Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/102145
Type: Artigo de periódico
Title: Experimental Tendon Repair: Glycosaminoglycan Arrangement In Newly Synthesized Collagen Fibers.
Author: Mello M.L.
de Campos Vidal B.
Abstract: Changes in the macromolecular orientation and metachromasy of glycosaminoglycans (GAG) in newly synthesized and assembled collagen fibers in rat Achilles tendon after tendon excision were investigated in toluidine blue (TB)-stained preparations, based in the selective absorption of polarized light (= linear dichroism, LD) and of absorption of unpolarized light in situ. Extrinsic LD was observed microspectrophotometrically from the early phases of tendon repair onwards, although the absorption peaks in both parallel and perpendicular directions with respect to the plane of polarized light and the long axis of the collagen fibers occurred at the same wavelength, and thus differed from the pattern situation in normal adult controls. Compared to normal adult tendons, the pattern of LD in newly synthesized and assembled fibers was still not fully attained 110 days after surgical tendon removal. This incomplete recovery possibly reflected the influence of aging during the repair process. There was no correlation between LD and metachromasy. The highest absorption values for metachromatic staining occurred on the 7th day after tendon removal, at a time when LD was not intense. Treatment with hyaluronidase showed that the LD in the early stages of tendon repair was mostly due to hyaluronate whereas the LD in the later stages was due to chondroitin sulfates. The changes in LD during Achilles tendon repair were attributed to gradual modifications in the composition and macromolecular orientation of GAGs relative to the long axis of the collagen fibers.
Editor: 
Rights: aberto
Identifier DOI: 
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-2142708564&partnerID=40&md5=658687f5a0addf0d25f29d840bf049c0
Date Issue: 2003
Appears in Collections:Unicamp - Artigos e Outros Documentos

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