title: Expression of the extracellular matrix proteins collagen I, collagen III and fibronectin and matrix metalloproteinase-1 and -13 in the skin of patients with inguinal hernia.
abstract: Although abnormal collagen metabolism has been ascribed an important role in the high recurrence rates after surgical hernia repair, knowledge on tissue sampled in the region affected by inguinal hernias is poor. In the present study, we determined collagen type I and type III in the skin of adult patients with indirect and direct inguinal hernias by both immunohistochemistry and Western blot analysis. In addition, we quantified the immunohistochemical expression of fibronectin and matrix metalloproteinase (MMP)-1 and -13. The results indicated that the ratio of collagen type I/III was significantly decreased in the skin of patients with either indirect (n = 9) or direct hernia (n = 7), with a concomitant increase in collagen type III (p < 0.001 vs. controls, n = 7, without affection of the inguinal region). There was no significant difference between patients with indirect and direct hernia (p > 0.05). MMP-13 was not expressed in any of the skin samples investigated, whereas MMP-1 was found in the epidermis. Fibronectin was predominantly detected at the epidermal-dermal junction. MMP-1, MMP-13 and fibronectin levels were significantly different between patients and controls (p > 0. 05). We conclude that in contrast to the unchanged expression of fibronectin and MMP-1 and MMP-13, the decreased ratios of collagen tpye I/III with the basically increased amount of collagen type III could be of significant importance for the pathophysiology of hernias. The specific ratio collagen I/III probably reflects the altered structural integrity and mechanical stability of the connective tissue in both indirect and direct hernias. Moreover, our findings stress that hernias should be regarded as the manifestation of a systemic disease in the inguinal region with a genetic background, explaining the high recurrence rates after repeated suture repair, as well as the usefulness of surgical meshes in this clinical setting.
authors.affiliation: Department of Surgery, Technical University of Aachen, Germany. Klinge@alpha.imib.rwth-aachen.de
authors.forename: U
authors.initials: U
authors.lastname: Klinge
authors.forename: H
authors.initials: H
authors.lastname: Zheng
authors.forename: Z
authors.initials: Z
authors.lastname: Si
authors.forename: V
authors.initials: V
authors.lastname: Schumpelick
authors.forename: R S
authors.initials: RS
authors.lastname: Bhardwaj
authors.forename: L
authors.initials: L
authors.lastname: Muys
authors.forename: B
authors.initials: B
authors.lastname: Klosterhalfen
mesh_terms: D000368:Aged; D003094:Collagen / Q000378:metabolism*; D017364:Collagenases / Q000378:metabolism*; D005260:Female; D005353:Fibronectins / Q000378:metabolism*; D006552:Hernia, Inguinal / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D020781:Matrix Metalloproteinase 1 / Q000378:metabolism*; D053509:Matrix Metalloproteinase 13; D008875:Middle Aged; D012867:Skin / Q000378:metabolism*
chemical_list: D005353:Fibronectins; D003094:Collagen; D017364:Collagenases; C507079:MMP13 protein, human; D053509:Matrix Metalloproteinase 13; D020781:Matrix Metalloproteinase 1