Changes in Histoanatomical Distribution Of Types I, III And V Collagen Promote Adaptative Remodeling in Posterior Tibial Tendon Rupture

Abstract

INTRODUCTION:Posterior tibial tendon dysfunction is a common cause of adult flat foot deformity, and its etiology is unknown. PURPOSE: In this study, we characterized the morphologic pattern and distribution of types I, III and V collagen in posterior tibial tendon dysfunction. METHOD: Tendon samples from patients with and without posterior tibial tendon dysfunction were stained by immunofluorescence using antibodies against types I, III and V collagen. RESULTS: Control samples showed that type V deposited near the vessels only, while surgically obtained specimens displayed type V collagen surrounding other types of collagen fibers in thicker adventitial layers. Type III collagen levels were also increased in pathological specimens. On the other hand, amounts of collagen type I, which represents 95% of the total collagen amount in normal tendon, were decreased in pathological specimens. CONCLUSION: Fibrillogenesis in posterior tibial tendon dysfunction is altered due to higher expression of types III and V collagen and a decreased amount of collagen type I, which renders the originating fibrils structurally less resistant to mechanical forces.

The COL5A1 genotype is associated with range of motion

“…Saunders et al [21] stated that COL5A1 genotypes might interact with age for ROM in physically active subjects. On the other hand, Goncalves-Neto et al [22] and Satomi et al [23] reported that damaged and pathological tendons contained relatively higher proportion of collagen type V, and these alterations were accompanied by a reduction in type I collagen. Thus, according to COL5A1 genotype might be increase rate of injuries in elderly.…”

Murine tendon function is adversely affected by aggrecan accumulation due to the knockout of ADAMTS5

“…The reparative task for cells, whether mature or progenitor, is primarily to re-establish the normal tensional properties of the tissue by the secretion and integration of newly synthesized collagen into the existing network, which is largely composed of heterotypic fibrils of collagens I and III along with minor amounts of type V. 1,2 This process also requires production and organization of a noncollagenous matrix which, among many other components, contains members of the collagen binding SLRP family and the large proteoglycans (PGs), versican, and aggrecan. 3 To date, there has been no clearly defined mechanistic role for aggrecan (or versican) in tendon cell behavior, matrix homeostatic maintenance, tissue injury, and repair.…”

Uso de células mononucleares da medula óssea no tratamento de tendinites induzidas experimentalmente em equinos

“…Quanto à presença de neovascularização, os equinos do GC apresentaram maior quantidade de pequenos vasos, sendo estes de parede mais espessa. Os vasos não foram identificados em grande número na maioria dos cortes histológicos, diferentemente do que foi identificado por Silver et al (1983), e em equinos tratados com glicosaminoglicanos polissulfatados, quando foi descrita uma vascularização em grande intensidade (Marxen et al, 2004). Marr et al (1993) relataram que a diminuição da celularidade e da vascularização são indicativas de progressiva maturação do tecido de granulação, pois a deposição de colágeno exerce pressão mecânica sobre as delicadas paredes de capilares neoformados, levando à diminuição da vascularização.…”

“…Nesse caso, a marcação para fibras colágenas do tipo I e III foi difusa. Satomi et al (2008) descreveram a marcação via imunofluorescência para colágeno tipo I e III na tendinose em humanos com distribuição semelhante, sendo a fibra colágena tipo I marcada de forma discreta e difusa, como também para fibra colágena tipo III, porém mais proeminente.…”