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Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Aging+(Albany+NY) 2019 ; 11 (13): 4354-4366 Nephropedia Template TP
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Ammonia induces calpain-dependent cleavage of CRMP-2 during neurite degeneration in primary cultured neurons #MMPMID31278888
Cai Z; Zhu X; Zhang G; Wu F; Lin H; Tan M
Aging (Albany NY) 2019[Jul]; 11 (13): 4354-4366 PMID31278888show ga
Hyperammonemia in the CNS induces irreversible damages to neurons due to ultimate cell loss. Neurite degeneration, a primary event that leads to neuronal cell death, remains less elucidated especially in hyperammonemia circumstances. Here, we found that the administration of ammonia induced neurite degeneration in cultured cerebellar granule neurons. The resulting altered neuronal morphology, rupture of neurites, and disassembly of the cytoskeleton led to cell death. Calcein and Fluo-4 staining revealed that ammonia induced intracellular calcium dysregulation. Subsequently activated calpain cleaved CRMP-2, a microtubule assembly protein. Pharmacologically inhibition of calpain, but not caspases or GSK-3, suppressed the cleavage of CRMP-2 and reversed neurite degeneration under ammonia treatment. Exposure to ammonia decreased whereas inhibition of calpain restored the amplitude and frequency of miniature excitatory postsynaptic currents. These data suggest a mechanism by which elevated ammonia level may induce neuronal dysfunction via abnormal calcium influx and calpain-dependent CRMP-2 cleavage, leading to abnormal synaptic transmission, cytoskeletal collapse, and neurite degeneration.
|Ammonia/*toxicity[MESH]
|Animals[MESH]
|Calcium/metabolism[MESH]
|Calpain/*metabolism[MESH]
|Hyperammonemia/*metabolism[MESH]
|Intercellular Signaling Peptides and Proteins/*metabolism[MESH]