| Address: | "Departments of Pediatrics and Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, PA, 17033, USA, bmiller3@psu.edu" |
| DOI: | 10.1007/978-3-642-54215-2_3 |
| ISSN/ISBN: | 0171-2004 (Print) 0171-2004 (Linking) |
| Abstract: | "Trp2 was the second ortholog of the Drosophila trp gene to be identified. Whereas full-length TRPC2 transcripts have been cloned in a number of species including mice, rats, and New World monkeys, TRPC2 is a pseudogene in humans, apes, Old World monkeys, and in a number of other vertebrates. TRPC2 is highly expressed in the rodent VNO. It is also detectable at the protein level in murine erythroblasts, sperm, and brain and has been detected in other tissues by RT-PCR. Its activation by DAG and by erythropoietin has been described in greatest detail, and inhibition by Ca(2+)-calmodulin has been reported. The major demonstrated functions of TRPC2 are regulation of pheromone-evoked signaling in the rodent VNO, regulation of erythropoietin-stimulated calcium influx in murine erythroid cells, and ZP3-evoked calcium influx into sperm. Depletion of TRPC2 in knockout mice resulted in changes in behavior including altered sex discrimination and lack of male-male aggression. The red cells of TRPC2 knockout mice showed increased mean corpuscular volume, mean corpuscular hemoglobin, and hematocrit and reduced mean corpuscular hemoglobin concentration. TRPC2-depleted red cells were resistant to oxidative stress-induced hemolysis" |
| Keywords: | "Amino Acid Sequence Animals Cell Membrane Permeability Gene Expression Regulation Genetic Predisposition to Disease Humans Ion Channel Gating Membrane Potentials Mice Mice, Knockout Molecular Sequence Data Phenotype Protein Conformation Structure-Activity;" |
| Notes: | "MedlineMiller, Barbara A eng Review Germany 2014/04/24 Handb Exp Pharmacol. 2014; 222:53-65. doi: 10.1007/978-3-642-54215-2_3" |
