Reference : Biochemical Study of Collagen in Adult Groin Hernias
Scientific journals : Article
Human health sciences : Surgery
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/58072
Biochemical Study of Collagen in Adult Groin Hernias
English
Pans, Alain mailto [Centre Hospitalier Universitaire de Liège - CHU > > Chirurgie abdominale - Clinique André Renard >]
Albert, Adelin mailto [Université de Liège - ULg > Département des sciences de la santé publique > Informatique médicale et biostatistique >]
Lapiere, C. M. [Université de Liège - ULG > > >Laboratoire de Biologie des Tissus Conjonctifs > > >]
Nusgens, Betty mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Laboratoire de Biologie des tissus Conjonctifs > >]
Feb-2001
Journal of Surgical Research
95
2
107-13
Yes (verified by ORBi)
International
0022-4804
[en] BACKGROUND: Previous works have suggested that a defect in collagen fiber structure may play a role in inguinal hernia formation. These studies focused mainly on the rectus sheath or the skin, while only few reports dealt with the transversalis fascia. According to these findings and to our previous biomechanical and histological studies suggesting that a connective tissue pathology could play a role in the genesis of groin hernias, we performed a biochemical investigation of the collagen in the transversalis fascia and rectus sheath. MATERIALS AND METHODS: The samples were collected from 40 adult patients with uni- or bilateral hernias and from 20 control subjects without hernia (autopsies and organ donors). A constant area of tissue was taken by using a calibrator. The wet and dry weights per 100 mm(2) were determined and the total collagen concentration as well as its sequential extractibility in NaCl, acetic acid, and pepsin was measured. The ratios of alpha(1)/alpha(2) chains (I) and of type I/III collagen were assessed by polyacrylamide gel electrophoresis. RESULTS: Samples collected in the control and patient sheaths showed an increased wet weight per 100 mm(2) in the patients. The wet and dry weights per unit area were increased in the patient fascias. The collagen concentration was increased in the indirect hernias. The fascias from the direct hernias (DH) presented a significantly increased collagen extractibility after pepsin digestion (5.6%), when compared to the control fascias (2.6%). The extractibility was 3.4% in the nonherniated (NH) sides. The qualitative study (ratios alpha(1)/alpha(2) (I) and I/III collagen) showed no difference between the fascia groups. CONCLUSIONS: The significant increase of collagen extractibility with pepsin in the DH fascias and at a lesser degree in the NH fascias suggests that molecular alterations of collagen could be involved in the genesis of groin hernias. This connective tissue pathology would express preferentially its effects in the inguinal region, since we have observed no major difference between the rectus sheaths of controls and those of patients.
Researchers
http://hdl.handle.net/2268/58072
10.1006/jsre.2000.6024
original publication available on the Journal of Surgical Research website

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