{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T14:03:49Z","timestamp":1790863429208,"version":"4.1.0"},"reference-count":39,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T00:00:00Z","timestamp":1788998400000},"content-version":"am","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100003554","name":"Lundbeck Foundation","doi-asserted-by":"publisher","award":["grant number R413-2022-621"],"award-info":[{"award-number":["grant number R413-2022-621"]}],"id":[{"id":"10.13039\/501100003554","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100024571","name":"The Novo Nordisk Foundation Center for Protein Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100024571","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Foundation","doi-asserted-by":"publisher","award":["NNF14CC0001"],"award-info":[{"award-number":["NNF14CC0001"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Foundation","doi-asserted-by":"publisher","award":["NNF24SA0098829"],"award-info":[{"award-number":["NNF24SA0098829"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Foundation","doi-asserted-by":"publisher","award":["NNF21OC0072070"],"award-info":[{"award-number":["NNF21OC0072070"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Standardized molecular methods to assess the host response to breast implants are lacking. Mass spectrometry\u2013based proteomics offers an unbiased approach to characterize the capsule proteome and the foreign-body response.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Objectives<\/jats:title>\n                    <jats:p>The aim of this study was to establish proof of concept for deep proteomic profiling of human breast implant capsule tissue and explore the proteomic profile associated with capsular contracture.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>Capsule biopsies were obtained from women with capsular contracture (Baker III\/IV, n = 24) and noncontracture controls (Baker I, n = 24). Proteomic profiles were analyzed by liquid chromatography\u2013tandem mass spectrometry with label-free quantification. Differential expression, co-expression network, and functional enrichment analyses were performed, and capsules were additionally scored with a validated histopathological system.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Deep proteomic profiling quantified 7258 proteins (median 5879 per sample). Unsupervised analyses separated contracture from control samples without previous grouping information, indicating a distinct contracture-associated proteome (P = .001). The authors identified 77 differentially expressed proteins (31 upregulated, 46 downregulated). Extracellular matrix (ECM) remodeling dominated, with upregulation of MMP9 and inhibitors TIMP1 and TIMP3. A profibrotic transforming growth factor-beta (TGF-\u03b2) signature included THBS1, THBS2, periostin, and TGM2, and innate immune activation included MPO, FCGR1A, S100A8, and S100A9. Co-expression network analysis identified a contracture-associated neutrophil degranulation module, and an adaptive immune module linked to implantation time and rupture.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>Deep proteomic profiling of human breast implant capsules is feasible and revealed a contracture-associated proteomic phenotype dominated by ECM dysregulation, a profibrotic TGF-\u03b2 axis, and innate and adaptive immune activation. These findings provide proof of concept for capsule proteomics as a tool to study the host response to breast implants.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1093\/asj\/sjag186","type":"journal-article","created":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T11:54:54Z","timestamp":1788954894000},"source":"Crossref","is-referenced-by-count":0,"title":["Proteomic Profiling of Breast Implant Capsules: A Novel Approach for Studying Biocompatibility and Capsular Contracture"],"prefix":"10.1093","author":[{"given":"Andreas","family":"Larsen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3160-8548","authenticated-orcid":false,"given":"Ole","family":"\u00d8stergaard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tim 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