Acidic glycoproteins accumulate in calcified areas of bioprosthetic tissue

This study was performed to evaluate the role of collagen fibrils, cellular elements and matrix proteins in calcification of glutaraldehyde (GA)-fixed bioprosthetic material.

Lyoplant (lyophilized bovine pericardium, type I collagen) was processed according to three protocols. DF-group (double fixation): after conventional fixation in GA (0.5% for 72 h; storage 0.25%) Lyoplant was implanted subcutaneously into rats for 5 days. Specimens were explanted and re-fixed (conventional fixation), followed by autologous or homologous reimplantation in rats for 21 or 63 days. CF-group (conventional fixation): Lyoplant patches were conventionally fixed (as DF-group), kept in 0.9% saline for one week, and then autologously and homologously reimplanted. GF-group (high-concentration GA): Lyoplant patches were processed (as GF-group) but 0.5% GA was used for tissue storage. Explanted specimens were studied by light microscopic histochemistry; calcium contents were measured by atomic absorption spectroscopy.

Severe calcification occurred in the DF-group without differences between autologous and homologous reimplantation. In CF- and GF-groups, calcification was negligible, but immunologic response against homologous implants was accompanied by increased calcium content. Histologic characterization of matrix material in calcified areas revealed oxyphilic glycoproteins, identified as sialoglycans.

Modification of extracellular matrix by GA is assumed as essential to cause calcification of bioprosthetic material. Calcium deposition and accumulation of sialoglycans are simultaneous events. A specific role of this glycoprotein for calcification has to be considered.