| Clathrin pit-mediated endocytosis of neutrophil elastase and cathepsin G by cancer cells. | |
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MedLine Citation:
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PMID: 22915586 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Neutrophil elastase (NE) is a neutrophil-derived serine proteinase with broad substrate specificity. We have recently demonstrated that NE is capable of entering tumor cell endosomes and processing novel intracellular substrates. In the current study, we sought to determine the mechanism by which NE enters tumor cells. Our results show that NE enters into early endosomal antigen-1(+) endosomes in a dynamin- and clathrin-dependent but flotillin-1- and caveolin-1-independent fashion. Cathepsin G (but not proteinase-3) also enters tumor endosomes via the same mechanism. We utilized (125)I-labeled NE to demonstrate that NE binds to the surface of cancer cells. Incubation of radiolabeled NE with lung cancer cells displays a dissociation constant (K(d)) of 284 nm. Because NE is known to bind to heparan sulfate- and chondroitin sulfate-containing proteoglycans, we treated cells with glycanases to remove these confounding factors, which did not significantly diminish cell surface binding or endosomal entry. Thus, NE and CG bind to the surface of cancer cells, presumably to a cell surface receptor, and subsequently undergo clathrin pit-mediated endocytosis. |
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Authors:
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Alyssa D Gregory; Pamela Hale; David H Perlmutter; A McGarry Houghton |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2012-08-22 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 287 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-15 Completed Date: 2012-12-31 Revised Date: 2013-05-07 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 35341-50 Citation Subset: IM |
Affiliation:
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Department of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, 15261, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals CHO Cells Cathepsin G / genetics, metabolism* Caveolin 1 / genetics, metabolism Chondroitin Sulfates / genetics, metabolism Clathrin / genetics, metabolism* Coated Pits, Cell-Membrane / genetics, metabolism* Cricetinae Cricetulus Endocytosis* Humans Leukocyte Elastase / genetics, metabolism* Lung Neoplasms / genetics, metabolism* Neoplasm Proteins / genetics, metabolism* Protein Binding / genetics Protein Transport / genetics |
| Grant Support | |
ID/Acronym/Agency:
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5T32HL007563-24/HL/NHLBI NIH HHS; R01 HL108979/HL/NHLBI NIH HHS; R01HL108979/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Caveolin 1; 0/Clathrin; 0/Neoplasm Proteins; 9007-28-7/Chondroitin Sulfates; EC 3.4.21.20/CTSG protein, human; EC 3.4.21.20/Cathepsin G; EC 3.4.21.37/Leukocyte Elastase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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