Changes in histoanatomical distribution of types I, III and V collagen promote adaptative remodeling in posterior tibial tendon rupture

Authors

  • Érika Satomi Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Rheumatology
  • Walcy R. Teodoro Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Rheumatology
  • Edwin R. Parra Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Pathology
  • Túlio D. Fernandes Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Orthopedics
  • Ana Paula P. Velosa Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Rheumatology
  • Vera Luiza Capelozzi Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Pathology
  • Natalino Hajime Yoshinari Universidade de São Paulo; Faculdade de Medicina; Hospital das Clínicas; Department of Rheumatology

DOI:

https://doi.org/10.1590/S1807-59322008000100003

Keywords:

Collagen, Tendon, Tendinopathy, 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.

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Published

2008-01-01

Issue

Section

Clinical Sciences

How to Cite

Changes in histoanatomical distribution of types I, III and V collagen promote adaptative remodeling in posterior tibial tendon rupture . (2008). Clinics, 63(1), 9-14. https://doi.org/10.1590/S1807-59322008000100003