, 16:1205

Suppression of matrix metalloproteinase-9 expression in undifferentiated, non-apoptotic keratinocytes is abrogated by the cleavage of poly(ADP-ribose) polymerase-1

Original Paper

DOI: 10.1007/s10495-011-0650-9

Cite this article as:
Kobayashi, T. Apoptosis (2011) 16: 1205. doi:10.1007/s10495-011-0650-9


Matrix metalloproteinase (MMP)-9, an enzyme that degrades the extracellular matrix, has been implicated as a key enzyme in the process of tissue remodeling. This study demonstrates the regulation of MMP-9 transcription through a gene regulatory element in its promoter (the KRE-M9 element). The KRE-M9-binding protein was purified and identified as poly(ADP-ribose) polymerase-1 (PARP-1), which inhibits the transcription of MMP-9 similar to involucrin. This regulation occurs in non-apoptotic keratinocytes using the distinctive culture conditions of high and low Ca2+ levels. PARP cleavage, which occurs during apoptosis, results in de-repression of MMP-9 promoter activity. These data clarify a new role of PARP-1 and suggest a physiologically relevant connection between caspase activation and MMP-9 expression.


KeratinocyteMMP-9PARP-1CaspaseInvolucrinApoptosisCell differentiation

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  1. 1.Department of DermatologyNational Defense Medical CollegeSaitamaJapan