[HTML][HTML] The serine protease plasmin cleaves the amino-terminal domain of the NR2A subunit to relieve zinc inhibition of the N-methyl-D-aspartate receptors
Zinc is hypothesized to be co-released with glutamate at synapses of the central nervous
system. Zinc binds to NR1/NR2A N-methyl-d-aspartate (NMDA) receptors with high affinity
and inhibits NMDAR function in a voltage-independent manner. The serine protease
plasmin can cleave a number of substrates, including protease-activated receptors, and may
play an important role in several disorders of the central nervous system, including ischemia
and spinal cord injury. Here, we demonstrate that plasmin can cleave the native NR2A …
system. Zinc binds to NR1/NR2A N-methyl-d-aspartate (NMDA) receptors with high affinity
and inhibits NMDAR function in a voltage-independent manner. The serine protease
plasmin can cleave a number of substrates, including protease-activated receptors, and may
play an important role in several disorders of the central nervous system, including ischemia
and spinal cord injury. Here, we demonstrate that plasmin can cleave the native NR2A …
