ArticleProceedings of the National Academy of Sciences of the United States of America1993
The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 49 citations in OpenAlex.
- TcCYPR04, a Cacao Papain-Like Cysteine-Protease Detected in Senescent and Necrotic Tissues Interacts with a Cystatin TcCYS4.PloS one · 2015Article
- pH-induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: implications for zymogen activation.Protein science : a publication of the Protein Society · 2001Article
- Biogenesis of the protein storage vacuole crystalloid.The Journal of cell biology · 2000Article
- Rubella virus nonstructural protein protease domains involved in trans- and cis-cleavage activities.Journal of virology · 2000Article
- Expression and characterization of a recombinant cysteine proteinase of Leishmania mexicana.The Biochemical journal · 2000Article
- Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly.Journal of virology · 1999Article
- Effect of carbohydrate position on lysosomal transport of procathepsin L.Molecular biology of the cell · 1998Article
- Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic beta-cells.The Journal of cell biology · 1997Article
- Expression of functional recombinant human procathepsin B in mammalian cells.The Biochemical journal · 1996Article
- Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.The EMBO journal · 1996Article
- Mitogenic function of human procathepsin D: the role of the propeptide.The Biochemical journal · 1994Article
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2 authors at 1 institution in 1 country.
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Abstract
Two lysosomal proenzymes, procathepsins L and D, bind to mouse fibroblast microsomal membranes at acidic pH. This membrane association is independent of the mannose-6-phosphate receptors and requires the presence of the N-terminal propeptides of the enzymes. We have identified the protein that specifically binds procathepsin L at pH 5. A 43-kDa membrane protein coimmunoprecipitated with procathepsin L at pH 5 but not at pH 7 when cells were denatured with detergents. Similarly, a 43-kDa integral membrane protein bound procathepsin L in three kinds of ligand blots at pH 5 but not at pH 7. A synthetic peptide containing the 24 N-terminal residues of mouse procathepsin L blocked the binding of procathepsin L to this integral membrane protein on ligand blots. These results indicate that the 43-kDa integral membrane protein is a lysosomal proenzyme receptor that specifically binds the procathepsin L activation peptide at acidic pH.
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