Selective Binding and Uptake of Ribonuclease A and Glyceraldehyde-3-phosphate Dehydrogenase by Isolated Rat Liver Lysosomes

Ana Maria Cuervo, Stanley R. Terlecky, J. Fred Dice, Erwin Knecht

Research output: Contribution to journalArticle

101 Citations (Scopus)

Abstract

Ribonuclease A (RNase A) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are selectively taken up and degraded by isolated rat liver lysosomes by very similar processes. The uptake and degradation of both of these proteins are stimulated by the heat shock cognate protein of 73 kDa and ATP/Mg2+. Both binding and uptake of RNase A and GAPDH by lysosomes are saturable, and uptake of RNase A and GAPDH requires a protease-sensitive component within the lysosomal membrane. GAPDH competes for binding and uptake of RNase A by lysosomes and vice versa while another protein, ovalbumin, does not compete. RNase S-peptide (amino acids 1-20 of RNase A) also competes for RNase A binding and uptake by lysosomes, while RNase S-protein (amino acids 21-124 of RNase A) does not compete. The uptake of RNase A by lysosomes appears to involve an intermediate step in which approximately 2 kDa of the polypeptide's COOH terminus remains outside lysosomes while the remainder is inside the lysosomal lumen.

Original languageEnglish (US)
Pages (from-to)26374-26380
Number of pages7
JournalJournal of Biological Chemistry
Volume269
Issue number42
StatePublished - Oct 21 1994
Externally publishedYes

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Pancreatic Ribonuclease
Glyceraldehyde-3-Phosphate Dehydrogenases
Lysosomes
Liver
Rats
Proteins
Amino Acids
Ovalbumin
Heat-Shock Proteins
Proteolysis
Peptide Hydrolases
Adenosine Triphosphate
Membranes
Degradation
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Selective Binding and Uptake of Ribonuclease A and Glyceraldehyde-3-phosphate Dehydrogenase by Isolated Rat Liver Lysosomes. / Cuervo, Ana Maria; Terlecky, Stanley R.; Dice, J. Fred; Knecht, Erwin.

In: Journal of Biological Chemistry, Vol. 269, No. 42, 21.10.1994, p. 26374-26380.

Research output: Contribution to journalArticle

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N2 - Ribonuclease A (RNase A) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are selectively taken up and degraded by isolated rat liver lysosomes by very similar processes. The uptake and degradation of both of these proteins are stimulated by the heat shock cognate protein of 73 kDa and ATP/Mg2+. Both binding and uptake of RNase A and GAPDH by lysosomes are saturable, and uptake of RNase A and GAPDH requires a protease-sensitive component within the lysosomal membrane. GAPDH competes for binding and uptake of RNase A by lysosomes and vice versa while another protein, ovalbumin, does not compete. RNase S-peptide (amino acids 1-20 of RNase A) also competes for RNase A binding and uptake by lysosomes, while RNase S-protein (amino acids 21-124 of RNase A) does not compete. The uptake of RNase A by lysosomes appears to involve an intermediate step in which approximately 2 kDa of the polypeptide's COOH terminus remains outside lysosomes while the remainder is inside the lysosomal lumen.

AB - Ribonuclease A (RNase A) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are selectively taken up and degraded by isolated rat liver lysosomes by very similar processes. The uptake and degradation of both of these proteins are stimulated by the heat shock cognate protein of 73 kDa and ATP/Mg2+. Both binding and uptake of RNase A and GAPDH by lysosomes are saturable, and uptake of RNase A and GAPDH requires a protease-sensitive component within the lysosomal membrane. GAPDH competes for binding and uptake of RNase A by lysosomes and vice versa while another protein, ovalbumin, does not compete. RNase S-peptide (amino acids 1-20 of RNase A) also competes for RNase A binding and uptake by lysosomes, while RNase S-protein (amino acids 21-124 of RNase A) does not compete. The uptake of RNase A by lysosomes appears to involve an intermediate step in which approximately 2 kDa of the polypeptide's COOH terminus remains outside lysosomes while the remainder is inside the lysosomal lumen.

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