Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism

Article Abstract:

Research was conducted to show that the calcium regulatory protein called calmodulin coprecipitates with L-selectin and binds directly to the cytoplasmic tail of L-selectin. Cells were prepared with trifluoperazine and paraformaldehyde while L-selectin mutants were determined using an oligonucleotide-directed mutagenesis system. Results indicated that epitopes on the cytoplasmic tail and the extracellular membrane proximal cleavage region of L-selectin was not functionally linked.

Proteins, Cell research, Cytological research

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Importance of the intracellular domain of NR2 subunits for NMDA receptor function in vivo

Article Abstract:

Research was conducted to study the importance of the intracellular domain of NR2 subunits for methyl aspartate receptor function in vivo. Genomic DNA was isolated from cell clones while mice brains were homogenized in lysis buffer and sucrose. NR2 genes were also manipulated by electroporation and were identified by polymerase chain reaction. Results showed that the synaptic activation of receptor channels led to postsynaptic elevations of the intracellular Ca2+ concentration.

Calcium ions, Brain research, Methyl aspartate, N-methyl-D-aspartate

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Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit

Article Abstract:

Calmodulin may regulate the functioning of N-methyl-D-aspartate (NMDA) receptors by binding to the receptor's NR1 subunit. NMDA receptors are calcium ion channels that are highly permeable to extracellular calcium. Calmodulin readily binds with two sites in the NR1 subunit and reduces the amount of time in which the receptor gate is open to admit calcium ions. However, the absence of calcium outside the cell also limits the action of calmodulin.

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