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Extracellular Matrix Protection Factor‐2 Reduces Collagen Degradation in Primary Serum‐Free Cultures of Inflamed Human Gingival Fibroblasts
Author(s) -
Chmielewski Sarah,
Mattioli Patrisia,
Isaac Tamika,
Buckley Andrea Lynn,
Seutter Sara,
Gambardella Eric,
Green Kevan,
Shamseddin Seyed,
Borghaei Ruth,
Selim Abdulhafez,
D'Angelo Marina
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.640.5
Subject(s) - collagenase , extracellular matrix , fibroblast , matrix metalloproteinase , type i collagen , extracellular , chemistry , cell culture , population , matrix (chemical analysis) , pathology , microbiology and biotechnology , medicine , biology , biochemistry , in vitro , enzyme , environmental health , chromatography , genetics
Some form of periodontal disease affects nearly everyone over the age of 30. The hallmarks of periodontal disease include inflammation of the gum tissue surrounding the teeth and concomitant collagen degradation in the extracellular matrix of gingival fibroblasts. Our laboratory has developed a novel enzyme inhibitor, Extracellular Matrix Protection Factor‐2 (ECPF‐2), that can reversibly interfere with the collagenase, matrix metalloprotease‐8 (MMP‐8), and its ability to digest its substrate, collagen type I. Serum‐free, primary cultures of human gingival fibroblasts (HGVF) isolated from tissue removed during oral surgery were established (passages 1 through 4). 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 cell layer and associated extracellular matrix of these cultures was tested for collagen degradation utilizing an immunosorbence assay that measures degradation fragments generated when collagenase digests fibrillar collagen type I. Cells isolated from noninflamed tissue produced 2.56ng/culture degraded collagen, while inflamed tissue produced an average of 8.11 ng/culture. When smoking was considered as a factor, cultures of inflamed gingival fibroblasts prepared from a current smoker produced the most degraded collagen per culture (9.83 ng/culture current smoker, 7.90 ng/culture previous smoker and 6.64 ng/culture non‐smoker). Treatment for 24 hours with 5 ug ECPF‐2 reduced the amount of degraded collagen produced in gingival fibroblast cultures isolated from the inflamed current smoker by 15% (9.80 ng/culture untreated versus 8.45 ng/culture ECPF‐2 treated). These data support the therapeutic potential of ECPF‐2 to slow degradation of gingival tissue associated with periodontal disease Support or Funding Information Center for Chronic Disorders of Aging Pilot Grant and PCOM's Division of Research This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .