consequences of its accumulation.
The role of LBs in the pathophysiology of LD has been unclear for many years. For instance, it was hypothesized that the primary cause of LD was an impairment in autophagy and that the accumulation of LBs was a consequence of this defect [21][22][23][24]. However, several groups, including ours, took advantage of mouse models of LD to demonstrate that excess glycogen underlies the pathology of this disease. Indeed, impeding or reducing glycogen synthesis in malin- or laforin-deficient mice prevents LB formation and prevents all the pathologic traits of the disease [4][25][26][27]. These models also showed that autophagy impairment is secondary to LB accumulation since autophagy markers are also normalized when glycogen accumulation is prevented [4][28]. 

2. Lafora Bodies in Neurons and Astrocytes

In the first description of LD in 1911, Dr. Gonzalo Rodriguez-Lafora reported the presence of LBs in neurons [29]. Until recently, it was widely believed that LBs accumulated exclusively in this cell type, and thus, all the pathologic traits of the disease were attributed to the toxic effects of neuronal LBs [8][30][31][32]. However, the premise that LBs are present exclusively in this cell population was inconsistent with the fact that, as mentioned before, brain glycogen is present mainly in astrocytes in normal conditions. It is now clear that LBs also accumulate in astrocytes. In 2011, scholars reported the presence of LBs in these cells in a malin-deficient mouse model [33], but the significance of this discovery was underestimated. Several years later, scholars [34][35] demonstrated that most LBs are present in astrocytes, particularly in regions like the hippocampus. Scholars classified these bodies into neuronal (nLBs), and Corpora amylacea-like (CAL), the latter present in astrocytes, which were named this way because of their resemblance to Corpora amylacea, which are glycogen aggregates that accumulate in aged brains [36] (see below). Interestingly, CAL and nLBs differ not only in the cell type in which they accumulate but also in their shape and subcellular localization. CAL are polymorphic and present predominantly in astrocytic processes, and they show a patchy distribution, each patch corresponding to an individual astrocyte. In contrast, nLBs are normally present in the form of a single spherical aggregate close to the neuronal nucleus, and they resemble inclusion bodies formed by protein aggregates such as Lewy bodies [37]. The progressive accumulation of CAL and nLBs takes place in parallel, and both types of LB are already present at early stages in mouse models of LD [5][35].
Astrocytes have been shown to have phagocytic activity and can engulf apoptotic cells [38]. Thus, LBs present in astrocytes might not have originated in astrocytes themselves, but instead, they may have a neuronal origin; i.e., proceeding from the phagocytosis of an apoptotic body derived from a dead neuron. To decipher the origin of astrocytic LBs, as well as to understand their contribution to the pathology of LD, scholars generated a malin-deficient mouse in which GS was specifically deleted from astrocytes (malinKO + GSGfap-KO mice), thus preventing the synthesis of glycogen specifically in this cell type. The brains of these animals contained nLBs but were devoid of CAL, thereby unequivocally demonstrating that the latter originate in astrocytes [28] (Figure 2).
/media/item_content/202303/641d1ccd573e3cells-12-00722-g002.png
Figure 2. Accumulation of glycogen aggregates in neurons and astrocytes and neuroinflammation in mouse models of LD. GS, glial fibrillary acidic protein (Gfap) and ionized calcium-binding adapter molecule 1 (Iba1) immunostainings of mouse hippocampi are shown. GS immunostaining reveals the presence of few CAL aggregates in control mice. In contrast, the hippocampi of malinKO mice show a conspicuous accumulation of CAL and nLBs, while the hippocampi of malinKO + GSGfap-KO mice only show nLBs (although not illustrated in this summary figure, the cell types containing the aggregates have been identified in several studies by using co-staining with cell-specific markers; e.g., see [33][34][35][36]). Gfap and Iba1 immunostainings, markers of astroglia and microglia, respectively, show a prominent neuroinflammation in the brains of malinKO mice that is not present in malinKO + GSGfap-KO brains. Arrows: CAL, arrowheads: nLBs. Scale bar: 500 μm.

3. Role of Astrocytic LBs in the Pathophysiology of LD

The demonstration that LBs are also present in astrocytes opened up the possibility that these astrocytic LBs contribute to the pathology of LD. In fact, the quantification of CAL and nLBs showed that in brain regions like the hippocampus, CAL are clearly predominant over nLBs [34][35]. The analysis of malinKO+GSGfap-KO brains confirmed this quantification since the hippocampi of these mice are largely free of LBs [28] (Figure 2). Furthermore, RNA-Seq studies indicated that most of the upregulated genes in the brains of malin- and laforin-deficient mice encode pro-inflammatory mediators and that reactive glia, including astrocytes, are responsible for the expression of these inflammatory genes [39].

The initial symptom of LD is most commonly the presence of epileptic seizures, which worsen progressively with age. Animal models of LD reproduce this pathologic trait of the disease in the form of increased susceptibility to epileptogenic drugs like kainic acid. Astrocytes play essential roles in brain function, including the regulation of extracellular potassium and glutamate homeostasis, thus making them crucial actors in epilepsy [40]. In this regard, astrocytic glycogen has been shown to fuel potassium uptake into astrocytes, since the astrocytic sodium/potassium pump uses ATP obtained from glucose 6-phosphate originating from glycogen breakdown [41][42]. The non-clearance of extracellular potassium would result in neuronal hypersynchronization and burst firing, which would result in seizure generation and propagation. Thus, it has been suggested that alterations in glycogen metabolism contribute to the imbalance of glutamatergic and GABAergic neurotransmission associated with epileptic seizures [43]. Accordingly, it was reasonable to hypothesize that the impairment of astrocytic glycogen metabolism in LD compromises potassium uptake, which would increase excitability and thus be responsible for the epileptic phenotype of the disease. In line with this hypothesis, the presence of glycogen aggregates in astrocytes has also been described in patients with temporal lobe epilepsy [44]. Surprisingly, malinKO + GSGfap-KO mice do not show a significant amelioration of susceptibility to epilepsy [28], thereby indicating that astrocytic glycogen accumulation is not the main factor responsible for the epileptic phenotype of LD. Importantly, the deletion of GS specifically in astrocytes does not increase susceptibility to epilepsy per se [45]. Thus, the epileptic phenotype of LD might be attributable to neuronal LBs, most likely to those present in GABAergic interneurons, which would impair their function and generate an imbalance of glutamatergic and GABAergic transmission.
In summary, astrocytic glycogen accumulation drives the neuroinflammatory phenotype of LD but not the increased susceptibility to epilepsy, which might be attributable to neuronal LBs.

References

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