Serum albumin is the most prominent protein in blood, and it aids in bone fracture healing, though the manner through which enhanced healing occurs is not well understood. This study investigates the influence of calcium on the bioactivity of albumin due to the prevalence of calcium at bone injury sites. Bovine serum albumin (BSA) was exposed to varying concentrations of calcium, adsorbed to tissue culture polystyrene, and the subsequent BSA-coated surfaces were evaluated with calcium titration, and cell adhesion, viability, and binding inhibition studies. Calcium-modified BSA improved overall MC3T3-E1 osteoblast-like cell adhesion, although high calcium concentrations induced cell death. Inhibiting specific integrins revealed that without calcium exposure, cell binding to BSA was primarily mediated by integrins that typically bind to the GFOGER sequence of collagen. As calcium exposure increases, the primary binding interaction transitioned to integrins known to bind RGD. However, cell binding to calcium-modified BSA was not completely eliminated during the inhibition studies indicating additional unidentified binding interactions occur. Overall, these results suggest that the exposure to calcium induces conformational changes that affect the cell-binding bioactivity of BSA, which may explain the beneficial impact of albumin in bone tissue.
Keywords: MC3T3-E1 adhesion; albumin; calcium; integrin binding; tissue engineering.
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