| First Author | Glitsch M | Year | 1996 |
| Journal | Pflugers Arch | Volume | 432 |
| Issue | 1 | Pages | 134-43 |
| PubMed ID | 8662278 | Mgi Jnum | J:34025 |
| Mgi Id | MGI:81503 | Doi | 10.1007/s004240050115 |
| Citation | Glitsch M, et al. (1996) Functional characterization of two 5-HT3 receptor splice variants isolated from a mouse hippocampal cell line. Pflugers Arch 432(1):134-43 |
| abstractText | Two splice variants of the ligand-gated 5- hydroxytryptamine or serotonin 5-HT3 receptor that differ in a six-amino-acid deletion were cloned by polymerase chain reaction from the hippocampus x neuroblastoma cell line HN9.10e. When expressed in Xenopus oocytes, both variants individually formed 5-HT3 receptors that revealed no significant differences in current responses to the agonists 5-HT and 1-phenylbiguanide and block by the specific antagonist LY-278,584-maleate. For both receptors, the monovalent cations Na+, K+, Rb+ and Li+ showed the same relative permeability; NH4+ permeated approximate to 2.7 times better than Na+, and Tris(+) was only poorly permeable. In contrast to other reports, the receptors were completely and reversibly blocked by extracellular Cs+ in both oocytes and native HN9.10 cells. Moreover, Ca2+ was not permeant and exhibited a concentration-dependent decrease (0.9-18 mM) of the 5-HT- induced currents without affecting the inward rectification of the current/voltage relation. The two receptors were reversibly inhibited by nanomolar concentrations of the specific inhibitor of protein kinase C (PKC) bisindolylmaleimide, but not by the equipotent and less specific inhibitor staurosporine. A regulatory effect on both 5-HT3 receptor subunits by PKC-mediated protein phosphorylation might be possible, however a functional role of the two splice variants present in one cell remains to be determined. |
