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The creation of an antithrombotic surface by apyrase immobilization

Nilsson, Per H. (author)
Linnéuniversitetet,Institutionen för naturvetenskap, NV,Linnaeus University
Engberg, Anna E. (author)
Linnéuniversitetet,Institutionen för naturvetenskap, NV,Linnaeus University
Bäck, Jennie (author)
Uppsala universitet,Enheten för klinisk immunologi
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Faxälv, Lars (author)
Östergötlands Läns Landsting,Linköpings universitet,Klinisk kemi,Hälsouniversitetet
Lindahl, Tomas (author)
Östergötlands Läns Landsting,Linköpings universitet,Klinisk kemi,Hälsouniversitetet
Nilsson, Bo (author)
Uppsala universitet,Enheten för klinisk immunologi
Nilsson Ekdahl, Kristina (author)
Uppsala universitet,Linnéuniversitetet,Institutionen för naturvetenskap, NV,Linnaeus University,Enheten för klinisk immunologi
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 (creator_code:org_t)
Elsevier BV, 2010
2010
English.
In: Biomaterials. - : Elsevier BV. - 0142-9612 .- 1878-5905. ; 31:16, s. 4484-4491
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Blood incompatibility reactions caused by surfaces often involve platelet activation and subsequent platelet-initiated activation of the coagulation and complement cascades. The goal of this study was to immobilize apyrase on a biomaterial surface in order to develop an enzymatically active surface that would have the capacity to inhibit platelet activation by degrading ADP. We were able to immobilize apyrase on a polystyrene surface with preservation of the enzymatic activity. We then analyzed the hemocompatibility of the apyrase surface and of control surfaces by incubation with platelet-rich plasma (PRP) or whole blood. Monitoring of markers of platelet, coagulation, and complement activation and staining of the surfaces revealed decreased levels of platelet and coagulation activation parameters on the apyrase surface. The formation of antithrombin-thrombin and antithrombin-factor XIa complexes and the extent of platelet consumption were significantly lower on the apyrase surface than on any of the control surfaces. No significant differences were seen in complement activation (C3a levels). Staining of the apyrase surface revealed low platelet adherence and no formation of granulocyte platelet complexes. These results demonstrate that it is possible to create an antithrombotic surface targeting the ADP amplification of platelet activation by immobilizing apyrase.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Immunology in the medical area (hsv//eng)

Keyword

Blood compatibiliy; Apyrase; Platelet; Platelet regulation; Adenosine diphosphate
Immunology
Immunologi
Immunologi
Immunology
Biomedical Sciences
Biomedicinsk vetenskap
MEDICINE

Publication and Content Type

ref (subject category)
art (subject category)

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