publication . Article . 2003

high binding capacity of cyclophilin b to chondrocyte heparan sulfate proteoglycans and its release from the cell surface by matrix metalloproteinases possible role as a proinflammatory mediator in arthritis

Fr�d�ric De Ceuninck; Fabrice Allain; Audrey Caliez; Genevi�ve Spik; Paul M. Vanhoutte;
  • Published: 04 Aug 2003 Journal: Arthritis & Rheumatism, volume 48, pages 2,197-2,206 (issn: 0004-3591, eissn: 1529-0131, Copyright policy)
  • Publisher: Wiley
Objective To study cyclophilin B, a protein newly identified as a secretion product of cultured chondrocytes, in the context of chondrocyte pathobiology. Methods Cyclophilin B was purified by sequential chromatographic processing of the secretion medium of cultured guinea pig chondrocytes. Its presence both at the surface of chondrocyte monolayers and in cartilage was demonstrated by immunohistochemistry. Binding sites at the surface of chondrocytes were characterized by Scatchard plot analysis using 125I-labeled cyclophilin B, and by glycosidase treatments. The release of cyclophilin B from chondrocytes by activated matrix metalloproteinases (MMPs) was studied ...
free text keywords: Immunology, Immunology and Allergy, Pharmacology (medical), Rheumatology, Chondrocyte, medicine.anatomical_structure, medicine, Extracellular matrix, Matrix metalloproteinase, Biology, Peptidylprolyl isomerase, Binding protein, Secretion, Cis-trans-Isomerases, Cartilage
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