| Hauptseite > Publikationsdatenbank > Fetuin-A is a mineral carrier protein: Small angle neutron scattering provides new insight on Fetuin-A controlled calcification inhibition > print |
| 001 | 13705 | ||
| 005 | 20240619092021.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21156141 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC3000477 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bpj.2010.10.030 |
| 024 | 7 | _ | |2 WOS |a WOS:000285438900022 |
| 024 | 7 | _ | |2 MLZ |a HeissPJS2010 |
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| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Heiss, A. |b 0 |
| 245 | _ | _ | |a Fetuin-A is a mineral carrier protein: Small angle neutron scattering provides new insight on Fetuin-A controlled calcification inhibition |
| 260 | _ | _ | |a New York, NY |b Rockefeller Univ. Press |c 2010 |
| 300 | _ | _ | |a 3986 - 3995 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 882 |a Biophysical Journal |v 99 |x 0006-3495 |y 12 |
| 500 | _ | _ | |a This 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. |
| 520 | _ | _ | |a Clinical 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. |
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| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Calcification, Physiologic |
| 650 | _ | 2 | |2 MeSH |a Calcium: metabolism |
| 650 | _ | 2 | |2 MeSH |a Calcium Phosphates: metabolism |
| 650 | _ | 2 | |2 MeSH |a Carrier Proteins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Cattle |
| 650 | _ | 2 | |2 MeSH |a Colloids |
| 650 | _ | 2 | |2 MeSH |a Minerals: metabolism |
| 650 | _ | 2 | |2 MeSH |a Neutron Diffraction |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 2 | |2 MeSH |a Scattering, Small Angle |
| 650 | _ | 2 | |2 MeSH |a Time Factors |
| 650 | _ | 2 | |2 MeSH |a Ultrafiltration |
| 650 | _ | 2 | |2 MeSH |a alpha-Fetoproteins: metabolism |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Calcium Phosphates |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Carrier Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Colloids |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Minerals |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a alpha-Fetoproteins |
| 650 | _ | 7 | |0 7440-70-2 |2 NLM Chemicals |a Calcium |
| 650 | _ | 7 | |2 WoSType |a J |
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