Publication | Closed Access
A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular Proteins
961
Citations
30
References
1989
Year
Protein AssemblyProteasomeMolecular BiologyProtein RefoldingProtein FoldingProteomicsProtein DegradationMonoclonal AntibodyProtein ChemistryProtein Quality ControlProtein FunctionInternal PeptidesBiochemistryIntracellular ProteinProtein TransportTranslational ProteomicsCell BiologyProtein PhosphorylationNatural SciencesIntracellular ProteinsLysosomal DegradationCellular BiochemistryMedicineLysosomal Storage Disease
A 73-kilodalton (kD) intracellular protein was found to bind to peptide regions that target intracellular proteins for lysosomal degradation in response to serum withdrawal. This protein cross-reacted with a monoclonal antibody raised to a member of the 70-kD heat shock protein (hsp70) family, and sequences of two internal peptides of the 73-kD protein confirm that it is a member of this family. In response to serum withdrawal, the intracellular concentration of the 73-kD protein increased severalfold. In the presence of adenosine 5′-triphosphate (ATP) and MgCl 2 , the 73-kD protein enhanced protein degradation in two different cell-free assays for lysosomal proteolysis.
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