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Full-Text Articles in Life Sciences
Restoration Of Motor Defects Caused By Loss Of Drosophila Tdp-43 By Expression Of The Voltage-Gated Calcium Channel, Cacophony, In Central Neurons, Kayly M. Lembke, David B. Norton, Charles Scudder
Restoration Of Motor Defects Caused By Loss Of Drosophila Tdp-43 By Expression Of The Voltage-Gated Calcium Channel, Cacophony, In Central Neurons, Kayly M. Lembke, David B. Norton, Charles Scudder
Faculty Publications - Department of Biological & Molecular Science
Defects in the RNA-binding protein, TDP-43, are known to cause a variety of neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal lobar dementia. A variety of experimental systems have shown that neurons are sensitive to TDP-43 expression levels, yet the specific functional defects resulting from TDP-43 dysregulation have not been well described. Using the Drosophila TDP-43 ortholog TBPH, we previously showed that TBPH-null animals display locomotion defects as third instar larvae. Furthermore, loss of TBPH caused a reduction in cacophony, a Type II voltage-gated calcium channel, expression and that genetically restoring cacophony in motor neurons in TBPH mutant animals was …
Role Of The Invertebrate Electrogenic 2na+/H+ Antiporter In Monovalent And Divalent Cation Transport, Gregory A. Ahearn, Jeff Duerr, V. Pennington
Role Of The Invertebrate Electrogenic 2na+/H+ Antiporter In Monovalent And Divalent Cation Transport, Gregory A. Ahearn, Jeff Duerr, V. Pennington
Faculty Publications - Department of Biological & Molecular Science
In recent years, an electrogenic 2Na+/1H+ antiporter has been identified in a variety of invertebrate epithelial brush-border membranes of gut, kidney and gill tissues. The antiporter differs significantly in its physiological properties from the electroneutral 1Na+/1H+ antiporter proposed for vertebrate cells. In all invertebrate cells examined, the antiporter displayed a 2:1 transport stoichiometry, responded to an induced transmembrane potential and exhibited a high binding affinity for the divalent cation Ca2+, which acted as a competitive inhibitor of Na+ transport. A monoclonal antibody specific for the crustacean electrogenic antiporter inhibited 2Na+/1H+ exchange, but was without effect on Na+-dependent D-glucose transport. Immunoreactivity …