Universität zu Köln

Sastre, E. Andres, Maly, K., Zhu, M., Witte-Bouma, J., Trompet, D., Boehm, A. M., Brachvogel, B., van Nieuwenhoven, C. A., Maes, C., van Osch, G. J. V. M., Zaucke, F. and Farrell, E. (2021). Spatiotemporal distribution of thrombospondin-4 and-5 in cartilage during endochondral bone formation and repair. Bone, 150. NEW YORK: ELSEVIER SCIENCE INC. ISSN 1873-2763

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Abstract

During skeletal development most bones are first formed as cartilage templates, which are gradually replaced by bone. If later in life those bones break, temporary cartilage structures emerge to bridge the fractured ends, guiding the regenerative process. This bone formation process, known as endochondral ossification (EO), has been widely studied for its potential to reveal factors that might be used to treat patients with large bone defects. The extracellular matrix of cartilage consists of different types of collagens, proteoglycans and a variety of noncollagenous proteins that organise the collagen fibers in complex networks. Thrombospondin-5, also known as cartilage oligomeric matrix protein (TSP-5/COMP) is abundant in cartilage, where it has been described to enhance collagen fibrillogenesis and to interact with a variety of growth factors, matrix proteins and cellular receptors. However, very little is known about the skeletal distribution of its homologue thrombospondin-4 (TSP4). In our study, we compared the spatiotemporal expression of TSP-5 and TSP-4 during postnatal bone formation and fracture healing. Our results indicate that in both these settings, TSP-5 distributes across all layers of the transient cartilage, while the localisation of TSP-4 is restricted to the population of hypertrophic chondrocytes. Furthermore, in fractured bones we observed TSP-4 sparsely distributed in the periosteum, while TSP-5 was absent. Last, we analysed the chemoattractant effects of the two proteins on endothelial cells and bone marrow stem cells and hypothesised that, of the two thrombospondins, only TSP-4 might promote blood vessel invasion during ossification. We conclude that TSP-4 is a novel factor involved in bone formation. These findings reveal TSP-4 as an attractive candidate to be evaluated for bone tissue engineering purposes.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Sastre, E. Andres UNSPECIFIED UNSPECIFIED UNSPECIFIED Maly, K. UNSPECIFIED UNSPECIFIED UNSPECIFIED Zhu, M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Witte-Bouma, J. UNSPECIFIED UNSPECIFIED UNSPECIFIED Trompet, D. UNSPECIFIED UNSPECIFIED UNSPECIFIED Boehm, A. M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Brachvogel, B. UNSPECIFIED UNSPECIFIED UNSPECIFIED van Nieuwenhoven, C. A. UNSPECIFIED UNSPECIFIED UNSPECIFIED Maes, C. UNSPECIFIED UNSPECIFIED UNSPECIFIED van Osch, G. J. V. M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Zaucke, F. UNSPECIFIED UNSPECIFIED UNSPECIFIED Farrell, E. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-589875
DOI:	10.1016/j.bone.2021.115999
Journal or Publication Title:	Bone
Volume:	150
Date:	2021
Publisher:	ELSEVIER SCIENCE INC
Place of Publication:	NEW YORK
ISSN:	1873-2763
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language OLIGOMERIC MATRIX PROTEIN; GENE-EXPRESSION; COMP; ANGIOGENESIS; ACTIVATION; CELLS; MICE; STEM Multiple languages Endocrinology & Metabolism Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/58987