A Shielding Topology Stabilizes the Early Stage Protein-Mineral Complexes of Fetuin-A and Calcium Phosphate: A Time-Resolved Small-Angle X-ray Study

被引：54

作者：

Rochette, Christophe N. ^{[1
]}

Rosenfeldt, Sabine ^{[1
]}

Heiss, Alexander ^{[2
]}

Narayanan, Theyencheri ^{[3
]}

Ballauff, Matthias ^{[1
]}

Jahnen-Dechent, Willi ^{[2
]}

机构：

[1] Univ Bayreuth, D-95444 Bayreuth, Germany

[2] Rhein Westfal TH Aachen, Dept Biomed Engn, Biointerface Grp, D-52074 Aachen, Germany

[3] European Synchrotron Radiat Facil, F-38043 Grenoble, France

来源：

CHEMBIOCHEM | 2009年 / 10卷 / 04期

关键词：

aggregation; biomineralization; calciprotein particles; fetuin-A; small-angle X-ray scattering (SAXS); IN-VITRO; SERUM; PRECURSOR; BRUSHITE; CACO3;

D O I：

10.1002/cbic.200800719

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We report on the earliest stages of the formation of complexes of calcium phosphate in the presence of the serum protein alpha(2)-HS glycoprotein/fetuin-A termed calciprotein particles (CPPs). Time-resolved small-angle X-ray scattering (TR-SAXS) and stopped-flow analysis were used to monitor the growth of protein mineral particles nucleating from supersaturated salt solutions. It was found that fetuin-A did not influence the formation of mineral nuclei. However, fetuin-A did prevent the aggregation of nuclei and thus mineral precipitation. Hence, fetuin-A shielded spontaneously formed mineral nuclei, leading to stable calciprotein particles in the first stage of mineralization. Fetuin-A is therefore critically required during the earliest stages of the formation of protein-mineral complexes in order to prevent uncontrolled mineralization.

引用

页码：735 / 740

页数：6

共 21 条

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