Matrix metalloproteinasa-9 increases NMDA receptor lateral diffusion

• Autorzy: Michaluk P. , Mikasova L. , Groc L. , Frischknecht R. , Choquet D. , Kaczmarek L.
• Języki publikacji: EN

Abstrakty

EN

Matrix metalloproteinase-9 (MMP-9) has emerged as a physiological regulator of NMDA receptor (NMDAR)-dependent synaptic plasticity and memory. The pathways by which MMP-9 affects NMDAR signaling remain, however, not well understood. Using single Quantum Dot tracking we demonstrate that MMP-9 enzymatic activity increases NR1-NMDAR surface traffi cking but has no infl uence on AMPA receptor (AMPAR) mobility. Other extracellular protease – Cathepsin G has no effect on both NMDAR and AMPAR lateral diffusion. The mechanism of MMP-9 action on NMDAR is caused neither by change in overall extracellular matrix (ECM) structure, nor by cleavage of NMDAR subunits, but by infl uence on integrinbeta 1 signaling. These fi ndings describe a new target pathway for MMP-9 action in key physiological and pathological brain processes.

• Wydawca: -
• Czasopismo: Acta Neurobiologiae Experimentalis
• Rocznik: 2009
• Tom: 69
• Numer: 3
• Opis fizyczny: p.303

Twórcy

autor

Michaluk P.

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

autor

Mikasova L.

• Laboratory of Cellular Physiology of the Synapse, University of Bordeaux 2, Bordeaux, France

autor

Groc L.

• Laboratory of Cellular Physiology of the Synapse, University of Bordeaux 2, Bordeaux, France

autor

Frischknecht R.

• Department of Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, Magdeburg, Germany

autor

Choquet D.

• Laboratory of Cellular Physiology of the Synapse, University of Bordeaux 2, Bordeaux, France

autor

Kaczmarek L.

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