Artículos de revistas
Changes In The Connective Tissue Sheath Of Wistar Rat Nerve With Aging
Registro en:
Annals Of Anatomy. Urban Und Fischer Verlag Jena, v. 196, n. 6, p. 441 - 448, 2014.
9409602
10.1016/j.aanat.2014.08.005
2-s2.0-84908191584
Autor
Esquisatto M.A.M.
de Aro A.A.
Feo H.B.
Gomes L.
Institución
Resumen
The alterations due to aging in the peripheral nerves can affect the physiology of these structures. Thus, the purpose of the present study was to describe the activity of the MMP-2 and MMP-9, as well as the structure and composition of the extracellular matrix of the rat sciatic nerve during maturation and aging. Our results have shown that the extracellular matrix of the sciatic nerve of 30-, 180- and 730-day-old Wistar rats present ultrastructural, morphometrical and biochemical changes during aging. The perineurium was the structure most affected by age, as evidenced by a decrease in thickness and in collagen fibril content. Cytochemical analysis detected proteoglycans in the basal membrane of Schwann cells and around perineural cells, as well as on the collagen fibrils of the perineurium and endoneurium at all ages. Biochemical analyses showed that the quantity of non-collagenous proteins was higher in 730-day-old animals compared to other ages, while the uronic acid content was higher in 30-day-old animals. Morphometrical analysis detected greater numbers of myelinated fibers and increased myelin thickness in 180-day-old animals. Zymography analysis detected greater amounts and activity of MMP-2 and MMP-9 in 180- and 730-day-old animals compared to younger rats. In conclusion, our results showed changes in the structural organization and composition of extracellular matrix of the sciatic nerve during aging, such as increase in the non-collagenous protein content and higher MMP-2 and MMP-9 activity, decrease in uronic acid concentration and in collagen fibril content in the perineurium, as well as degeneration of nerve fibers. 196 6 441 448 Aimes, R.T., Quigley, J.P., Matrix metalloproteinase-2 is an interstitial collagenase. 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