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Proteome analysis of rat serum proteins adsorbed onto synthetic octacalcium phosphate crystals.

Authors: Kaneko, H  Kamiie, J  Kawakami, H  Anada, T  Honda, Y  Shiraishi, N  Kamakura, S  Terasaki, T  Shimauchi, H  Suzuki, O 
Citation: Kaneko H, etal., Anal Biochem. 2011 Nov 15;418(2):276-85. Epub 2011 Jul 26.
Pubmed: (View Article at PubMed) PMID:21839718
DOI: Full-text: DOI:10.1016/j.ab.2011.07.022

The present study was designed to determine which proteins are selectively adsorbed onto two bone substitute materials, octacalcium phosphate (OCP) and hydroxyapatite (HA) crystals, from rat serum by proteome analysis. Ground crystals of synthetic OCP and commercially available sintered HA, with the same surface area, were incubated in rat serum proteins at 37 degrees C for 24 h. The proteins from the crystals extracted with guanidine-HCl-EDTA were listed on the basis of the results of liquid chromatography tandem mass spectrometry (LC/MS/MS). A total of 138 proteins were detected from OCP; 103 proteins were detected from HA. Forty-eight proteins were from both crystals. A quantitative analysis of the proteins detected was performed for the extracted two bone formation-related proteins apolipoprotein E (Apo E), a protein known to promote osteoblast differentiation, and complement 3 (C3). HA adsorbed C3 (3.98 +/- 0.03 fmol/mug protein) more than OCP (1.81 +/- 0.07 fmol/mug protein) did, while OCP adsorbed Apo E (2.42 +/- 0.03 fmol/mug protein) more than HA (1.21 +/- 0.01 fmol/mug protein) did even after deleting the high-abundance proteins, such as albumin. The results demonstrated that OCP exhibits a similar property but distinct capacity with HA in adsorbing bone formation-related proteins from the serum constituents.

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CRRD Object Information
CRRD ID: 6903929
Created: 2012-10-08
Species: All species
Last Modified: 2012-10-08
Status: ACTIVE



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