Isolation, purification, and partial characterization of an autocrine periodontal ligament cell chemotactic factor.

Periodontal ligament (PDL) cells are believed to play a critically important role in the regeneration of the periodontium. We have suggested that polypeptide growth factors can enhance periodontal regeneration by stimulating PDL cell chemotaxis and mitogenesis. This manuscript describes the identification of a novel chemotactic factor isolated from human PDL cells which we named PDL-CTX. PDL-CTX induces the directed migration of human PDL cells in vitro and was found to be a more potent chemotactic agent than other known growth factors. Additionally, PDL-CTX has no chemotactic effect on gingival fibroblasts or gingival epithelial cells. Both tryptic digestion and boiling abolished PDL-CTX's biological activity. The designed purification method included Mono-S cation exchange, heparin-sepharose affinity, and microbore reverse-phase HPLC. The purified factor has a relative molecular weight of approximately 7000 daltons based on sodium dodecyl sulfate (SDS) gel analysis. The amino acid composition and partial amino acid sequence were determined from HPLC-purified material. These were determined to be unique. Further investigation of the biological functions of PDL-CTX on PDL cells and other ligament cells should help improve our understanding of ligament repair.