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

Satomi E, Teodoro WR, Parra ER, Fernandes TD, Velosa AP, Capelozzi VL, Yoshinari NH - Clinics (Sao Paulo) (2008)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Department of Rheumatology, Hospital das Clínicas, Faculdade de Medicina, Universidade de São Paulo, São Paulo, SP, Brazil.

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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Related in: MedlinePlus

Type I, III and V collagenous fibers in tendon controls (panels A, C and E) and posterior tibial tendon dysfunction (PTTD) patients (panels B, D, F, G and H) labeled with fluorescein and observed under a fluorescent microscope. Control tendons show parallel orientation of type I (A) and III (C) collagen and strong green fluorescence and a finely reticulated type V collagen (E) network in the interstitium and basement membranes of vessels, coincident with the maintenance of the architecture of the tendons. In contrast, PTTD shows distorted architecture and a diffuse increase of birefringence for all three types of collagen. Type I collagen birefringence is discrete and diffusely distributed in pathologic tendons (B). Type III has the same distribution found for type I but is more prominent and thus defines the fibrosis process installation (D). Type V collagen was mostly found in the vessel walls and around them, resulting in a finely reticulated network (F) when compared to type III fibers. In panels G and H, the strong birefringence of type III and V collagen in the periadvential areas with more vascular density are shown Original magnification X 100 in panels B, D and F; X200 in panels A, C, E, G and H)
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f2-cln63_1p0009: Type I, III and V collagenous fibers in tendon controls (panels A, C and E) and posterior tibial tendon dysfunction (PTTD) patients (panels B, D, F, G and H) labeled with fluorescein and observed under a fluorescent microscope. Control tendons show parallel orientation of type I (A) and III (C) collagen and strong green fluorescence and a finely reticulated type V collagen (E) network in the interstitium and basement membranes of vessels, coincident with the maintenance of the architecture of the tendons. In contrast, PTTD shows distorted architecture and a diffuse increase of birefringence for all three types of collagen. Type I collagen birefringence is discrete and diffusely distributed in pathologic tendons (B). Type III has the same distribution found for type I but is more prominent and thus defines the fibrosis process installation (D). Type V collagen was mostly found in the vessel walls and around them, resulting in a finely reticulated network (F) when compared to type III fibers. In panels G and H, the strong birefringence of type III and V collagen in the periadvential areas with more vascular density are shown Original magnification X 100 in panels B, D and F; X200 in panels A, C, E, G and H)

Mentions: Collagen Expression in Posterior Tibial Tendon Matrix Types I, III and V collagen fibers in control (Figure 2 -panels A, C and E) and pathologic samples (Figure 2 - panels B, D, F, G and H) were immunostained. Clearly, tendons from the control patients show a green birefringence for type I, III and V collagens. Type I collagen presents a parallel orientation of the fibers in all structures of the tendon (Figure 2A), whereas type III physically interact with the type I collagen fibers and the corresponding vessels in a homogeneous pattern (Figure 2C). A finely reticulated pattern of type V collagen birefringence is particularly evident in control tendons (Figure 2E).


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

Satomi E, Teodoro WR, Parra ER, Fernandes TD, Velosa AP, Capelozzi VL, Yoshinari NH - Clinics (Sao Paulo) (2008)

Type I, III and V collagenous fibers in tendon controls (panels A, C and E) and posterior tibial tendon dysfunction (PTTD) patients (panels B, D, F, G and H) labeled with fluorescein and observed under a fluorescent microscope. Control tendons show parallel orientation of type I (A) and III (C) collagen and strong green fluorescence and a finely reticulated type V collagen (E) network in the interstitium and basement membranes of vessels, coincident with the maintenance of the architecture of the tendons. In contrast, PTTD shows distorted architecture and a diffuse increase of birefringence for all three types of collagen. Type I collagen birefringence is discrete and diffusely distributed in pathologic tendons (B). Type III has the same distribution found for type I but is more prominent and thus defines the fibrosis process installation (D). Type V collagen was mostly found in the vessel walls and around them, resulting in a finely reticulated network (F) when compared to type III fibers. In panels G and H, the strong birefringence of type III and V collagen in the periadvential areas with more vascular density are shown Original magnification X 100 in panels B, D and F; X200 in panels A, C, E, G and H)
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2664193&req=5

f2-cln63_1p0009: Type I, III and V collagenous fibers in tendon controls (panels A, C and E) and posterior tibial tendon dysfunction (PTTD) patients (panels B, D, F, G and H) labeled with fluorescein and observed under a fluorescent microscope. Control tendons show parallel orientation of type I (A) and III (C) collagen and strong green fluorescence and a finely reticulated type V collagen (E) network in the interstitium and basement membranes of vessels, coincident with the maintenance of the architecture of the tendons. In contrast, PTTD shows distorted architecture and a diffuse increase of birefringence for all three types of collagen. Type I collagen birefringence is discrete and diffusely distributed in pathologic tendons (B). Type III has the same distribution found for type I but is more prominent and thus defines the fibrosis process installation (D). Type V collagen was mostly found in the vessel walls and around them, resulting in a finely reticulated network (F) when compared to type III fibers. In panels G and H, the strong birefringence of type III and V collagen in the periadvential areas with more vascular density are shown Original magnification X 100 in panels B, D and F; X200 in panels A, C, E, G and H)
Mentions: Collagen Expression in Posterior Tibial Tendon Matrix Types I, III and V collagen fibers in control (Figure 2 -panels A, C and E) and pathologic samples (Figure 2 - panels B, D, F, G and H) were immunostained. Clearly, tendons from the control patients show a green birefringence for type I, III and V collagens. Type I collagen presents a parallel orientation of the fibers in all structures of the tendon (Figure 2A), whereas type III physically interact with the type I collagen fibers and the corresponding vessels in a homogeneous pattern (Figure 2C). A finely reticulated pattern of type V collagen birefringence is particularly evident in control tendons (Figure 2E).

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Department of Rheumatology, Hospital das Clínicas, Faculdade de Medicina, Universidade de São Paulo, São Paulo, SP, Brazil.

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.

Show MeSH
Related in: MedlinePlus