Role of Sialidase in Long-Term Potentiation at Mossy Fiber-CA3 Synapses and Hippocampus-Dependent Spatial Memory

Minami, Akira; Saito, Masakazu; Mamada, Shou; Ieno, Daisuke; Hikita, Tomoya; Takahashi, Toshifumi; Otsubo, Tadamune; Ikeda, Kiyoshi; Suzuki, Takashi

doi:10.1371/journal.pone.0165257

Cited by 26 publications

(34 citation statements)

References 47 publications

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“…Minami et al . developed a highly sensitive histochemical imaging probe for sialidase activity, BTP3-Neu5Ac, which is cleaved by all 4 neuraminidases and demonstrated that, at neutral pH, the probe stained mossy fiber terminal fields in rat hippocampal acute slices [ 100 ]. The authors further showed that neuraminidase inhibitor DANA significantly impaired LTP at mossy fiber-CA3 pyramidal cell synapse.…”

Section: Rapid Changes In Cerebral Neuraminidase Activity Associated mentioning

confidence: 99%

Keeping it trim: roles of neuraminidases in CNS function

Pshezhetsky

Ashmarina

2018

Glycoconj J

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The sialylated glyconjugates (SGC) are found in abundance on the surface of brain cells, where they form a dense array of glycans mediating cell/cell and cell/protein recognition in numerous physiological and pathological processes. Metabolic genetic blocks in processing and catabolism of SGC result in development of severe storage disorders, dominated by CNS involvement including marked neuroinflammation and neurodegeneration, the pathophysiological mechanisms of which are still discussed. SGC patterns in the brain are cell and organelle-specific, dynamic and maintained by highly coordinated processes of their biosynthesis, trafficking, processing and catabolism. The changes in the composition of SGC during development and aging of the brain cannot be explained based solely on the regulation of the SGC-synthesizing enzymes, sialyltransferases, suggesting that neuraminidases (sialidases) hydrolysing the removal of terminal sialic acid residues also play an essential role. In the current review we summarize the roles of three mammalian neuraminidases: neuraminidase 1, neuraminidase 3 and neuraminidase 4 in processing brain SGC. Emerging data demonstrate that these enzymes with different, yet overlapping expression patterns, intracellular localization and substrate specificity play essential roles in the physiology of the CNS.

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Section: Rapid Changes In Cerebral Neuraminidase Activity Associated mentioning

confidence: 99%

Keeping it trim: roles of neuraminidases in CNS function

Pshezhetsky

Ashmarina

2018

Glycoconj J

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“…Measurements of sialidase activity. Sialidase activity was measured according to the procedure described previously 7,41 . Briefly, INS-1D cells or C6 rat glioma cells stably expressing the rat sialidase isozyme Neu3 were lysed in n-octyl-β-D -glucoside buffer.…”

Section: Methodsmentioning

confidence: 99%

The sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid is a glucose-dependent potentiator of insulin secretion

