Matrix metalloproteinase expression in basal cell carcinoma: Relationship between enzyme profile and collagen fragmentation pattern

Taskin Yucel, Amar Mutnal, Kevin Fay, Suzanne E.G. Fligiel, Timothy Wang, Timothy Johnson, Shan R. Baker, James Varani

Research output: Contribution to journalArticlepeer-review

Abstract

Matrix metalloproteinases (MMPs) with collagenolytic and gelatinolytic activities are up-regulated in basal cell carcinoma. In the present study we demonstrate that the major collagenolytic enzyme detected is MMP-1 (interstitial collagenase) while gelatinolytic enzymes include both MMP-2 (72-kDa gelatinase A) and MMP-9 (92-kDa gelatinase B). Significant fractions of all three enzymes are present as active forms. In spite of the fact that high levels of gelatinolytic enzymes are present, the major fragmentation products resulting from digestion of intact type I collagen are the 1/4 and 3/4 fragments (products of MMP-1-mediated digestion). Thus, it appears that the gelatinolytic enzymes are not capable of degrading the collagen fragments as rapidly as they are produced. Since previous studies have demonstrated that interaction of interstitial fibroblasts with high molecular weight fragments of type I collagen leads to increased MMP production, the present results suggest a mechanism underlying altered function of stromal elements in the connective tissue adjacent to the growing neoplasm.

Original languageEnglish (US)
Pages (from-to)151-160
Number of pages10
JournalExperimental and Molecular Pathology
Volume79
Issue number2
DOIs
StatePublished - Oct 2005

Keywords

  • Basal cell carcinoma
  • Collagen
  • Collagen fragments
  • Collagenase
  • Gelatinase

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Molecular Biology
  • Clinical Biochemistry

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