Gingival crevicular fluid fibronectin degradation in periodontal health and disease

Abstract

Abstract— The molecular forms of fibronectin (FN) in gingival crevicular fluid of five subjects with at least two sites exhibiting clinical signs of inflammation and pockets of at least 4 mm (test group) and five subjects with clinically healthy periodontium (control group) were investigated. Samples were collected with standard filter paper strips. In the test group samples from both diseased and healthy sites were collected. After collection the test group received one episode of periodontal treatment (scaling and root planing). The sampling and clinical recordings were repeated for the diseased sites after about 2 wk. The crevicular fluid FN was analyzed using sodium dodecyl sulphate gel electrophoresis followed by western blotting with polyclonal antibodies against FN. Both intact FN and FN fragments were found in all samples. A larger proportion of FN was in degraded form in the diseased sites than in the healthy or the treated sites. FN was also degraded into smaller peptide fragments in the diseased than in the treated sites. These results suggest that crevicular fluid FN is partially degraded both in periodontal health and disease and that the degree of degradation of FN increases with periodontal inflammation and decreases with periodontal treatment.

JNK1 and JNK2 Oppositely Regulate p53 in Signaling Linked to Apoptosis Triggered by an Altered Fibronectin Matrix

“…Degraded matrix conveys messages that are different from those normally conveyed by an intact or stable matrix, and the degradation increases with the severity of the disease. In periodontal disease and arthritis, FN fragments are most abundant in the most diseased sites (6,(25)(26)(27)(28)(29)(30). Previously, we found that a proteolytic 40-kDa fragment of FN associated with the most advanced disease also induced apoptosis of periodontal ligament fibroblasts in vitro by down-regulating p53 and c-Myc (6, 7).…”

Mutations in the Heparin Binding Domain of Fibronectin in Cooperation with the V Region Induce Decreases in pp125 Levels Plus Proteoglycan-mediated Apoptosis via Caspases

“…In addition, these data further support the idea that intact FN has functions distinct from those of its fragments, which may have profound implications for wound-healing dynamics and inflammatory diseases. In periodontal disease, for example, inflammatory cytokines and bacterial products would stimulate fibroblasts of the periodontium to express greater amounts of matrix metalloproteinases (44), which in turn would degrade the extracellular matrix, thereby generating FN fragments (8,9). From our own studies and those of others, we know that FN fragments can on their own also induce elevated matrix metalloproteinase expression (1, 2) and tissue destruction in vitro (3) and suppress cell proliferation and chemotaxis (45), functions not normally observed with intact FN.…”

“…For example, the central cell binding domain of FN (FN 120) induces rabbit synovial fibroblasts (1) and human fibroblasts (2) to express elevated levels of matrix metalloproteinases, whereas fragments from the amino-terminal and gelatin binding domains induce chondrolysis in vitro, the latter effect presumably through matrix metalloproteinase and serine proteinase induction (3,4). These FN fragments are also associated with chronic inflammatory states in vivo, since high levels of such fragments have been found in synovial fluids from arthritic patients (5-7) and in gingival crevicular fluid from patients with periodontitis (8,9).…”

Specific Pro‐Apoptotic Fibronectin Fragments Modulate Proteinase Expression in Periodontal Ligament Cells

“…3,4 One of the ECM breakdown products in periodontitis is fibronectin (FN) and its fragments. 5 FN is a 450-kDa glycoprotein composed of several functional domains ( Fig. 1) and alternatively spliced regions that mediate multiple cell functions by interacting with cell-surface integrin and proteoglycan receptors and with other ECM proteins.…”