Adsorption of human salivary proteins to titanium powder. I. Adsorption of human salivary albumin.

Titanium (Ti) is among the most widely used implant materials in dentistry today. The success of Ti implants is associated with their interactions with the surrounding tissues and biological fluids. In the present study, the adsorption of salivary proteins to Ti and the effect of calcium (Ca) on this process were investigated. Untreated and Ca-treated Ti powders were suspended in human clarified whole saliva. After incubation, the supernatant fluid was collected for protein analysis. The powders were then washed and resuspended in EDTA to desorb proteins from Ti surfaces. Sodium dodecylsulphate polyacrylamide gel electrophoresis and Bradford protein assay were conducted to determine the concentration and type of proteins that adsorbed onto Ti surfaces. The presence of Ca ions enhanced the adsorption of salivary proteins to Ti. A 66 kDa protein, identified by immunoblotting as albumin, was found as the main adsorbed salivary protein. Adsorption of albumin to Ti pretreated with Ca was significantly greater than to native Ti. The Ca-dependent adsorption process was reversed by EDTA. The data suggest that salivary albumin is one of the main constituents of a salivary biofilm formed on Ti dental implants and its adsorption to Ti surfaces is Ca-dependent. The presence of albumin on Ti dental implants may affect plaque accumulation on the implants and the biocompatibility of Ti implants.

[1]  R. Meffert,et al.  Dental implants: a review. , 1992, Journal of periodontology.

[2]  D. I. Hay,et al.  Human salivary acidic proline-rich proteins and statherin promote the attachment of Actinomyces viscosus LY7 to apatitic surfaces , 1988, Infection and immunity.

[3]  Newman Mg,et al.  A study of in vitro attachment of Streptococcus sanguis and Actinomyces viscosus to saliva-treated titanium. , 1989 .

[4]  D. I. Hay,et al.  Adhesive properties of strains of Fusobacterium nucleatum of the subspecies nucleatum, vincentii and polymorphum. , 1991, Oral microbiology and immunology.

[5]  R. Ellen,et al.  Adhesion of Actinomyces viscosus to Porphyromonas (Bacteroides) gingivalis-coated hexadecane droplets , 1991, Journal of bacteriology.

[6]  E. Veerman,et al.  Protein, albumin and cystatin concentrations in saliva of healthy subjects and of patients with gingivitis or periodontitis. , 1993, Journal of periodontal research.

[7]  J. Ellingsen,et al.  A study on the mechanism of protein adsorption to TiO2. , 1991, Biomaterials.

[8]  H. Busscher,et al.  A transmission electron microscopy study of the adsorption patterns of early developing artificial pellicles on human enamel. , 1989, Archives of oral biology.

[9]  W. Bowen,et al.  Adhesion of Actinomyces Isolates to Experimental Pellicles , 1993, Journal of dental research.

[10]  C. Lavelle Applied physiology of the mouth , 1975 .

[11]  L. Tabak,et al.  Adherence of Streptococcus sanguis to salivary mucin bound to glass. , 1982, Journal of dental research.

[12]  J. van Houte,et al.  On the formation of dental plaques. , 1973, Journal of periodontology.

[13]  D. Beighton,et al.  Proteolytic activity of oral streptococci. , 1990, FEMS microbiology letters.

[14]  R. Genco,et al.  Synthetic peptides analogous to the fimbrillin sequence inhibit adherence of Porphyromonas gingivalis , 1992, Infection and immunity.

[15]  R. Gibbons,et al.  Bacterial adherence in oral microbial ecology. , 1975, Annual review of microbiology.

[16]  M. Edgerton,et al.  Characterization of acquired denture pellicle from healthy and stomatitis patients. , 1992, The Journal of prosthetic dentistry.

[17]  P. Gjermo,et al.  An in vivo model for the identification of serum proteins in the acquired subgingival pellicle. , 1991, Journal of clinical periodontology.

[18]  H. Towbin,et al.  Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[19]  M. Cannon,et al.  Quantitative study of the interaction of salivary acidic proline-rich proteins with hydroxyapatite. , 1978, Caries research.

[20]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[21]  G. Embery,et al.  Adsorption of glycosaminoglycans to commercially pure titanium. , 1992, Biomaterials.

[22]  S. Abrams,et al.  The role of human salivary acidic proline-rich proteins in the formation of acquired dental pellicle in vivo and their fate after adsorption to the human enamel surface. , 1983, Archives of oral biology.

[23]  W. Bowen,et al.  Identification of IgA, IgG, lysozyme, albumin, alpha-amylase and glucosyltransferase in the protein layer adsorbed to hydroxyapatite from whole saliva. , 1983, Scandinavian journal of dental research.