{"corpus_id":85890298,"paper_sha":"5cfd2332771643c71a2b2d7ede26baf483b6453d","doi":"10.1074/jbc.271.45.28485","arxiv_id":null,"pmid":null,"pmcid":null,"mag_id":2166179228,"dblp_id":null,"acl_id":null,"title":"Osteopontin N-terminal Domain Contains a Cryptic Adhesive Sequence Recognized by α9β1 Integrin*","year":1996,"publication_date":"1996-11-08","venue":"Journal of Biological Chemistry","journal":{"name":"The Journal of Biological Chemistry","pages":"28485 - 28491","volume":"271"},"journal_issn":null,"journal_title":null,"publication_types":[],"pubmed_pub_types":null,"s2_fields_of_study":["Biology","Medicine","Chemistry"],"reference_count":54,"citation_count":241,"influential_citation_count":4,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":null,"chemicals":null,"comments_corrections":null,"source_flags":1,"s2_open_access_pdf_url":null,"s2_open_access_landing_url":null,"s2_open_access_license":null,"s2_open_access_status":null,"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":"Osteopontin is an adhesive glycoprotein implicated in numerous diseases associated with inflammation and remodeling. There are several structural domains in osteopontin that are of particular interest. The RGD motif is a cell attachment sequence shown to be critical for cell adhesion through αv-containing integrins. In close proximity to the RGD domain is the thrombin cleavage site. Previous observations suggest that thrombin cleavage of osteopontin occurs in vivo and may be physiologically important. To study the functional significance of osteopontin cleavage by thrombin, we made glutathione S-transferase-osteopontin fusion proteins. These proteins contain either the N- or C-terminal domains expected to be formed following thrombin cleavage at the Arg169-Ser170 peptide bond. We compared these osteopontin fragments with native osteopontin in their ability to support adhesion of several different cell lines and identified the receptors mediating these interactions. Our data show that the N-terminal osteopontin fragment, which contains the RGD domain, supports adhesion of a melanoma cell line that is unable to bind native osteopontin. This suggests that osteopontin adhesive interactions may be regulated by thrombin cleavage. We also demonstrate that osteopontin contains a cryptic binding activity, which can be recognized by a novel osteopontin receptor. This receptor has been identified as the α9β1 integrin.","claims":[{"public_id":"cl_c45cdfe60b8d526bfabd3f336caf2b75","status":"active","text":"Glutathione S-transferase-osteopontin fusion proteins were constructed to represent the N-terminal and C-terminal domains generated by thrombin cleavage of osteopontin at the Arg169-Ser170 peptide bond.","confidence":0.9,"contributors":[{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["extraction"],"url":"https://sah.borca.ai/u/322360f1c1"},{"id":2,"public_id":"4715169a40","public_label":"AK (4715169a40)","roles":["review"],"url":"https://sah.borca.ai/u/4715169a40"},{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["review"],"url":"https://sah.borca.ai/u/12632b8b5f"},{"id":1165,"public_id":"ezd9qvkvax","public_label":"The Reverser‮ 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