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1.
Cells Tissues Organs ; 169(3): 248-56, 2001.
Article in English | MEDLINE | ID: mdl-11455120

ABSTRACT

Identification of a small animal model that undergoes pathological temporomandibular joint (TMJ) degeneration would represent a significant research tool. To date however, no such model has been described. We therefore have investigated the pathological and immunohistochemical features of the TMJ of a transgenic mouse that over expresses the human form of TNFalpha. The TMJ of this animal appears to undergo changes that resemble arthriditics of temporomandibular dysfunction. Furthermore, the disc and articular cells express MMP9 and IL-1. Future work should validate this animal model as one that would have utility for the study of TMJ disorders. Maintenance of connective tissues in joints such as the TMJ is a normal process that allows for the reconstitution of important anatomic features. This maintenance involves both the removal and re-synthesis of structural proteins such as collagens, elastins and proteoglycans. An imbalance in the pathways for degradation and synthesis can lead to the degeneration of joint tissues. We describe the presence of a matrix metalloproteinase, MMP9 (92-kD gelatinase), in TMJ disc and articular cells that likely function in the degradative process. Additionally, we show that this enzyme is under the control of pro-inflammatory cytokines whereby TGFbeta and IL-1 stimulate and PGE(2) inhibits its activity.


Subject(s)
Cytokines/metabolism , Matrix Metalloproteinases/metabolism , Temporomandibular Joint Disorders/metabolism , Temporomandibular Joint/metabolism , Animals , Cattle , Cytokines/pharmacology , Disease Models, Animal , Humans , Immunohistochemistry , In Vitro Techniques , Matrix Metalloproteinases/genetics , Mice , Mice, Transgenic , Models, Biological , RNA, Messenger/genetics , RNA, Messenger/metabolism , Temporomandibular Joint/pathology , Temporomandibular Joint Disorders/genetics , Temporomandibular Joint Disorders/pathology , Tumor Necrosis Factor-alpha/genetics , Tumor Necrosis Factor-alpha/metabolism
2.
Cell Adhes Commun ; 3(4): 273-81, 1995 Nov.
Article in English | MEDLINE | ID: mdl-8821030

ABSTRACT

Elastin-derived peptides (kappa-elastin: kappa E, mean molecular mass: 75 kDa), either coated onto plastic dishes or added to culture media (0.26 to 1.33 nM) stimulated the growth of human skin fibroblasts (HSF) strains obtained from different donors and tested at different cell passages (4 to 12). Coated 44.4 micrograms/cm2 insoluble elastin (iE) exhibited the same action; coated iE or kappa E significantly modifies the HSF morphology: after 5-6 days of culture, HSF are more elongated, and at preconfluence state, formation of HSF clusters surrounding iE were observed. Increased 3H thymidine incorporation and proliferative effect of HSF by kappa E (1.3 to 2.2 fold as compared to control cells) was observed after a lag phase period which raised with initial HSF density. Optimal proliferative effect was obtained at kappa E 8.5 10(-10) M, a value close to the dissociation constant (kD = 2.7 10(-10) M) of kappa E to HSF. Valine-glycine-valine-alanine-proline-glycine (VGVAPG), but not valine-glycine-valine (VGV) or Valine-glycine-valine-valine-glycine-alanine (VGVVGA) also significantly stimulated, optimally at 7.0 10(-10) M, HSF proliferation. It was concluded that the stimulatory influence of elastin derived peptides on HSF proliferation was mediated through a binding to plasmalemmal receptor of HSF.


Subject(s)
Elastin/pharmacology , Fibroblasts/cytology , Oligopeptides/pharmacology , Adult , Cell Division/drug effects , Cells, Cultured , Culture Media , Elastin/chemistry , Female , Humans , Oligopeptides/chemical synthesis , Skin/cytology
3.
Cell Biol Int ; 18(2): 111-7, 1994 Feb.
Article in English | MEDLINE | ID: mdl-8019482

ABSTRACT

Elastin-derived peptides were previously shown to influence human skin fibroblasts (HSF) chemotaxis and proliferation (Ghuysen et al., 1992). We report here that culturing HSF on kappa-elastin (kappa E) but not onto fibronectin (FN) enhanced the secretion of latent elastinolytic activity. The proteinase involved was identified as the 72 kDa gelatinase A. Moreover, HSF-kappa E as well as HSF-FN interactions modulated the secretions of Il1 induced expressions of elastinolytic activities.


Subject(s)
Elastin/metabolism , Fibronectins/metabolism , Pancreatic Elastase/metabolism , Peptide Fragments/metabolism , Skin/enzymology , Adolescent , Adult , Amino Acid Sequence , Cells, Cultured , Culture Media, Serum-Free , Endopeptidases/metabolism , Female , Fibroblasts/enzymology , Gelatinases/metabolism , Humans , Interleukin-1/metabolism , Matrix Metalloproteinase 2 , Metalloendopeptidases/metabolism , Molecular Sequence Data , Phenylmercuric Acetate/analogs & derivatives , Skin/cytology , Sulfhydryl Reagents
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