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000013705 0247_ $$2DOI$$a10.1016/j.bpj.2010.10.030
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000013705 084__ $$2WoS$$aBiophysics
000013705 1001_ $$0P:(DE-HGF)0$$aHeiss, A.$$b0
000013705 245__ $$aFetuin-A is a mineral carrier protein: Small angle neutron scattering provides new insight on Fetuin-A controlled calcification inhibition
000013705 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2010
000013705 300__ $$a3986 - 3995
000013705 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000013705 440_0 $$0882$$aBiophysical Journal$$v99$$x0006-3495$$y12
000013705 500__ $$aThis study was supported by the German Research Foundation (Deutsche Forschungsgemeinschaft) within the priority program "Principles of Biomineralization. A. Heiss thanks Prof. J. Mayer (GFE, Rheinisch-Westfalische Technische Hochschule, Aachen University) for supporting the project.
000013705 520__ $$aClinical studies and animal experiments have shown that the serum protein fetuin-A is a highly effective inhibitor of soft tissue calcification. This inhibition mechanism was elucidated on the basis of an in vitro fetuin-A-mineral model system. In a previous study, we found that in a two-stage process ∼100-nm sized calciprotein particles (CPPs) were formed whose final stage was stabilized by a compact outer fetuin-A monolayer against further growth. Quantitative small-angle neutron scattering data analysis revealed that even at a fetuin-A concentration close to the stability limit, only approximately one-half of the mineral ions and only 5% of the fetuin-A were contained in the CPPs. To uncover the interplay of the remaining supersaturated mineral ion fraction and of the 95% non-CPP fetuin-A, we explored the fetuin-A monomer fraction in solution by contrast variation small-angle neutron scattering. Our results suggest that the mineral ions coalesce to subnanometer-sized clusters, reminiscent of Posner clusters, which are stabilized by fetuin-A monomers. Hence, our experiments revealed a second mechanism of long-term mineral ion stabilization by the fetuin-A that is complementary to the formation of CPPs.
000013705 536__ $$0G:(DE-Juel1)FUEK415$$2G:(DE-HGF)$$aGroßgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)$$cP55$$x0
000013705 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000013705 588__ $$aDataset connected to Web of Science, Pubmed
000013705 650_2 $$2MeSH$$aAnimals
000013705 650_2 $$2MeSH$$aCalcification, Physiologic
000013705 650_2 $$2MeSH$$aCalcium: metabolism
000013705 650_2 $$2MeSH$$aCalcium Phosphates: metabolism
000013705 650_2 $$2MeSH$$aCarrier Proteins: metabolism
000013705 650_2 $$2MeSH$$aCattle
000013705 650_2 $$2MeSH$$aColloids
000013705 650_2 $$2MeSH$$aMinerals: metabolism
000013705 650_2 $$2MeSH$$aNeutron Diffraction
000013705 650_2 $$2MeSH$$aProtein Binding
000013705 650_2 $$2MeSH$$aScattering, Small Angle
000013705 650_2 $$2MeSH$$aTime Factors
000013705 650_2 $$2MeSH$$aUltrafiltration
000013705 650_2 $$2MeSH$$aalpha-Fetoproteins: metabolism
000013705 650_7 $$00$$2NLM Chemicals$$aCalcium Phosphates
000013705 650_7 $$00$$2NLM Chemicals$$aCarrier Proteins
000013705 650_7 $$00$$2NLM Chemicals$$aColloids
000013705 650_7 $$00$$2NLM Chemicals$$aMinerals
000013705 650_7 $$00$$2NLM Chemicals$$aalpha-Fetoproteins
000013705 650_7 $$07440-70-2$$2NLM Chemicals$$aCalcium
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000013705 693__ $$0EXP:(DE-MLZ)KWS2-20140101$$1EXP:(DE-MLZ)FRMII-20140101$$5EXP:(DE-MLZ)KWS2-20140101$$6EXP:(DE-MLZ)NL3ao-20140101$$aForschungs-Neutronenquelle Heinz Maier-Leibnitz$$eKWS-2: Small angle scattering diffractometer$$fNL3ao$$x0
000013705 7001_ $$0P:(DE-Juel1)VDB4339$$aPipich, V.$$b1$$uFZJ
000013705 7001_ $$0P:(DE-HGF)0$$aJahnen-Dechent, W.$$b2
000013705 7001_ $$0P:(DE-Juel1)130962$$aSchwahn, D.$$b3$$uFZJ
000013705 773__ $$0PERI:(DE-600)1477214-0$$a10.1016/j.bpj.2010.10.030$$gVol. 99, p. 3986 - 3995$$p3986 - 3995$$q99<3986 - 3995$$tBiophysical journal$$v99$$x0006-3495$$y2010
000013705 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3000477
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