Biochemical Study of Collagen in Adult Groin Hernias
| Autor: | Charles M. Lapière, Adelin Albert, Alain Pans, Betty Nusgens |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Adult
Male Pathology medicine.medical_specialty Rectus Abdominis Connective tissue Hernia Inguinal Groin Pepsin Reference Values medicine Humans Hernia Fascia biology business.industry Organ Size Rectus sheath Anatomy Middle Aged medicine.disease Control subjects Pepsin A Tissue Donors body regions Inguinal hernia medicine.anatomical_structure Connective Tissue biology.protein Female Surgery Autopsy Collagen business Fascia (architecture) |
| Zdroj: | Journal of Surgical Research. 95:107-113 |
| ISSN: | 0022-4804 |
| Popis: | 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 α 1 /α 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 α 1 /α 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. |
| Databáze: | OpenAIRE |
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