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Blood, 15 August 2001, Vol. 98, No. 4, pp. 1231-1238
PHAGOCYTES
Molecular basis of biomaterial-mediated foreign body
reactions
Wen-Jing Hu,
John W. Eaton,
Tatiana P. Ugarova,and
Liping Tang
From the Department of Pediatrics, Baylor College of
Medicine, Houston, TX.
Despite being inert and nontoxic, implanted biomaterials often
trigger adverse foreign body reactions such as inflammation, fibrosis,
infection, and thrombosis. With regard to the inflammatory responses to
biomaterial implants, it was previously found that a crucial
precedent event was the spontaneous adsorption and denaturation of
fibrinogen on implant surfaces. It was further found that interactions between the phagocyte integrin Mac-1 (CD11b/CD18) and one short sequence within the fibrinogen D domain ( 190-202; P1) at least partially explained phagocyte accumulation on implant surfaces. However, the reason that adsorbed fibrinogen is proinflammatory while soluble fibrinogen clearly is notremained obscure. In this study, therefore, the question of how fibrinogen is converted to a
proinflammatory state when adsorbed to biomaterial surfaces is
investigated. In soluble fibrinogen, the 13 amino acid P1
sequence was found to be hidden. However, the adsorption and
denaturation of fibrinogen on the surfaces of commonly used
biomaterials lead to the exposure of P1 and a second neo-epitope,
377-395 (P2), which also interacts with Mac-1 and is similarly
occult in the soluble protein. The extent of biomaterial-mediated P1
and P2 exposure appears directly related to the severity of
inflammatory responses to a test panel of biomaterials. Finally,
thrombin-mediated conversion of fibrinogen to fibrin also exposes both
P1 and P2 epitopes. These observations may help explain both the
inflammation caused by many types of implanted biomaterials and that
which occurs naturally following thrombotic events.
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