High Throughput Assay Identifies Glafenine as a Corrector for the Folding Defect in Corneal Dystrophy-Causing Mutants of SLC4A11. Protein misfolding, causing retention of nascent protein in the endoplasmic reticulum (ER), is the most common molecular phenotype for disease alleles of membrane proteins. Strategies are needed to identify therapeutics able to correct such folding/trafficking defects of cell swelling are compared. A small-scale screen revealed that the nonsteroidal anti-inflammatory drugs (NSAIDs), glafenine, ibuprofen, and acetylsalicylic acid dissolved in 0.2% dimethyl sulfoxide (DMSO), partially rescued the trafficking defect in some SLC4A11 mutants, expressed in HEK293 cells. These SLC4A11 mutants retained functional activity when rescued to the plasma membrane by glafenine
or "floctafenic acid" or floctafenine or flunixin or "flunixin meglumine" or flupirtine or Flurbiprofen or frakefamide or fulranumab or funapide or Gabapentin or gefapixant or giripladib or "glafenic acid" or Glafenine or "gw 493838" or "gw 842166" or hasamal or ibudilast or Ibuprofen or indantadol or Interleukin or Ketamine or lacosamide or lappaconitine or lenabasum or letimide or lexanopadol or "Magnesium
vulnerable to oxidative and mitochondrial damage and more prone to apoptotic death.A small-scale drug screen showed that Glafenine, a disused NSAID, was able to move some SLC4A11 mutants to the cell surface, suggesting that other NSAIDs might also have therapeutic potential.Further, the retained protein in the Endoplasmic reticulum and the effects of various drugs on its expression to the surface was taken