Joint bone spine · 2002
Changes in collagen matrix composition in human posterior tibial tendon dysfunction.
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Gonçalves-Neto Joaquim, Witzel S S, Teodoro W R, Carvalho-Júnior A E, Fernandes T D, Yoshinari H H
Аннотация
OBJECTIVE: To investigate whether tendon degeneration in posterior tibial tendon dysfunction syndrome is associated with changes in extracellular matrix collagen composition.
METHODS: Specimens from grossly abnormal tendon regions from 9 patients with posterior tibial tendon dysfunction syndrome were prepared for routine histology. Collagens I, III and V were typed by immunoblotting and quantified by densitometry after SDS-PAGE. Proline and hydroxyproline residues were determined by liquid chromatography. Four other samples from grossly normal homologous tendon regions and one surgical specimen from a healthy patient undergoing arthrodesis of the ankle after an accident were included as control.
RESULTS: In the grossly abnormal surgical posterior tibial tendon specimens we observed three types of histopathologic conditions present to varying degrees: increased mucin content, fibroblast hypercellularity and neovascularization. Analysis of degenerate tendons demonstrated a 79.3% increase in total proline and a 32.4% increase in 4-hydroxyproline. In addition, damaged tissue contained a higher proportion of collagen type III (mean increase: 53.6%) associated with a concomitant increase in type V collagen (mean increase: 26.4%). These alterations were accompanied by a reduction in type I collagen (mean decrease: 41.4%).
CONCLUSIONS: In posterior tibial tendon dysfunction syndrome, the degenerative process results from marked changes in both structural organization and molecular composition of matrix collagens. The higher proportion of type V and type IlI collagens in degenerated tendons is likely to contribute to a decrease in the mechanical resistance of the tissue.
METHODS: Specimens from grossly abnormal tendon regions from 9 patients with posterior tibial tendon dysfunction syndrome were prepared for routine histology. Collagens I, III and V were typed by immunoblotting and quantified by densitometry after SDS-PAGE. Proline and hydroxyproline residues were determined by liquid chromatography. Four other samples from grossly normal homologous tendon regions and one surgical specimen from a healthy patient undergoing arthrodesis of the ankle after an accident were included as control.
RESULTS: In the grossly abnormal surgical posterior tibial tendon specimens we observed three types of histopathologic conditions present to varying degrees: increased mucin content, fibroblast hypercellularity and neovascularization. Analysis of degenerate tendons demonstrated a 79.3% increase in total proline and a 32.4% increase in 4-hydroxyproline. In addition, damaged tissue contained a higher proportion of collagen type III (mean increase: 53.6%) associated with a concomitant increase in type V collagen (mean increase: 26.4%). These alterations were accompanied by a reduction in type I collagen (mean decrease: 41.4%).
CONCLUSIONS: In posterior tibial tendon dysfunction syndrome, the degenerative process results from marked changes in both structural organization and molecular composition of matrix collagens. The higher proportion of type V and type IlI collagens in degenerated tendons is likely to contribute to a decrease in the mechanical resistance of the tissue.