title: Degradation of extracellular matrix molecules in interleukin-1α treated bovine nasal cartilage.
abstract: This work aimed to show and compare the degradation time of some of cartilage extracellular matrix components using an in vitro model for cartilage degradation induced by interleukin-1α. It is known that elucidation of molecular events under Interleukin-1α induction of bovine nasal cartilage could obtain useful data to understand more about involving mechanisms for tissue breakdown in joint disease.
  
  
  
  The cartilage was taken from an adult bovine in a local slaughterhouse. After removing the whole perichondrium, the equal 2 mm diameter pieces of bovine nasal cartilage were punched out and cultured in Dulbecco's modified Eagle's medium DMEM with or without 10 ng/ml Interleukin-1α for 24 days. Each 3 days, the media were removed and exchanged by fresh media, and the removed media were stored in -20 degrees C. Sodium dodecyl sulphate/polyacrylamid-gel electrophoresis SDS-PAGE and Western-blot methods were used for analyzing the samples.
  
  
  
  The first fragment of fibromodulin (FM) was seen at day 6 and further fragments were appeared at day 18. Cartilage oligomeric matrix protein (COMP) releasing was as a successive pattern during culture period and the first fragment was found at day 6. Collagen IX fragments were seen at day 9 and in a progressive pattern until the end of the study.
  
  
  
  This study shows that FM and COMP could be considered as the suitable candidates for studying the mechanisms that participate in the cartilage degradations.
authors.affiliation: Cellular and Molecular Research Center, Dept. of Anatomical Sciences, Faculty of Medicine, Ahvaz Jundishapour University of medical Sciences, Ahvaz, Iran. behnaz.shohani@gmail.com
authors.forename: Behnaz
authors.initials: B
authors.lastname: Shohani
authors.affiliation: Cellular and Molecular Research Center, Dept. of Anatomical Sciences, Faculty of Medicine, Ahvaz Jundishapour University of medical Sciences, Ahvaz, Iran. behnaz.shohani@gmail.com
authors.forename: Mahmoud
authors.initials: M
authors.lastname: Orazizadeh
authors.affiliation: Cellular and Molecular Research Center, Dept. of Anatomical Sciences, Faculty of Medicine, Ahvaz Jundishapour University of medical Sciences, Ahvaz, Iran. behnaz.shohani@gmail.com
authors.forename: Mahmoud
authors.initials: M
authors.lastname: Hashemitabar
authors.affiliation: Dept. of Clinical Sciences, 
  Section for Molecular Skeletal Biology, BMC, Plan C12, Lund, Sweden.
authors.forename: Dick
authors.initials: D
authors.lastname: Heinegard
mesh_terms: D000818:Animals; D001172:Arthritis, Rheumatoid / Q000503:physiopathology; D015415:Biomarkers / Q000378:metabolism; D015153:Blotting, Western; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005109:Extracellular Matrix / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000032:analysis / Q000378:metabolism*; D024022:Fibrillar Collagens / Q000032:analysis / Q000378:metabolism*; D000071235:Fibromodulin; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism*; D053582:Interleukin-1alpha / Q000378:metabolism*; D064235:Matrilin Proteins; D055171:Nasal Cartilages / Q000378:metabolism*; D011509:Proteoglycans / Q000032:analysis / Q000378:metabolism*; D013997:Time Factors; D046509:Tissue Culture Techniques
chemical_list: D015415:Biomarkers; D016326:Extracellular Matrix Proteins; D024022:Fibrillar Collagens; D006023:Glycoproteins; D053582:Interleukin-1alpha; D064235:Matrilin Proteins; D011509:Proteoglycans; D000071235:Fibromodulin