title: Novel Mechanisms of Spinal Cord Plasticity in a Mouse Model of Motoneuron Disease.
abstract: A hopeful spinal cord repairing strategy involves the activation of neural precursor cells. Unfortunately, their ability to generate neurons after injury appears limited. Another process promoting functional recovery is synaptic plasticity. We have previously studied some mechanisms of spinal plasticity involving BDNF, Shh, Notch-1, Numb, and Noggin, by using a mouse model of motoneuron depletion induced by cholera toxin-B saporin. TDP-43 is a nuclear RNA/DNA binding protein involved in amyotrophic lateral sclerosis. Interestingly, TDP-43 could be localized at the synapse and affect synaptic strength. Here, we would like to deepen the investigation of this model of spinal plasticity. After lesion, we observed a glial reaction and an activity-dependent modification of Shh, Noggin, and Numb proteins. By using multivariate regression models, we found that Shh and Noggin could affect motor performance and that these proteins could be associated with both TDP-43 and Numb. Our data suggest that TDP-43 is likely an important regulator of synaptic plasticity, probably in collaboration with other proteins involved in both neurogenesis and synaptic plasticity. Moreover, given the rapidly increasing knowledge about spinal cord plasticity, we believe that further efforts to achieve spinal cord repair by stimulating the intrinsic potential of spinal cord will produce interesting results.
authors.affiliation: Department of Biomedical and Biotechnological Sciences, University of Catania, Via Santa Sofia 64, 95127 Catania, Italy ; IOM Ricerca s.r.l., Via Penninazzo 11, 95029 Viagrande, Italy.
authors.forename: Rosario
authors.initials: R
authors.lastname: Gulino
authors.affiliation: Department of Biomedical and Biotechnological Sciences, University of Catania, Via Santa Sofia 64, 95127 Catania, Italy.
authors.forename: Rosalba
authors.identifier: 0000-0002-1614-4696
authors.initials: R
authors.lastname: Parenti
authors.affiliation: Department of Biomedical and Biotechnological Sciences, University of Catania, Via Santa Sofia 64, 95127 Catania, Italy.
authors.forename: Massimo
authors.initials: M
authors.lastname: Gulisano
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis* / Q000235:genetics; D049109:Cell Proliferation / Q000235:genetics; D004268:DNA-Binding Proteins / Q000096:biosynthesis* / Q000235:genetics; D004195:Disease Models, Animal; D053823:Hedgehog Proteins / Q000096:biosynthesis* / Q000235:genetics; D006801:Humans; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000235:genetics; D051379:Mice; D016472:Motor Neuron Disease / Q000235:genetics* / Q000503:physiopathology; D009046:Motor Neurons / Q000378:metabolism / Q000473:pathology; D009419:Nerve Tissue Proteins / Q000096:biosynthesis* / Q000235:genetics; D009473:Neuronal Plasticity / Q000235:genetics; D054789:Ribosome Inactivating Proteins, Type 1 / Q000633:toxicity; D000076985:Saporins; D013119:Spinal Cord Injuries / Q000139:chemically induced / Q000235:genetics / Q000503:physiopathology; D000099176:Noggin Protein
chemical_list: D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D053823:Hedgehog Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D054789:Ribosome Inactivating Proteins, Type 1; D000076985:Saporins; D000099176:Noggin Protein; C106293:Numb protein, mouse; C465570:Shh protein, mouse; C578077:Tardbp protein, mouse