PMID- 26968213 OWN - NLM STAT- MEDLINE DCOM- 20161013 LR - 20231111 IS - 1559-4106 (Electronic) IS - 1934-8630 (Print) IS - 1559-4106 (Linking) VI - 11 IP - 2 DP - 2016 Jun 11 TI - Differential surface activation of the A1 domain of von Willebrand factor. PG - 029803 LID - 10.1116/1.4943618 [doi] LID - 029803 AB - The clotting protein von Willebrand factor (VWF) binds to platelet receptor glycoprotein Ibalpha (GPIbalpha) when VWF is activated by chemicals, high shear stress, or immobilization onto surfaces. Activation of VWF by surface immobilization is an important problem in the failure of cardiovascular implants, but is poorly understood. Here, the authors investigate whether some or all surfaces can activate VWF at least in part by affecting the orientation or conformation of the immobilized GPIbalpha-binding A1 domain of VWF. Platelets binding to A1 adsorbed onto polystyrene surfaces translocated rapidly at moderate and high flow, but detached at low flow, while platelets binding to A1 adsorbed onto glass or tissue-culture treated polystyrene surfaces translocated slowly, and detached only at high flow. Both x-ray photoelectron spectroscopy and conformation independent antibodies reported comparable A1 amounts on all surfaces. Time-of-flight secondary ion mass spectrometry (ToF-SIMS) and near-edge x-ray absorption fine structure spectra suggested differences in orientation on the three surfaces, but none that could explain the biological data. Instead, ToF-SIMS data and binding of conformation-dependent antibodies were consistent with the stabilization of an alternative more activated conformation of A1 by tissue culture polystyrene and especially glass. These studies demonstrate that different material surfaces differentially affect the conformation of adsorbed A1 domain and its biological activity. This is important when interpreting or designing in vitro experiments with surface-adsorbed A1 domain, and is also of likely relevance for blood-contacting biomaterials. FAU - Tronic, Elaine H AU - Tronic EH AD - Department of Bioengineering, University of Washington, Seattle, Washington 98195. FAU - Yakovenko, Olga AU - Yakovenko O AD - Department of Bioengineering, University of Washington, Seattle, Washington 98195. FAU - Weidner, Tobias AU - Weidner T AD - Department of Bioengineering, University of Washington, Seattle, Washington 98195. FAU - Baio, Joe E AU - Baio JE AD - Department of Chemical Engineering, University of Washington, Seattle, Washington 98195. FAU - Penkala, Rebecca AU - Penkala R AD - Department of Bioengineering, University of Washington, Seattle, Washington 98195. FAU - Castner, David G AU - Castner DG AD - Departments of Bioengineering and Chemical Engineering, University of Washington, Seattle, Washington 98195. FAU - Thomas, Wendy E AU - Thomas WE AD - Department of Bioengineering, University of Washington, Seattle, Washington 98195. LA - eng GR - P41 EB002027/EB/NIBIB NIH HHS/United States GR - R01 HL106074/HL/NHLBI NIH HHS/United States GR - 1R01 HL106074/HL/NHLBI NIH HHS/United States GR - EB-002027/EB/NIBIB NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, U.S. Gov't, Non-P.H.S. DEP - 20160611 PL - United States TA - Biointerphases JT - Biointerphases JID - 101275679 RN - 0 (Platelet Glycoprotein GPIb-IX Complex) RN - 0 (Polystyrenes) RN - 0 (von Willebrand Factor) SB - IM MH - Blood Platelets/*physiology MH - *Cell Adhesion MH - Glass MH - Humans MH - Platelet Glycoprotein GPIb-IX Complex/*metabolism MH - Polystyrenes MH - Protein Binding MH - Protein Structure, Tertiary MH - *Surface Properties MH - von Willebrand Factor/*metabolism PMC - PMC4788635 EDAT- 2016/03/13 06:00 MHDA- 2016/10/14 06:00 PMCR- 2016/03/11 CRDT- 2016/03/13 06:00 PHST- 2016/03/13 06:00 [entrez] PHST- 2016/03/13 06:00 [pubmed] PHST- 2016/10/14 06:00 [medline] PHST- 2016/03/11 00:00 [pmc-release] AID - 1.4943618 [pii] AID - 329602BIP [pii] AID - 10.1116/1.4943618 [doi] PST - epublish SO - Biointerphases. 2016 Jun 11;11(2):029803. doi: 10.1116/1.4943618.