This title appears in the Scientific Report :
2010
Please use the identifier:
http://dx.doi.org/10.1016/j.bpj.2010.10.030 in citations.
Fetuin-A is a mineral carrier protein: Small angle neutron scattering provides new insight on Fetuin-A controlled calcification inhibition
Fetuin-A is a mineral carrier protein: Small angle neutron scattering provides new insight on Fetuin-A controlled calcification inhibition
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 proce...
Saved in:
Personal Name(s): | Heiss, A. |
---|---|
Pipich, V. / Jahnen-Dechent, W. / Schwahn, D. | |
Contributing Institute: |
JCNS; JCNS Streumethoden; IFF-4 Neutronenstreuung; IFF-5 |
Published in: | Biophysical journal, 99 (2010) S. 3986 - 3995 |
Imprint: |
New York, NY
Rockefeller Univ. Press
2010
|
Physical Description: |
3986 - 3995 |
DOI: |
10.1016/j.bpj.2010.10.030 |
PubMed ID: |
21156141 |
Document Type: |
Journal Article |
Research Program: |
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI) |
Series Title: |
Biophysical Journal
99 |
Subject (ZB): | |
Publikationsportal JuSER |
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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. | ||
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 | |
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650 | 7 | |0 0 |2 NLM Chemicals |a Colloids | |
650 | 7 | |0 0 |2 NLM Chemicals |a Minerals | |
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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. | ||
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