{"corpus_id":25270053,"paper_sha":"350cb5b29c24226c0ab50c7e2aa6514df03ac418","doi":"10.1074/jbc.M109.065805","arxiv_id":null,"pmid":20053996,"pmcid":"PMC2832975","mag_id":2092536645,"dblp_id":null,"acl_id":null,"title":"A Novel Mannose-binding Lectin/Ficolin-associated Protein Is Highly Expressed in Heart and Skeletal Muscle Tissues and Inhibits Complement Activation*","year":2010,"publication_date":"2010-01-06","venue":"Journal of Biological Chemistry","journal":{"name":"The Journal of Biological Chemistry","pages":"8234 - 8243","volume":"285"},"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":28,"citation_count":157,"influential_citation_count":7,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Alternative Splicing","mj":false,"qs":[{"q":"physiology","mj":false,"ui":"Q000502"}],"ui":"D017398"},{"d":"Amino Acid Sequence","mj":false,"ui":"D000595"},{"d":"Animals","mj":false,"ui":"D000818"},{"d":"Antibody Specificity","mj":false,"ui":"D000918"},{"d":"CHO Cells","mj":false,"ui":"D016466"},{"d":"Complement Activation","mj":false,"qs":[{"q":"physiology","mj":true,"ui":"Q000502"}],"ui":"D003167"},{"d":"Cricetinae","mj":false,"ui":"D006224"},{"d":"Cricetulus","mj":false,"ui":"D003412"},{"d":"Cross Reactions","mj":false,"ui":"D003429"},{"d":"Humans","mj":false,"ui":"D006801"},{"d":"Immunohistochemistry","mj":false,"ui":"D007150"},{"d":"Isomerism","mj":false,"ui":"D007536"},{"d":"Lectins","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D037102"},{"d":"Mannose-Binding Lectins","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D037241"},{"d":"Mannose-Binding Protein-Associated Serine Proteases","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":true,"ui":"Q000235"},{"q":"immunology","mj":false,"ui":"Q000276"},{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D050606"},{"d":"Molecular Sequence Data","mj":false,"ui":"D008969"},{"d":"Molecular Weight","mj":false,"ui":"D008970"},{"d":"Muscle, Skeletal","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D018482"},{"d":"Myocardium","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D009206"},{"d":"RNA, Messenger","mj":false,"qs":[{"q":"metabolism","mj":false,"ui":"Q000378"}],"ui":"D012333"},{"d":"Reverse Transcriptase Polymerase Chain Reaction","mj":false,"ui":"D020133"},{"d":"Ficolins","mj":false,"ui":"D000097604"}],"chemicals":[{"n":"Lectins","ui":"D037102","reg":"0"},{"n":"Mannose-Binding Lectins","ui":"D037241","reg":"0"},{"n":"Mannose-Binding Protein-Associated Serine Proteases","ui":"D050606","reg":"EC 3.4.21.-"},{"n":"RNA, Messenger","ui":"D012333","reg":"0"},{"n":"Ficolins","ui":"D000097604","reg":"0"},{"n":"MASP1 protein, human","ui":"C084067","reg":"EC 3.4.21.-"},{"n":"MASP2 protein, human","ui":"C105296","reg":"EC 3.4.21.-"}],"comments_corrections":null,"source_flags":5,"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":"The human lectin complement pathway involves circulating complexes consisting of mannose-binding lectin (MBL) or three ficolins (ficolin-1, -2, and -3) in association with three MBL/ficolin-associated serine proteases (MASP) (MASP-1, -2, and -3) and a nonenzymatic sMAP. MASP-1 and MASP-3 (MASP1 isoforms 1 and 2, respectively) are splice variants of the MASP1 gene, whereas MASP-2 and sMAP are splice variants of the MASP2 gene. We have identified a novel serum protein of 45 kDa that is associated with MBL and the ficolins. This protein is named MBL/ficolin-associated protein 1 (MAP-1 corresponding to MASP1 isoform 3). The transcript generating MAP-1 (MASP1_v3) contains exons 1–8 and a novel exon encoding an in-frame stop codon. The corresponding protein lacks the serine protease domains but contains most of the common heavy chain of MASP-1 and MASP-3. Additionally MAP-1 contains 17 unique C-terminal amino acids. By use of quantitative PCR and MAP-1-specific immunohistochemistry, we found that MAP-1 is highly expressed in myocardial and skeletal muscle tissues as well as in liver hepatocytes with a different expression profile than that observed for MASP-1 and MASP-3. MAP-1 co-precipitated from human serum with MBL, ficolin-2, and ficolin-3, and recombinant MAP-1 was able to inhibit complement C4 deposition via both the ficolin-3 and MBL pathway. In conclusion we have identified a novel 45-kDa serum protein derived from the MASP1 gene, which is highly expressed in striated muscle tissues. It is found in complex with MBL and ficolins and may function as a potent inhibitor of the complement system in vivo.","claims":[{"public_id":"cl_f93efd949acd5a70cd49b9ca1a75b0a1","status":"active","text":"MAP-1 is a novel 45-kDa serum protein derived from the MASP1 gene, highly expressed in striated muscle tissues, and found in complex with MBL and ficolins.","confidence":0.95,"contributors":[{"id":32,"public_id":"7c402c1b98","public_label":"뀨 (7c402c1b98)","roles":["extraction"],"url":"https://sah.borca.ai/u/7c402c1b98"},{"id":35,"public_id":"b2adb6bfad","public_label":"Anonymous (b2adb6bfad)","roles":["review"],"url":"https://sah.borca.ai/u/b2adb6bfad"},{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["review"],"url":"https://sah.borca.ai/u/322360f1c1"}],"url":"https://sah.borca.ai/claims/cl_f93efd949acd5a70cd49b9ca1a75b0a1"},{"public_id":"cl_06b597423090131fb3f521d07e7e6b51","status":"active","text":"MAP-1 is highly expressed in myocardial and skeletal muscle tissues as well as in liver hepatocytes, with a different expression profile than MASP-1 and MASP-3.","confidence":0.9,"contributors":[{"id":32,"public_id":"7c402c1b98","public_label":"뀨 (7c402c1b98)","roles":["extraction"],"url":"https://sah.borca.ai/u/7c402c1b98"},{"id":35,"public_id":"b2adb6bfad","public_label":"Anonymous (b2adb6bfad)","roles":["review"],"url":"https://sah.borca.ai/u/b2adb6bfad"},{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["review"],"url":"https://sah.borca.ai/u/322360f1c1"}],"url":"https://sah.borca.ai/claims/cl_06b597423090131fb3f521d07e7e6b51"},{"public_id":"cl_9d85c4e796c8966446fc20491d0b0482","status":"active","text":"MAP-1 lacks serine protease domains but contains most of the common heavy chain of MASP-1 and MASP-3 plus 17 unique C-terminal amino acids.","confidence":0.95,"contributors":[{"id":32,"public_id":"7c402c1b98","public_label":"뀨 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