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Changes in histoanatomical distribution of types I, III and V collagen promote adaptative remodeling in posterior tibial tendon rupture
Satomi, Érika; Teodoro, Walcy R; Parra, Edwin R; Fernandes, Túlio D; Velosa, Ana Paula P; Capelozzi, Vera Luiza; Yoshinari, Natalino Hajime.
  • Satomi, Érika; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Rheumatology. São Paulo. BR
  • Teodoro, Walcy R; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Rheumatology. São Paulo. BR
  • Parra, Edwin R; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Pathology. São Paulo. BR
  • Fernandes, Túlio D; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Orthopedics. São Paulo. BR
  • Velosa, Ana Paula P; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Rheumatology. São Paulo. BR
  • Capelozzi, Vera Luiza; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Pathology. São Paulo. BR
  • Yoshinari, Natalino Hajime; Universidade de São Paulo. Faculdade de Medicina. Hospital das Clínicas. Department of Rheumatology. São Paulo. BR
Clinics ; 63(1): 9-14, 2008. ilus
Article in English | LILACS | ID: lil-474921
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 percent 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.
Subject(s)

Full text: Available Index: LILACS (Americas) Main subject: Collagen Type I / Collagen Type III / Collagen Type V / Posterior Tibial Tendon Dysfunction Type of study: Observational study Limits: Adult / Aged / Female / Humans Language: English Journal: Clinics Journal subject: Medicine Year: 2008 Type: Article Affiliation country: Brazil Institution/Affiliation country: Universidade de São Paulo/BR

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Full text: Available Index: LILACS (Americas) Main subject: Collagen Type I / Collagen Type III / Collagen Type V / Posterior Tibial Tendon Dysfunction Type of study: Observational study Limits: Adult / Aged / Female / Humans Language: English Journal: Clinics Journal subject: Medicine Year: 2008 Type: Article Affiliation country: Brazil Institution/Affiliation country: Universidade de São Paulo/BR