Characterization of Collagenous Matrix Assembly in a Chondrocyte Model System

Sorcha Yingst, Boise State University
Kaci Bloxham, Boise State University
Lisa R. Warner, Boise State University
Raquel J. Brown, Boise State University
Jennifer Cole, Boise State University
Linda Kenoyer, Boise State University
William B. Knowlton, Boise State University
Julia T. Oxford, Boise State University

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Journal of Biomedical Materials Research Part A, Volume 90A, Issue 1, 247–255. DOI: 10.1002/jbm.a.32078

Abstract

Collagen is a major component of the newly synthesized pericellular microenvironment of chondrocytes. Collagen types II, IX, and XI are synthesized and assembled into higher ordered complexes by a mechanism in which type XI collagen plays a role in nucleation of new fibrils, and in limiting fibril diameter. This study utilizes a cell line derived from the Swarm rat chondrosarcoma that allows the accumulation and assembly of pericellular matrix. Immunofluorescence and atomic force microscopy were used to assess early intermediates of fibril formation. Results indicate that this cell line synthesizes and secretes chondrocyte-specific pericellular matrix molecules including types II, IX, and XI collagen and is suitable for the study of newly synthesized collagen matrix under the experimental conditions used. AFM data indicate that small fibrils or assemblies of microfibrils are detectable and may represent precursors of the ∼20 nm thin fibrils reported in cartilage. Treatment with hyaluronidase indicates that the dimensions of the small fibrils may be dependent upon the presence of hyaluronan within the matrix. This study provides information on the composition and organization of the newly synthesized extracellular matrix that plays a role in establishing the material properties and performance of biological materials such as cartilage.