Minami

Fujita

Shimba

et al. 2020

Sci Rep

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Sialidase cleaves sialic acid residues from a sialoglycoconjugate: oligosaccharides, glycolipids and glycoproteins that contain sialic acid. Histochemical imaging of the mouse pancreas using a benzothiazolylphenol-based sialic acid derivative (BTP3-Neu5Ac), a highly sensitive histochemical imaging probe used to assess sialidase activity, showed that pancreatic islets have intense sialidase activity. The sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid (DANA) remarkably enhances glutamate release from hippocampal neurons. Since there are many similar processes between synaptic vesicle exocytosis and secretory granule exocytosis, we investigated the effect of DANA on insulin release from β-cells. Insulin release was induced in INS-1D cells by treatment with 8.3 mM glucose, and the release was enhanced by treatment with DANA. In a mouse intraperitoneal glucose tolerance test, the increase in serum insulin levels was enhanced by intravenous injection with DANA. However, under fasting conditions, insulin release was not enhanced by treatment with DANA. Calcium oscillations induced by 8.3 mM glucose treatment of INS-1D cells were not affected by DANA. Blood insulin levels in sialidase isozyme Neu3-deficient mice were significantly higher than those in WT mice under ad libitum feeding conditions, but the levels were not different under fasting conditions. These results indicate that DANA is a glucose-dependent potentiator of insulin secretion. The sialidase inhibitor may be useful for anti-diabetic treatment with a low risk of hypoglycemia. Sialidase is a hydrolase that removes sialic acid from a sialoglycoconjugate. Mammalian sialidase has four isozymes: Neu1, Neu2, Neu3 and Neu4. These four isozymes have differences in the tissues where they are expressed, their subcellular locations, their substrate specificity and their pH dependency 1. It has been proposed that sialidase contributes to the regulation of insulin signalling and sensitivity. Neu1, a lysosomal sialidase, regulates insulin signalling for energy metabolism and glucose uptake 2. Neu3, a plasma membrane-associated sialidase, is associated with tissue-specific insulin sensitivity and glucose tolerance 3-5. Transgenic mice overexpressing Neu3 mainly in muscles developed severe insulin-resistant diabetes mellitus associated with hyperinsulinemia, islet hyperplasia and increased β-cell mass 5. Hepatic Neu3 overexpression, however, improves insulin sensitivity and glucose tolerance and is associated with changes in ganglioside composition and peroxisome proliferator-activated receptor gamma signalling 4. Recently, we reported that sialidase downregulates glutamate release from neurons 6. Since sialidase activity increases rapidly in response to neural excitation, sialidase is thought to play a role in the negative-feedback mechanism for glutamate release 7. In an effort to understand how sialidase might regulate synaptic transmission,

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“…For Neu1, some studies suggested a C-terminal transmembrane domain, whereas other studies excluded a transmembrane region proposing a lipid anchor 75,76 . Subcellular location and activity of sialidases might differ depending on the physiological conditions and the cell types, as demonstrated by the polysialic acid processing by Neu1 77 and the involvement of Neu4 in hippocampal memory processing 78 .…”

Section: Identified Sialidases and Sialyltransferases In Synaptosomesmentioning

confidence: 99%

Synaptic transmission induces site-specific changes in sialylation onN-linked glycoproteins in rat nerve terminals

Boll

Jensen

Schwämmle

et al. 2020

Preprint

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Synaptic transmission leading to release of neurotransmitters in the nervous system is a fast and highly dynamic process. Previously, protein interaction and phosphorylation have been thought to be the main regulators of synaptic transmission. Here we show a novel potential modulator of synaptic transmission, sialylation of N-linked glycosylation. The negatively charged sialic acids can be modulated, similarly to phosphorylation, by the action of sialyltransferases and sialidases thereby changing local structure and function of membrane glycoproteins. We characterized site-specific alteration in sialylation on N-linked glycoproteins in isolated rat nerve terminals after brief depolarization using quantitative sialiomics. We identified 1965 formerly sialylated N-linked glycosites in synaptic proteins and found that the abundances of 430 glycosites changed after five seconds depolarization. We observed changes on essential synaptic proteins such as synaptic vesicle proteins, ion channels and transporters, neurotransmitter receptors and cell adhesion molecules. This study is to our knowledge the first to describe ultra-fast site-specific modulation of the sialiome after brief stimulation of a biological system.

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Role of Sialidase in Long-Term Potentiation at Mossy Fiber-CA3 Synapses and Hippocampus-Dependent Spatial Memory

Cited by 26 publications

References 47 publications

Keeping it trim: roles of neuraminidases in CNS function

Keeping it trim: roles of neuraminidases in CNS function

The sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid is a glucose-dependent potentiator of insulin secretion

Synaptic transmission induces site-specific changes in sialylation onN-linked glycoproteins in rat nerve terminals

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