A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins

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 s...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1989-10, Vol.246 (4928), p.382-385
Main Authors: Chiang, H L, Terlecky, S R, Plant, C P, Dice, J F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Cells, Cultured
Heat-Shock Proteins - genetics
Heat-Shock Proteins - physiology
Immunoblotting
lysosomes
Lysosomes - metabolism
Molecular Sequence Data
Rats
Ribonuclease, Pancreatic - genetics
Ribonuclease, Pancreatic - metabolism
Sequence Homology, Nucleic Acid
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Summary: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 MgCl2, the 73-kD protein enhanced protein degradation in two different cell-free assays for lysosomal proteolysis.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2799391