Study of biochemical substrate and role of metalloproteinases in fascia transversalis from hernial processes
Identifiers
Permanent link (URI): http://hdl.handle.net/10017/59628DOI: 10.1046/j.1365-2362.1997.1400686.x
PMID: 9229232
ISSN: 0014-2972
Date
1997-06Affiliation
Universidad de Alcalá. Departamento Biomedicina y Biotecnología. Unidad docente Biología Celular y GenéticaBibliographic citation
Bellón, J.M. et al. (1997) ‘Study of biochemical substrate and role of metalloproteinases in fascia transversalis from hernial processes’, European journal of clinical investigation, 27(6), pp. 510–516. doi:10.1046/j.1365-2362.1997.1400686.x
Keywords
Extracellular matrix
Fascia transversalis
Hernia
Metalloproteinases
Document type
info:eu-repo/semantics/article
Rights
© 1997 Blackwell Science Ltd
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Access rights
info:eu-repo/semantics/openAccess
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.
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