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. 2002 Mar;131(3):324-31.
doi: 10.1067/msy.2002.121376.

Impaired balance of type I and type III procollagen mRNA in cultured fibroblasts of patients with incisional hernia

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Impaired balance of type I and type III procollagen mRNA in cultured fibroblasts of patients with incisional hernia

Zhongyi Si et al. Surgery. 2002 Mar.

Erratum in

  • Surgery 2002 May;131(5):501. Rhanjit, Bhardwaj [corrected to Bhardwaj, Rhanjit]; Rene, Peter Merten [corrected to Mertens, Peter Rene]

Abstract

Background: Recent findings of an impaired protein ratio of type I to type III procollagen showed a disturbed collagen metabolism in incisional hernia development. We analyzed the type I and type III procollagen messenger RNA to investigate whether these findings represent the altered extracellular matrix or a primary defect at the transcriptional level.

Methods: We examined cultured skin fibroblasts of patients with incisional or recurrent incisional hernia in comparison with those without any previous incision (control) and those with a skin scar without clinical appearance of a hernia (scar). Immunohistochemical detection of a lowered protein ratio of type I and type III collagen in the hernia skin tissue leads to mRNA expression analysis. The procollagen mRNA and the ratio of type I to type III procollagen mRNA are detected by reverse transcriptase-polymerase chain reaction and Northern blot analysis, the collagens type I and III by Western blot analysis.

Results: Reverse transcriptase-polymerase chain reaction revealed an increase of type I procollagen mRNA in the incisional and recurrent hernia (0.90 +/- 0.04 and 1.19 +/- 0.04, respectively) compared with stable scar (0.54 +/- 0.02) or healthy tissue (0.43 +/- 0.01). The obvious rise of type III procollagen mRNA to 4.13 +/- 0.04 for incisional, 6.02 +/- 0.03 for recurrent hernia, 2.29 +/- 0.04 for stable scar, and 1.72 +/- 0.03 for the healthy tissue showed a significantly decreased ratio of type I to type III procollagen mRNA in the hernia patients as compared with the controls (P <.01). By Western blot analysis, an increase of type I and type III collagen protein and a significant rise in the corresponding ratio in the recurrent hernia group were detected.

Conclusions: The altered synthesis of type I and type III collagen in cultured skin fibroblasts suggests a disorder of collagen metabolism, at least in patients with recurrent hernia. Hence, a basically impaired wound healing process is likely to contribute to the unsatisfactory results of incisional hernia repair.

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