Formation of molecular complexes by N-methyl-D-aspartate receptor subunit NR2B and ryanodine receptor 2 in neonatal rat myocard.
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Formation of molecular complexes by N-methyl-D-aspartate receptor subunit NR2B and ryanodine receptor 2 in neonatal rat myocard. / Seeber, Silke; Humeny, Andreas; Herkert, Matthias; Rau, Thomas; Eschenhagen, Thomas; Becker, Cord-Michael.
In: J BIOL CHEM, Vol. 279, No. 20, 20, 2004, p. 21062-21068.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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T1 - Formation of molecular complexes by N-methyl-D-aspartate receptor subunit NR2B and ryanodine receptor 2 in neonatal rat myocard.
AU - Seeber, Silke
AU - Humeny, Andreas
AU - Herkert, Matthias
AU - Rau, Thomas
AU - Eschenhagen, Thomas
AU - Becker, Cord-Michael
PY - 2004
Y1 - 2004
N2 - The N-methyl-d-aspartate (NMDA) receptor is a glutamate gated cation channel prevalent in the postsynaptic membranes of central nervous system neurons. The neurotransmitter receptor complex is thought to represent a tetramer where variable NR2 or NR3 polypeptides form heteromeric assemblies with an obligatory NR1 subunit. Recently, we showed that cardiac myocytes from perinatal rats transiently express the NMDA receptor subunit NR2B, the function of which in heart is unknown. To characterize the cardiac NR2B protein, we determined its subcellular distribution and specific molecular interaction partners. By immunostaining of rat heart tissue slices and acutely dissociated cardiac myocytes, the NR2B antigen was localized at the sarcomeric Z-bands. Using immunoprecipitation of detergent-solubilized NR2B protein and subsequent analysis employing matrix-assisted laser desorption/ionization time of flight mass spectrometry, ryanodine receptor 2 was identified as a molecular interaction partner of the cardiac NR2B polypeptide. Differences in antibody recognition indicate that the cardiac NR2B polypeptide carries a structurally altered C terminus as compared with the NR2B variant prevalent in central nervous system. Based on its localization and protein interaction, the function of cardiac NR2B protein may relate to mechanosensitivity or play a role in the regulation of the contractile apparatus of neonatal heart.
AB - The N-methyl-d-aspartate (NMDA) receptor is a glutamate gated cation channel prevalent in the postsynaptic membranes of central nervous system neurons. The neurotransmitter receptor complex is thought to represent a tetramer where variable NR2 or NR3 polypeptides form heteromeric assemblies with an obligatory NR1 subunit. Recently, we showed that cardiac myocytes from perinatal rats transiently express the NMDA receptor subunit NR2B, the function of which in heart is unknown. To characterize the cardiac NR2B protein, we determined its subcellular distribution and specific molecular interaction partners. By immunostaining of rat heart tissue slices and acutely dissociated cardiac myocytes, the NR2B antigen was localized at the sarcomeric Z-bands. Using immunoprecipitation of detergent-solubilized NR2B protein and subsequent analysis employing matrix-assisted laser desorption/ionization time of flight mass spectrometry, ryanodine receptor 2 was identified as a molecular interaction partner of the cardiac NR2B polypeptide. Differences in antibody recognition indicate that the cardiac NR2B polypeptide carries a structurally altered C terminus as compared with the NR2B variant prevalent in central nervous system. Based on its localization and protein interaction, the function of cardiac NR2B protein may relate to mechanosensitivity or play a role in the regulation of the contractile apparatus of neonatal heart.
M3 - SCORING: Zeitschriftenaufsatz
VL - 279
SP - 21062
EP - 21068
JO - J BIOL CHEM
JF - J BIOL CHEM
SN - 0021-9258
IS - 20
M1 - 20
ER -