Matrix metalloproteinase-7 (matrilysin) controls neutrophil egress by generating chemokine gradients

J Leukoc Biol. 2008 Jun;83(6):1404-12. doi: 10.1189/jlb.0108016. Epub 2008 Mar 11.

Abstract

Matrilysin [matrix metalloproteinase 7 (MMP7)] is induced by mucosal injury of many tissues. To assess function of this proteinase, we subjected wild-type and Mmp7(-/-) mice to acute colon injury. When matrilysin expression was increasing, 73% of wild-type mice died, whereas only 32% of Mmp7(-/-) mice succumbed. Although re-epithelialization was delayed in Mmp7(-/-) mice, overall injury did not differ markedly between genotypes. We hypothesized that differences in acute inflammation caused increased mortality in wild-type mice. Indeed, whereas overall neutrophil influx into tissue was similar in wild-type and Mmp7(-/-) mice, their location and extent of migration differed between genotypes. Neutrophils were dispersed throughout the mucosa and within the lumen of wild-type mice, but these leukocytes were largely confined to the submucosa in Mmp7(-/-) mice. The levels of neutrophil chemokines, keratinocyte-derived chemokine and MIP-2, increased in the colon tissue of both genotypes, but these factors were detected only in lumenal lavages of wild-type mice. Our findings indicate that matrilysin mediates beneficial and deleterious effects in response to injury. On one hand, it promotes re-epithelialization, but it also controls the transepithelial influx of neutrophils, which if excessive, can lead to tissue damage.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Movement
  • Chemokines / biosynthesis*
  • Colitis / immunology
  • Colon / pathology
  • Matrix Metalloproteinase 7 / genetics
  • Matrix Metalloproteinase 7 / physiology*
  • Mice
  • Mice, Inbred C57BL
  • Neutrophils / physiology*
  • Peroxidase / analysis
  • RNA, Messenger / analysis

Substances

  • Chemokines
  • RNA, Messenger
  • Peroxidase
  • Matrix Metalloproteinase 7