Cleavage of neuronal synaptosomal-associated protein of 25 kDa by exogenous matrix metalloproteinase-7

Arek Szklarczyk, George Oyler, Ron McKay, Charles Gerfen, Katherine Conant

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Matrix metalloproteinases (MMPs) belong to a family of zinc dependent enzymes best studied for their role in cancer and inflammation. Though MMPs typically target extracellular proteins, here we show that MMP-7, an MMP family member which lacks a C-terminal hemopexin-like domain, can cleave an intraneuronal protein that is critical to vesicular fusion and neurotransmitter release, synaptosomal-associated protein of 25 kDa (SNAP-25). Western blot analysis using an N-terminal specific antibody on extracts from cultured neurons suggests that cleavage occurs towards the C-terminal portion of SNAP 25. Additional studies with recombinant SNAP-25 demonstrate that cleavage occurs at amino acid 129. The ability of MMP-7 to cleave SNAP-25 is diminished by chlorpromazine and phenylarsine oxide, inhibitors of clathrin dependent endocytosis. Together, these results imply that exogenous MMP-7 can access an intraneuronal substrate and suggest that additional studies may be warranted to determine if SNAP function is impaired with brain inflammation.

Original languageEnglish (US)
Pages (from-to)1256-1263
Number of pages8
JournalJournal of Neurochemistry
Issue number4
StatePublished - Aug 2007
Externally publishedYes


  • Endocytosis
  • Matrilysin
  • Matrix metalloproteinase-7
  • Neuron
  • Synaptosomal-associated protein of 25 kDa

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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