Efficient degradation in vitro of all intermediate filament subunit proteins by the Ca2+-activated neutral thiol proteinase from Ehrlich ascites tumor cells and porcine kidney.
Vimentin, desmin, glial fibrillary acidic protein, neurofilament triplet proteins, and a mixture of cytokeratins were digested with Ca2+-activated neutral thiol proteinase isolated from Ehrlich ascites tumor (EAT) cells and porcine kidney. All intermediate filament proteins were degraded by the proteinase, although with different rates and Ca2+ optima. These results are in part at variance with our previous statement that the Ca2+-activated proteinase from EAT cells is specific for vimentin and desmin.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology* / Q000473:pathology; D002478:Cells, Cultured; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003546:Cysteine Endopeptidases; D003893:Desmin / Q000302:isolation & purification / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D007381:Intermediate Filament Proteins / Q000378:metabolism*; D007668:Kidney / Q000166:cytology / Q000201:enzymology*; D007700:Kinetics; D013552:Swine; D014746:Vimentin / Q000302:isolation & purification / Q000378:metabolism
D003893:Desmin; D005904:Glial Fibrillary Acidic Protein; D007381:Intermediate Filament Proteins; D014746:Vimentin; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002118:Calcium