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Biochemical and morphological alterations of the extracellular matrix of chicken calcaneal tendon during maturation
Authors:Haline Ballestero Fêo  Adriano Biancalana  Wilson Romero Nakagaki  Andrea Aparecida De Aro  Laurecir Gomes
Affiliation:1. Department of Functional and Structural Biology, IB, State University of Campinas—UNICAMP, Campinas, S?o Paulo, Brazil;2. Department of Cell Biology, Federal University of Pará—UFPA, Pará, Brazil;3. University of Western S?o Paulo—UNOESTE, Presidente Prudente, S?o Paulo, Brazil
Abstract:The region in tendons that surrounds bone extremities adapts to compression forces, developing a fibrocartilaginous structure. During maturation, changes occur in the amount and organization of macromolecules of the extracellular matrix of tendons, changing the tissue morphology. To study the effect of maturation on tendons, Pedrês chickens were sacrificed at 1, 5, and 8 months old and had the calcaneal tendon (CT) divided into proximal region, submitted to tension/compression forces ( p ), and distal region submitted to tension force ( d ). Morphological analysis of the p region showed the presence of fibrocartilage in all ages. In the central part of the fibrocartilage, near a diminishment of the metachromasy, there was also a development of a probable fat pad that increased with the maturation. The activity of MMP‐2 and MMP‐9 was higher at 5 and 8 months old, in both regions, compared with 1‐month‐old animals. In SDS‐PAGE analysis, components with electrophoretic migration similar to decorin and fibromodulin increased with maturation, particularly in the d region. The Western blotting confirmed the increased amount of fibromodulin with maturation. In conclusion, our results show that process of maturation leads to the appearance of a probable fat pad in the center of the fibrocartilage of CT, with a reduced amount of glycosaminoglycans and an increased activity of MMPs. Microsc. Res. Tech. 78:949–957, 2015. © 2015 Wiley Periodicals, Inc.
Keywords:  maturation  fibrocartilage  MMP  fat pad  collagen
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