title: Response of human engineered cartilage based on articular or nasal chondrocytes to interleukin-1β and low oxygen.
abstract: Previous studies showed that human nasal chondrocytes (HNC) exhibit higher proliferation and chondrogenic capacity as compared to human articular chondrocytes (HAC). To consider HNC as a relevant alternative cell source for the repair of articular cartilage defects it is necessary to test how these cells react when exposed to environmental factors typical of an injured joint. We thus aimed this study at investigating the responses of HNC and HAC to exposure to interleukin (IL)-1β and low oxygen. For this purpose HAC and HNC harvested from the same donors (N=5) were expanded in vitro and then cultured in pellets or collagen-based scaffolds at standard (19%) or low oxygen (5%) conditions. Resulting tissues were analyzed after a short (3 days) exposure to IL-1β, mimicking the initially inflammatory implantation site, or following a recovery time (1 or 2 weeks for pellets and scaffolds, respectively). After IL-1β treatment, constructs generated by both HAC and HNC displayed a transient loss of GAG (up to 21.8% and 36.8%, respectively) and, consistently, an increased production of metalloproteases (MMP)-1 and -13. Collagen type II and the cryptic fragment of aggrecan (DIPEN), both evaluated immunohistochemically, displayed a trend consistent with GAG and MMPs production. HNC-based constructs exhibited a more efficient recovery upon IL-1β withdrawal, resulting in a higher accumulation of GAG (up to 2.6-fold) compared to the corresponding HAC-based tissues. On the other hand, HAC displayed a positive response to low oxygen culture, while HNC were only slightly affected by oxygen percentage. Collectively, under the conditions tested mimicking the postsurgery articular environment, HNC retained a tissue-forming capacity, similar or even better than HAC. These results represent a step forward in validating HNC as a cell source for cartilage tissue engineering strategies.
authors: Departments of Surgery and of Biomedicine, University Hospital Basel, Basel, Switzerland.
authors: Celeste
authors: C
authors: Scotti
authors: Andrea
authors: A
authors: Osmokrovic
authors: Francine
authors: F
authors: Wolf
authors: Sylvie
authors: S
authors: Miot
authors: Giuseppe M
authors: GM
authors: Peretti
authors: Andrea
authors: A
authors: Barbero
authors: Ivan
authors: I
authors: Martin
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D064236:Cartilage Oligomeric Matrix Protein; D002358:Cartilage, Articular / Q000166:cytology* / Q000187:drug effects / Q000502:physiology; D002478:Cells, Cultured; D019902:Chondrocytes / Q000166:cytology* / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D024043:Collagen Type II / Q000378:metabolism; D000939:Epitopes / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D005260:Female; D006023:Glycoproteins / Q000378:metabolism; D006025:Glycosaminoglycans / Q000378:metabolism; D006801:Humans; D053583:Interleukin-1beta / Q000494:pharmacology*; D008297:Male; D064235:Matrilin Proteins; D020782:Matrix Metalloproteinases / Q000378:metabolism; D008875:Middle Aged; D009666:Nose / Q000166:cytology*; D010100:Oxygen / Q000494:pharmacology*; D023822:Tissue Engineering / Q000379:methods*; D054457:Tissue Scaffolds / Q000737:chemistry
chemical_list: D064236:Cartilage Oligomeric Matrix Protein; D024043:Collagen Type II; D000939:Epitopes; D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D006025:Glycosaminoglycans; D053583:Interleukin-1beta; D064235:Matrilin Proteins; C577553:TSP5 protein, human; D020782:Matrix Metalloproteinases; D010100:Oxygen