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. 2008 Jul;466(7):1577-82.
doi: 10.1007/s11999-008-0255-y. Epub 2008 Apr 19.

Collagens, proteoglycans, MMP-2, MMP-9 and TIMPs in human achilles tendon rupture

Evgenia Karousou  1 , Mario Ronga, Davide Vigetti, Alberto Passi, Nicola Maffulli
Affiliations

Collagens, proteoglycans, MMP-2, MMP-9 and TIMPs in human achilles tendon rupture

Evgenia Karousou et al. Clin Orthop Relat Res. 2008 Jul.

Abstract

Tendon integrity depends on the extracellular matrix (ECM) metabolism which is regulated by proteolytic enzymes. However, it is unclear which enzymes play a role in tendon rupture. We studied the ECM of 19 ruptured human Achilles tendons, comparing the composition of specimens harvested close to the rupture with specimens harvested from an apparently healthy area in the same tendon. We compared gene expression of collagen Type I, decorin, and versican including enzymes involved in their metabolism as matrix metalloproteases (MMP-2 and -9) and tissue inhibitory of metalloproteinase (TIMP-1 and -2) using real-time PCR, zymography and FACE analysis. We found greater gene expression of proteoglycan core protein decorin and versican, collagen Type I, MMPs and TIMPs in the tendon rupture. Zymography analysis, reflecting expression of enzymatic activity, confirmed the gene expression data at protein level. Carbohydrate content was greater in the macroscopically healthy area than in the ruptured area. In the ruptured area, we found increased core protein synthesis but without the normal glycosaminoglycan production. The tissue in the area of rupture undergoes marked rearrangement at molecular levels and supports the role of MMPs in the pathology.

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Figures

Fig. 1
Fig. 1
The gene expression pattern of tendon specimens harvested close and far from the rupture area is shown. The bars represent a mean of three different experiments on 19 different patients. R = gene expression of the ruptured area; H = gene expression of the control area.
Fig. 2
Fig. 2
The same genes reported in Fig. 1 are compared with the expression pattern of the Col I A1 gene. The bars represent a mean of three different experiments on 19 different patients. R = gene expression of the ruptured area; H = gene expression of the control area.
Fig. 3A–B
Fig. 3A–B
These are examples of FACE analysis of the glycosaminoglycan disaccharides obtained from the human tendons: H = control area; R = rupture area. (A) The nonsulphated glycosaminoglycans are shown. (B) The sulphated glycosaminoglycans disaccharides are shown. FACE analysis was performed on 19 different samples, and the data showed the same experimental pattern. The data are reported in the text with standard deviation.
Fig. 4A–B
Fig. 4A–B
Zymography of the extracts from human tendons is shown. The ladder indicates the molecular weight of the protein standards. H = control area; R = rupture area. The activity bands are the clear band on the dark background. The bands 72 kDa and 66 kDa represent the zymogen pro MMP2 and activated MMP-2 respectively. The bands with molecular weight above 100 kDa correspond to MMP-2 lipocalin complexes. Zymography was performed on 19 different samples, and the results showed the same experimental pattern (A) The 13th sample is shown. (B) The 16th sample is shown.
See this image and copyright information in PMC

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