Study of biochemical substrate and role of metalloproteinases in fascia transversalis from hernial processes

Abstract

The aim of this study was to examine the fascia transversalis (FT) from patients with direct and indirect hernia in an attempt to identify possible differences between each type of hernia. FT samples were obtained from 36 patients presenting inguinal hernia (23 indirect hernia and 13 direct hernia) who underwent surgery. We have analysed the ultrastructure of the fascia surrounding the hernial lesions, the proline and lysine hydroxylation in the tissue, the type I-type III collagen ratio and the presence of metalloproteinases. We have not detected ultrastructural differences in the collagen fibrils from FT in direct and indirect hernias. However, the interfibrillar matrix was more abundant in direct hernias, showing abundant electron-dense particles. No differences in proline hydroxylation were observed between each type of hernia. A small decrease in lysine hydroxylation was detected in patients with direct hernia. Enzyme-linked immunosorbent assays (ELISAs) showed no statistically significant differences in the type I-type III collagen absorbance ratios. Immunohistochemistry revealed no differences in the expression of matrix metalloproteinase-1. FT from patients presenting direct hernia showed a very strong staining vs. metalloproteinase-2 when compared with that observed in indirect hernia.

Quantitative and qualitative analysis of collagen types in the fascia transversalis of inguinal hernia patients

“…BELLÓN et al (3) could also not find meaningful differences in the amount of collagen in their patients group.…”

Biochemical Study of Collagen in Adult Groin Hernias

“…Hence, inguinal hernia could be considered a local manifestation of a more generalized collagen pathology. These studies about collagen disorder focused mainly on the rectus sheath [4 -6] or the skin [8], while only few reports dealt with the transversalis fascia [9]. In this report [9], a slight decrease in lysine hydroxylation and a significant increase in the expression of matrix degrading enzyme, the matrix metalloproteinase-2, were detected in fascias from direct hernia.…”

“…These studies about collagen disorder focused mainly on the rectus sheath [4 -6] or the skin [8], while only few reports dealt with the transversalis fascia [9]. In this report [9], a slight decrease in lysine hydroxylation and a significant increase in the expression of matrix degrading enzyme, the matrix metalloproteinase-2, were detected in fascias from direct hernia. Our previous biomechanical and histological studies [10,11] performed on the transversalis fascia and the rectus sheath in patients with inguinal hernia suggested that a connective tissue pathology could play a role in the genesis of groin hernias.…”

Quantitative analysis of collagen and elastic fibers in the transversalis fascia in direct and indirect inguinal hernia

“…This alteration may be due to an enhanced collagen turnover rate or increased breakdown of collagen by metalloproteinases. Bellon et al 20 showed an increased expression of metalloproteinase 2 in TF in direct compared to indirect hernias.…”