TY - JOUR
T1 - Proteome analysis of rat serum proteins adsorbed onto synthetic octacalcium phosphate crystals
AU - Kaneko, Hirofumi
AU - Kamiie, Junichi
AU - Kawakami, Hirotaka
AU - Anada, Takahisa
AU - Honda, Yoshitomo
AU - Shiraishi, Naru
AU - Kamakura, Shinji
AU - Terasaki, Tetsuya
AU - Shimauchi, Hidetoshi
AU - Suzuki, Osamu
N1 - Funding Information:
This study was partially supported by Grants-in-Aid ( 17076001 , 19390490 , 20659304 , 21591910 , 23390450 , 23659999 , 23106010 ) from the Ministry of Education, Science, Sports, and Culture of Japan and Suzuken Memorial Foundation.
PY - 2011/11/15
Y1 - 2011/11/15
N2 - 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 °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/μg protein) more than OCP (1.81 ± 0.07 fmol/μg protein) did, while OCP adsorbed Apo E (2.42 ± 0.03 fmol/μg protein) more than HA (1.21 ± 0.01 fmol/μg 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.
AB - 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 °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/μg protein) more than OCP (1.81 ± 0.07 fmol/μg protein) did, while OCP adsorbed Apo E (2.42 ± 0.03 fmol/μg protein) more than HA (1.21 ± 0.01 fmol/μg 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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U2 - 10.1016/j.ab.2011.07.022
DO - 10.1016/j.ab.2011.07.022
M3 - Article
C2 - 21839718
AN - SCOPUS:80052771964
SN - 0003-2697
VL - 418
SP - 276
EP - 285
JO - Analytical Biochemistry
JF - Analytical Biochemistry
IS - 2
ER -