{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T03:11:27Z","timestamp":1789009887384,"version":"build-2803163510"},"reference-count":56,"publisher":"American Society of Hematology","issue":"9","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2022,3,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Fibrinogen plays a pathologic role in multiple diseases. It contributes to thrombosis and modifies inflammatory and immune responses, supported by studies in mice expressing fibrinogen variants with altered function or with a germline fibrinogen deficiency. However, therapeutic strategies to safely and effectively tailor plasma fibrinogen concentration are lacking. Here, we developed a strategy to tune fibrinogen expression by administering lipid nanoparticle (LNP)-encapsulated small interfering RNA (siRNA) targeting the fibrinogen \u03b1 chain (siFga). Three distinct LNP-siFga reagents reduced both hepatic Fga messenger RNA and fibrinogen levels in platelets and plasma, with plasma levels decreased to 42%, 16%, and 4% of normal within 1 week of administration. Using the most potent siFga, circulating fibrinogen was controllably decreased to 32%, 14%, and 5% of baseline with 0.5, 1.0, and 2.0 mg\/kg doses, respectively. Whole blood from mice treated with siFga formed clots with significantly decreased clot strength ex vivo, but siFga treatment did not compromise hemostasis following saphenous vein puncture or tail transection. In an endotoxemia model, siFga suppressed the acute phase response and decreased plasma fibrinogen, D-dimer, and proinflammatory cytokine levels. In a sterile peritonitis model, siFga restored normal macrophage migration in plasminogen-deficient mice. Finally, treatment of mice with siFga decreased the metastatic potential of tumor cells in a manner comparable to that observed in fibrinogen-deficient mice. The results indicate that siFga causes robust and controllable depletion of fibrinogen and provides the proof-of-concept that this strategy can modulate the pleiotropic effects of fibrinogen in relevant disease models.<\/jats:p>","DOI":"10.1182\/blood.2021014559","type":"journal-article","created":{"date-parts":[[2021,12,27]],"date-time":"2021-12-27T22:00:46Z","timestamp":1640642446000},"page":"1302-1311","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":30,"title":["Suppression of fibrin(ogen)-driven pathologies in disease\u00a0models through controlled knockdown by\u00a0lipid\u00a0nanoparticle delivery of siRNA"],"prefix":"10.1182","volume":"139","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1760-3425","authenticated-orcid":false,"given":"Lih Jiin","family":"Juang","sequence":"first","affiliation":[{"name":"Michael Smith Laboratories,"},{"name":"Centre for Blood Research, and"},{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5074-6423","authenticated-orcid":false,"given":"Woosuk S.","family":"Hur","sequence":"additional","affiliation":[{"name":"Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6282-2657","authenticated-orcid":false,"given":"Lakmali M.","family":"Silva","sequence":"additional","affiliation":[{"name":"Proteases and Tissue Remodeling Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amy W.","family":"Strilchuk","sequence":"additional","affiliation":[{"name":"Michael Smith Laboratories,"},{"name":"Centre for Blood Research, and"},{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brenton","family":"Francisco","sequence":"additional","affiliation":[{"name":"Cancer and Blood Diseases Institute, Cincinnati Children's Hospital Medical Center and the University of Cincinnati College of Medicine, Cincinnati, OH;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8714-8440","authenticated-orcid":false,"given":"Jerry","family":"Leung","sequence":"additional","affiliation":[{"name":"Michael Smith Laboratories,"},{"name":"Centre for Blood Research, and"},{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1764-0245","authenticated-orcid":false,"given":"Madelaine K.","family":"Robertson","sequence":"additional","affiliation":[{"name":"Michael Smith Laboratories,"},{"name":"Centre for Blood Research, and"},{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1207-5769","authenticated-orcid":false,"given":"Dafna J.","family":"Groeneveld","sequence":"additional","affiliation":[{"name":"Department of Pathobiology and Diagnostic Investigation, Institute for Integrative Toxicology, Michigan State University, East Lansing, MI;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bridget","family":"La Prairie","sequence":"additional","affiliation":[{"name":"Michael Smith Laboratories,"},{"name":"Centre for Blood Research, and"},{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7916-9308","authenticated-orcid":false,"given":"Elizabeth M.","family":"Chun","sequence":"additional","affiliation":[{"name":"Proteases and Tissue Remodeling Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew P.","family":"Cap","sequence":"additional","affiliation":[{"name":"The United States Army Institute of Surgical Research, JBSA-Fort Sam Houston, TX;"},{"name":"Department of Medicine, Uniformed Services University, Bethesda, MD;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James P.","family":"Luyendyk","sequence":"additional","affiliation":[{"name":"Department of Pathobiology and Diagnostic Investigation, Institute for Integrative Toxicology, Michigan State University, East Lansing, MI;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph S.","family":"Palumbo","sequence":"additional","affiliation":[{"name":"Cancer and Blood Diseases Institute, Cincinnati Children's Hospital Medical Center and the University of Cincinnati College of Medicine, Cincinnati, OH;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pieter R.","family":"Cullis","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas H.","family":"Bugge","sequence":"additional","affiliation":[{"name":"Proteases and Tissue Remodeling Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew J.","family":"Flick","sequence":"additional","affiliation":[{"name":"Department of Pathology and 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