Persistent extracellular matrix remodelling at the interface to polymers used for hernia repair.
On the one hand, recurrence rates and postoperative complications following hernia repair are supposed to be influenced by the kind of mesh material used. On the other hand, an impaired collagen metabolism and cleavage within connective tissue has been suggested as decisive factor in the pathogenesis of recurrent hernia formation. The aim of our study was, therefore, to analyze the impact of commonly used mesh materials on quality of collagen deposition, expression of collagenases (matrix metalloproteinases; MMP-1/MMP-13), and specific tissue inhibitors of MMPs (TIMPs) in an animal study. Four different mesh materials were used (Prolene = polypropylene, Mersilene = polyester, and Vypro and Vypro II = combinations of polypropylene and polyglactin) and implanted as abdominal wall replacement in 60 male Wistar rats. Mesh samples were explanted after 3, 21, and 90 days and investigated using immunohistochemistry (expression of MMP-1/MMP-13 and TIMP-1) and cross-polarization microscopy (percentage of collagen type III to overall collagen). Besides an insufficient collagen composition with an increased percentage of collagen type III, we found a complex expression of collagenases and their inhibitors combined with a persistent chronic foreign-body reaction even 90 days after implantation. Except for TIMP-1 expression, which was significantly related to a lowered amount of inflammatory (r = -0.980, p = 0.02) and connective tissue formation (r = -0.951, p = 0.049), there was no relation to the expression of collagenases (MMP-1/MMP-13) with regard to the amount of inflammatory and connective tissue formation despite partly significant differences between implanted polymers.
Junge
K
K
Department of Surgery, German Centre of Excellence for Biomaterial and Implant Pathology, Technical University of Aachen, Aachen, Germany. karsten.junge@post.rwth-aachen.de
Rosch
R
R
Bialasinski
L
L
Klinge
U
U
Klosterhalfen
B
B
Schumpelick
V
V
D000818:Animals; D024061:Collagen Type III / Q000378:metabolism; D017364:Collagenases / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism*; D006555:Hernia, Ventral / Q000601:surgery*; D007150:Immunohistochemistry; D008297:Male; D020781:Matrix Metalloproteinase 1 / Q000378:metabolism; D053509:Matrix Metalloproteinase 13; D011091:Polyesters / Q000494:pharmacology; D011098:Polyglactin 910 / Q000494:pharmacology; D011126:Polypropylenes / Q000494:pharmacology; D011183:Postoperative Complications / Q000378:metabolism / Q000517:prevention & control; D051381:Rats; D017208:Rats, Wistar; D013526:Surgical Mesh; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000378:metabolism; D014945:Wound Healing
D024061:Collagen Type III; D011091:Polyesters; D011126:Polypropylenes; D019715:Tissue Inhibitor of Metalloproteinase-1; D011098:Polyglactin 910; D017364:Collagenases; D053509:Matrix Metalloproteinase 13; C507083:Mmp13 protein, rat; D020781:Matrix Metalloproteinase 1