Event Title
Extracellular Matrix Protection Factor-2 Reduces Collagen Degradation in Primary Serum-Free Cultures of Inflamed Human Gingival Fibroblasts
Location
Philadelphia, PA
Start Date
9-5-2018 1:00 PM
Description
Periodontal disease affects nearly everyone over the age of 30. The disease includes inflammation of the gum tissue surrounding the teeth and collagen degradation in the extracellular matrix (ECM). We have developed a novel enzyme inhibitor, Extracellular Matrix Protection Factor-2 (ECPF-2), that can reversibly interfere with matrix metalloprotease-8’s (MMP-8) digestion of collagen type 1. Serum-free, primary cultures of human gingival fibroblasts (HGVF) isolated from tissue removed during oral surgery were established. The tissue was collected from a patient population that included (a) non-inflamed, non-
smokers, (b) inflamed non-smokers, (c) inflamed previous smokers and (d) inflamed current smokers. The ECM of these cultures was tested for collagen degradation via an immunosorbence assay. Cells isolated from non-inflamed tissue produced 2.56ng/culture degraded collagen, while inflamed tissue produced an
average of 8.11ng/culture. In addition, cultures of inflamed gingival fibroblasts prepared from a current smoker produced the most degraded collagen per culture (9.83ng/culture current smoker, 7.90ng/culture previous smoker and 6.64ng/culture non-smoker). Treatment for 24 hours with 5ug ECPF-2 reduced the amount of degraded collagen produced in HGVF cultures isolated from the inflamed current smoker by 15%. These data support the therapeutic potential of ECPF-2 to slow degradation of gingival tissue associated with periodontal disease.
Embargo Period
5-30-2018
Extracellular Matrix Protection Factor-2 Reduces Collagen Degradation in Primary Serum-Free Cultures of Inflamed Human Gingival Fibroblasts
Philadelphia, PA
Periodontal disease affects nearly everyone over the age of 30. The disease includes inflammation of the gum tissue surrounding the teeth and collagen degradation in the extracellular matrix (ECM). We have developed a novel enzyme inhibitor, Extracellular Matrix Protection Factor-2 (ECPF-2), that can reversibly interfere with matrix metalloprotease-8’s (MMP-8) digestion of collagen type 1. Serum-free, primary cultures of human gingival fibroblasts (HGVF) isolated from tissue removed during oral surgery were established. The tissue was collected from a patient population that included (a) non-inflamed, non-
smokers, (b) inflamed non-smokers, (c) inflamed previous smokers and (d) inflamed current smokers. The ECM of these cultures was tested for collagen degradation via an immunosorbence assay. Cells isolated from non-inflamed tissue produced 2.56ng/culture degraded collagen, while inflamed tissue produced an
average of 8.11ng/culture. In addition, cultures of inflamed gingival fibroblasts prepared from a current smoker produced the most degraded collagen per culture (9.83ng/culture current smoker, 7.90ng/culture previous smoker and 6.64ng/culture non-smoker). Treatment for 24 hours with 5ug ECPF-2 reduced the amount of degraded collagen produced in HGVF cultures isolated from the inflamed current smoker by 15%. These data support the therapeutic potential of ECPF-2 to slow degradation of gingival tissue associated with periodontal disease.