{"corpus_id":22046890,"paper_sha":"5e13919ea733d8237527aacd2a7162ccacb6b3f4","doi":"10.1074/JBC.270.9.4689","arxiv_id":null,"pmid":7876240,"pmcid":null,"mag_id":2071660979,"dblp_id":null,"acl_id":null,"title":"Human Mast Cell Chymase and Leukocyte Elastase Release Latent Transforming Growth Factor-β1 from the Extracellular Matrix of Cultured Human Epithelial and Endothelial Cells (*)","year":1995,"publication_date":"1995-03-03","venue":"Journal of Biological Chemistry","journal":{"name":"The Journal of Biological Chemistry","pages":"4689 - 4696","volume":"270"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article","Research Support, Non-U.S. Gov't"],"s2_fields_of_study":["Biology","Medicine"],"reference_count":86,"citation_count":421,"influential_citation_count":14,"is_open_access":true,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Amnion","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D000650"},{"d":"Animals","mj":false,"ui":"D000818"},{"d":"Carrier Proteins","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D002352"},{"d":"Cells, Cultured","mj":false,"ui":"D002478"},{"d":"Chymases","mj":false,"ui":"D053818"},{"d":"Endothelium","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D004727"},{"d":"Epithelium","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D004848"},{"d":"Extracellular Matrix","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D005109"},{"d":"Humans","mj":false,"ui":"D006801"},{"d":"Intracellular Signaling Peptides and Proteins","mj":true,"ui":"D047908"},{"d":"Latent TGF-beta Binding Proteins","mj":false,"ui":"D053779"},{"d":"Leukocyte Elastase","mj":false,"ui":"D019272"},{"d":"Mast Cells","mj":false,"qs":[{"q":"enzymology","mj":true,"ui":"Q000201"}],"ui":"D008407"},{"d":"Mink","mj":false,"ui":"D008907"},{"d":"Pancreatic Elastase","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D010196"},{"d":"Protein Processing, Post-Translational","mj":false,"ui":"D011499"},{"d":"Serine Endopeptidases","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D012697"},{"d":"Transforming Growth Factor beta","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D016212"}],"chemicals":[{"n":"Carrier Proteins","ui":"D002352","reg":"0"},{"n":"Intracellular Signaling Peptides and Proteins","ui":"D047908","reg":"0"},{"n":"Latent TGF-beta Binding Proteins","ui":"D053779","reg":"0"},{"n":"Transforming Growth Factor beta","ui":"D016212","reg":"0"},{"n":"Serine Endopeptidases","ui":"D012697","reg":"EC 3.4.21.-"},{"n":"Pancreatic Elastase","ui":"D010196","reg":"EC 3.4.21.36"},{"n":"Leukocyte Elastase","ui":"D019272","reg":"EC 3.4.21.37"},{"n":"Chymases","ui":"D053818","reg":"EC 3.4.21.39"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":"http://www.jbc.org/article/S0021925818828290/pdf","s2_open_access_landing_url":"https://www.semanticscholar.org/paper/5e13919ea733d8237527aacd2a7162ccacb6b3f4","s2_open_access_license":"CCBY","s2_open_access_status":"HYBRID","pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"Monolayer cultures of human epithelial and endothelial cells were used to study the association of latent transforming growth factor-β1 (TGF-β1) to extracellular matrices and its release and activation during matrix degradation. Human umbilical vein endothelial cells and embryonic lung fibroblasts produced relatively high levels of TGF-β1, its propeptide (β1-latency-associated protein), and latent TGF-β-binding protein and incorporated latent TGF-β1 into their matrices as shown by immunoblotting. Amnion epithelial cells produced lower levels of these proteins. Confluent cultures of epithelial cells were exposed to matrix-degrading proteases and glycosidases. Mast cell chymase, leukocyte elastase, and plasmin efficiently released matrix-bound latent TGF-β1 complexes, while chondroitinase ABC and heparitinases were ineffective. The ability of the proteases to activate recombinant latent TGF-β1 was tested using growth inhibition assays and a novel sodium deoxycholate-polyacrylamide gel electrophoresis followed by immunoblotting. Sodium deoxycholate solubilized Mr 25,000 TGF-β1 but did not dissociate high Mr latent TGF-β1 complexes, allowing separation of these forms by polyacrylamide gel electrophoresis. Mast cell chymase and leukocyte elastase did not activate latent TGF-β1, suggesting that its release from matrix and activation are controlled by different mechanisms. The release of TGF-β from the matrix by leukocyte and mast cell enzymes may contribute to the accumulation of connective tissue in inflammation.","claims":[{"public_id":"cl_be204c48e9ce3f9eba4ef46f3d90157c","status":"active","text":"Chondroitinase ABC and heparitinases were ineffective at releasing matrix-bound latent TGF-β1 complexes.","confidence":0.92,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_be204c48e9ce3f9eba4ef46f3d90157c"},{"public_id":"cl_ae7b4e2ac1b82ec6d5b8ddc9d86118f1","status":"active","text":"Human umbilical vein endothelial cells and embryonic lung fibroblasts incorporated relatively high levels of latent TGF-β1 and its associated propeptide and binding protein into their extracellular matrices, whereas amnion epithelial cells produced lower levels of these 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