Abstract
A 24-kDa polypeptide which activated the incorporation of [3H]thymidine into human fibroblasts was isolated from the outer membrane vesicles of Porphyromonas gingivalis W50. This polypeptide, named fibroblast activating factor (FAF), was isolated by 3-[(3-cholamidopropyl)-dimethyl-ammonio]-1- propanesulfonate (CHAPS) detergent extraction and purified by DEAE ion- exchange chromatography and preparative isoelectric focusing. Purified FAF (100 ng of protein per ml) caused a 400% increase in [3H]thymidine incorporation into human gingival fibroblasts (HGFs) compared with results for controls. FAF was characterized as (i) a polypeptide with molecular masses of 24 kDa when heated at 100°C for 5 min and 44 kDa when unheated, (ii) heat sensitive but not affected by selected reducing reagents, and (iii) possessing slight phosphatase activity. N'-terminal sequence analysis revealed no homology with P. gingivalis peptides or with any host-derived growth factors. These data suggest that FAF functions as a significant virulence factor which in vivo is capable of modulating homeostasis in local connective tissues.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 588-595 |
| Number of pages | 8 |
| Journal | Infection and immunity |
| Volume | 61 |
| Issue number | 2 |
| State | Published - 1993 |
ASJC Scopus subject areas
- Parasitology
- Microbiology
- Immunology
- Infectious Diseases