Universität zu Köln

Bleuel, Judith, Zaucke, Frank, Brueggemann, Gert-Peter, Heilig, Juliane, Wolter, Marie-Louise, Hamann, Nina, Firner, Sara and Niehoff, Anja ORCID: 0000-0002-4165-0929 (2015). Moderate Cyclic Tensile Strain Alters the Assembly of Cartilage Extracellular Matrix Proteins In Vitro. J. Biomech. Eng.-Trans. ASME, 137 (6). NEW YORK: ASME. ISSN 1528-8951

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Abstract

Mechanical loading influences the structural and mechanical properties of articular cartilage. The cartilage matrix protein collagen II essentially determines the tensile properties of the tissue and is adapted in response to loading. The collagen II network is stabilized by the collagen II-binding cartilage oligomeric matrix protein (COMP), collagen IX, and matrilin-3. However, the effect of mechanical loading on these extracellular matrix proteins is not yet understood. Therefore, the aim of this study was to investigate if and how chondrocytes assemble the extracellular matrix proteins collagen II, COMP, collagen IX, and matrilin-3 in response to mechanical loading. Primary murine chondrocytes were applied to cyclic tensile strain (6%, 0.5 Hz, 30 min per day at three consecutive days). The localization of collagen II, COMP, collagen IX, and matrilin-3 in loaded and unloaded cells was determined by immunofluorescence staining. The messenger ribo nucleic acid (mRNA) expression levels and synthesis of the proteins were analyzed using reverse transcription-polymerase chain reaction (RT-PCR) and western blots. Immunofluorescence staining demonstrated that the pattern of collagen II distribution was altered by loading. In loaded chondrocytes, collagen II containing fibrils appeared thicker and strongly co-stained for COMP and collagen IX, whereas the collagen network from unloaded cells was more diffuse and showed minor costaining. Further, the applied load led to a higher amount of COMP in the matrix, determined by western blot analysis. Our results show that moderate cyclic tensile strain altered the assembly of the extracellular collagen network. However, changes in protein amount were only observed for COMP, but not for collagen II, collagen IX, or matrilin-3. The data suggest that the adaptation to mechanical loading is not always the result of changes in RNA and/or protein expression but might also be the result of changes in matrix assembly and structure.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Bleuel, Judith UNSPECIFIED UNSPECIFIED UNSPECIFIED Zaucke, Frank UNSPECIFIED UNSPECIFIED UNSPECIFIED Brueggemann, Gert-Peter UNSPECIFIED UNSPECIFIED UNSPECIFIED Heilig, Juliane UNSPECIFIED UNSPECIFIED UNSPECIFIED Wolter, Marie-Louise UNSPECIFIED UNSPECIFIED UNSPECIFIED Hamann, Nina UNSPECIFIED UNSPECIFIED UNSPECIFIED Firner, Sara UNSPECIFIED UNSPECIFIED UNSPECIFIED Niehoff, Anja UNSPECIFIED orcid.org/0000-0002-4165-0929 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-402704
DOI:	10.1115/1.4030053
Journal or Publication Title:	J. Biomech. Eng.-Trans. ASME
Volume:	137
Number:	6
Date:	2015
Publisher:	ASME
Place of Publication:	NEW YORK
ISSN:	1528-8951
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language COLLAGEN TYPE-IX; MULTIPLE EPIPHYSEAL DYSPLASIA; ARTICULAR-CARTILAGE; II COLLAGEN; DYNAMIC COMPRESSION; CHONDROCYTE AGGRECAN; GENE-EXPRESSION; MESSENGER-RNA; MATRILIN-3; METABOLISM Multiple languages Biophysics; Engineering, Biomedical Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/40270