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2009 | 69 | 3 |

Tytuł artykułu

Proteomic discovery of matrix metalloproteinase-9 substrates

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Języki publikacji

EN

Abstrakty

EN
Elucidation of protease substrates (“proteodegradomes”) is essential for understanding the proteolytic pathways and their networks and thus their role in the regulation of cell function. Matrix metalloproteinase-9 (MMP-9) is expressed by the adult brain and released in response to enhanced neuronal activity. It is well established that MMP-9 is involved in neuronal plasticity, including long-term potentiation, learning and memory. Under pathological conditions, during excitotoxicity, stroke and traumatic brain injury, MMP-9 is detrimental to the brain tissue, probably because of its enhanced activity. MMP-9 is locally inhibited by endogenous tissue inhibitors of metalloproteinase 1 (TIMP-1). In the current studies we optimized the isolation of synaptoneurosomal fractions from the murine hippocampus. In order to induce MMP-9 activity the synaptoneurosomal fractions were treated with 50 μM of glutamate for 20 min. To identify MMP-9 substrates, we compared the synaptic fractions isolated from wild type and MMP-9 knockout mice by two-dimensional electrophoresis (2-DE). We have found the differences in the 2-D gel patterns. Further studies will be complemented by in-gel digestion of the protein spots of interest, mass spectrometry of the resultant peptides, and peptide mass fi ngerprinting to identify each protein.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

69

Numer

3

Opis fizyczny

p.335

Twórcy

autor
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
autor
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
autor
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland

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Bibliografia

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