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2009 | 69 | 3 |

Tytuł artykułu

MMP-9 activation after neuronal stimulation is a polyadenylation dependent process

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Języki publikacji

EN

Abstrakty

EN
Recent studies indicate that MMP-9 (gelatinase B that regulates pericellular environment through the cleavage of protein components of the extracellular matrix) plays a role in synaptic plasticity. Szklarc zyk et al. (2002), Konopacki et al. (2008) and Wilczynski et al. (2008) have demonstrated the presence of mRNA and protein for MMP-9 at postsynaptic sides of rat hippocampal neurons. It was also shown by Michaluk et al. (2007) that gelatinolytic activity of MMP9 increases after stimulation of rat neuronal cultures with either glutamate or bicuculine. We observed the presence of MMP-9 protein and mRNA in synaptoneurosomes, the synaptic fraction isolated from hippocampus. To detect the activity of MMP-9 we measured the cleavage of its substrate, β-dystroglycan. By the use of this readout we showed that MMP-9 is activated 5 to 10 mintes after neuronal stimulation. We postulate here that MMP-9 is translated from dendritically-localized mRNA and the protein is produced in response to synaptic stimulation. Its rapid and local translation and secretion is a polyadenylation- and local translation-dependent process.

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Wydawca

-

Rocznik

Tom

69

Numer

3

Opis fizyczny

p.337

Twórcy

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

Bibliografia

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Bibliografia

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