Reactions of Formed Elements of Blood With Plasma Proteins at Interfaces*

Vroman, Leo; Adams, Ann L.; Klings, Madeleine; Fischer, Gena; Muñoz, Phillip A.; Solensky, Regina P.

doi:10.1111/j.1749-6632.1977.tb41753.x

Cited by 148 publications

(47 citation statements)

References 23 publications

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“…The rapid occurrence ofthe change in cellular shape and the maintenance of a high response at low concentrations ofcells suggest that it is a direct effect ofCF on the cells, Factors affecting cellular adhesiveness. Our data are consistent with the observations that the pretreatment of glass with albumin or serum reduces attachment of neutrophils to the treated surface (18). Though the chemical basis for this effect is yet to be determined, we used the phenomenon to provide a controlled level of attachment of neutrophils to a surface.…”

Section: Discussionsupporting

confidence: 78%

Motility and Adhesiveness in Human Neutrophils

Smith¹,

Hollers²,

Patrick³

et al. 1979

J. Clin. Invest.

220

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Section: Discussionsupporting

confidence: 78%

Motility and Adhesiveness in Human Neutrophils

Smith¹,

Hollers²,

Patrick³

et al. 1979

J. Clin. Invest.

220

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“…The ensuing chronic inflammation may prompt a number of serious iatrogenic consequences such as stress cracking on pacemaker leads (1, 2), osteolysis adjacent artificial joints (3)(4)(5), and fibrosis and capsule contracture surrounding mammary prostheses (6-10). In the search for the proximate trigger of these responses, a chaotic layer of spontaneously adsorbed host proteins on implant surfaces has been indicted as a possible culprit (11)(12)(13)(14)(15). This is because the adsorption of plasma proteins to implant surfaces is almost instantaneous; therefore, inflammatory cells likely interact with this protein layer rather than the material itself.…”

Section: Discussionmentioning

confidence: 99%

“…However, after implantation, biomaterials spontaneously acquire a layer of host protein. Therefore, this surface protein layer actually may be responsible for subsequent phagocyte attraction and activation on the surfaces of implants (11)(12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

Molecular determinants of acute inflammatory responses to biomaterials.

et al. 1996

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The frequent inflammatory responses to implanted medical devices are puzzling in view of the inert and nontoxic nature of most biomaterials. Because implant surfaces spontaneously adsorb host proteins, this proteinaceous film is probably important in the subsequent attraction of phagocytes. In fact, earlier we found that acute inflammatory responses to experimental polyethylene terephthalate implants in mice require the precedent adsorption of one particular host protein, fibrinogen. The present investigations were aimed at defining the molecular determinants of fibrinogen-mediated acute inflammatory responses to implanted biomaterials. We find: ( a ) plasmin degradation of purified fibrinogen into defined domains reveals that the proinflammatory activity resides within the D fragment, which contains neither the fibrin cross-linking sites nor RGD sequences; ( b ) the major (and, perhaps, exclusive) proinflammatory sequence appears to be fibrinogen ␥ 190-202, previously shown to interact with CD11b/CD18 (Mac-1). The chemically synthesized peptide, cross-linked to albumin (which itself does not promote inflammatory responses), mimics the proinflammatory effect of adsorbed native fibrinogen; and ( c ) this sequence probably promotes inflammatory responses through interactions with Mac-1 because phagocyte accumulation on experimental implants is almost completely abrogated by administration of recombinant neutrophil inhibitory factor (which blocks CD11b-fibrin(ogen) interaction). We conclude that improved knowledge of such surface-proteinphagocyte interactions may permit the future development of more biocompatible implantable materials. ( J. Clin. Invest. 1996. 97:1329-1334.)

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“…The question of why materials with diverse surface properties elicit the same FBR has troubled investigators for more than two decades (3)(4)(5). It is believed that implants acquire a protein coat immediately after implantation, which serves as a stimulus for the development of the FBR (6)(7)(8)(9)(10), and it has been suggested that fibrinogen is a critical component of this protein coat (10,11). Adsorption of proteins can be influenced by the surface properties of the material and may lead to modification of the FBR (3,(12)(13)(14)(15).…”

mentioning

confidence: 99%

Mice that lack the angiogenesis inhibitor, thrombospondin 2, mount an altered foreign body reaction characterized by increased vascularity

Kyriakides

Leach

Hoffman

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

145

101

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Disruption of the thrombospondin 2 gene (Thbs2) in mice results in a complex phenotype characterized chief ly by abnormalities in fibroblasts, connective tissues, and blood vessels. Consideration of this phenotype suggested to us that the foreign body reaction (FBR) might be altered in thrombospondin 2 (TSP2)-null mice. To investigate the participation of TSP2 in the FBR, polydimethylsiloxane (PDMS) and oxidized PDMS (ox-PDMS) disks were implanted in TSP2-null and control mice. Growth of TSP2-null and control skin fibroblasts in vitro also was evaluated on both types of disks. Normal fibroblasts grew as a monolayer on both surfaces, but attachment of the cells to ox-PDMS was weak and sensitive to movement. TSP2-null fibroblasts grew as aggregates on both surfaces, and their attachment was further compromised on ox-PDMS. After a 4-week implantation period, both types of PDMS elicited a similar FBR with a collagenous capsule in both TSP2-null and control mice. However, strikingly, the collagenous capsule that formed in TSP2-null mice was highly vascularized and thicker than that formed in normal mice. In addition, abnormally shaped collagen fibers were observed in capsules from mutant mice. These observations indicate that the presence or absence of an extracellular matrix component, TSP2, can inf luence the nature of the FBR, in particular its vascularity. The expression of TSP2 therefore could represent a molecular target for local inhibitory measures when vascularization of the tissue surrounding an implanted device is desired.

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Reactions of Formed Elements of Blood With Plasma Proteins at Interfaces*

Cited by 148 publications

References 23 publications

Motility and Adhesiveness in Human Neutrophils

Motility and Adhesiveness in Human Neutrophils

Molecular determinants of acute inflammatory responses to biomaterials.

Mice that lack the angiogenesis inhibitor, thrombospondin 2, mount an altered foreign body reaction characterized by increased vascularity

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