Genetic Mapping of Mouse Transient Receptor Potential (Trrp) Genes Responsible for Capacitative Calcium Entry Channels to Chromosomes 3, 7, 9, and X

Genomics ◽  
1998 ◽  
Vol 51 (2) ◽  
pp. 303-305 ◽  
Author(s):  
Kazuto Yamazaki ◽  
Takaharu Okada ◽  
Yasuo Mori ◽  
Isao Tanaka
Keyword(s):  
Genetic Mapping ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Transient Receptor

scholarly journals Molecular cloning and immunolocalization of a novel vertebrate trp homologue from Xenopus

1999 ◽  
Vol 340 (3) ◽  
pp. 593-599 ◽  
Author(s):  
Laura K. BOBANOVIĆ ◽  
Mika LAINE ◽  
Carl C. H. PETERSEN ◽  
Deborah L. BENNETT ◽  
Michael J. BERRIDGE ◽  
...  
Keyword(s):  
Antisense Oligonucleotides ◽  
Xenopus Oocytes ◽  
Transient Receptor Potential ◽  
Polyclonal Antibodies ◽  
Sequence Similarity ◽  
Receptor Potential ◽  
Calcium Entry ◽  
Capacitative Calcium Entry ◽  
Sequence Structure ◽  
Transient Receptor

We report the sequence, structure and distribution of a novel transient receptor potential (trp) homologue from Xenopus, Xtrp, determined by screening an oocyte cDNA library. On the basis of sequence similarity and predicted structure, Xtrp appears to be a homologue of mammalian trp1 proteins. Two polyclonal antibodies raised against distinct regions of the Xtrp sequence revealed Xtrp expression in various Xenopus tissues, and the localization of Xtrp at the plasma membrane of Xenopus oocytes and HeLa cells. Since capacitative calcium entry into Xenopus oocytes has been shown previously to be substantially inhibited by trp1 antisense oligonucleotides [Tomita, Kaneko, Funayama, Kondo, Satoh and Akaike (1998) Neurosci. Lett. 248, 195-198] we suggest that Xtrp may underlie capacitative calcium entry in Xenopus tissues.

Expression and relative abundance of short transient receptor potential channels in the rat renal microcirculation

2004 ◽  
Vol 286 (3) ◽  
pp. F546-F551 ◽  
Author(s):  
Carie S. Facemire ◽  
Peter J. Mohler ◽  
William J. Arendshorst
Keyword(s):  
Relative Abundance ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Cell Types ◽  
Calcium Entry ◽  
Transient Receptor Potential Channels ◽  
Trpc Channels ◽  
Renal Microcirculation ◽  
Resistance Vessels ◽  
Transient Receptor

In the resistance vessels of the renal microcirculation, store- and/or receptor-operated calcium entry contribute to the rise in vascular smooth muscle cell (VSMC) intracellular calcium concentration in response to vasoconstrictor hormones. Short transient receptor potential (TRPC) channels are widely expressed in mammalian tissues and are proposed mediators of voltage-independent cation entry in multiple cell types, including VSMCs. The seven members of the TRPC gene family (TRPC1-7) encode subunit proteins that are thought to form homo- and heterotetrameric channels that are differentially regulated depending on their subunit composition. In the present study, we demonstrate the relative abundance of TRPC mRNA and protein in freshly isolated rat renal resistance vessels, glomeruli, and aorta. TRPC1, 3, 4, 5, and 6 mRNA and protein were detected in both renal resistance vessels and aorta, whereas TRPC2 and TRPC7 mRNA were not expressed. TRPC1, 3, 5, and 6 protein was present in glomeruli. TRPC3 and TRPC6 protein levels were significantly greater in the renal resistance vessels, about six- to eightfold higher than in aorta. These data suggest that TRPC3 and TRPC6 may play a role in mediating voltage-independent calcium entry in renal resistance vessels that is functionally distinct from that in aorta.

The Canonical Transient Receptor Potential 6 Channel as a Putative Phosphatidylinositol 3,4,5-Trisphosphate-Sensitive Calcium Entry System†

Biochemistry ◽  
2004 ◽  
Vol 43 (37) ◽  
pp. 11701-11708 ◽  
Author(s):  
Ping-Hui Tseng ◽  
Ho-Pi Lin ◽  
Hongzhen Hu ◽  
Chunbo Wang ◽  
Michael Xi Zhu ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Calcium Entry ◽  
Canonical Transient Receptor Potential ◽  
Transient Receptor

Cloning, expression and subcellular localization of two novel splice variants of mouse transient receptor potential channel 2

2000 ◽  
Vol 351 (1) ◽  
pp. 115-122 ◽  
Author(s):  
Thomas HOFMANN ◽  
Michael SCHAEFER ◽  
Günter SCHULTZ ◽  
Thomas GUDERMANN
Keyword(s):  
Membrane Trafficking ◽  
Fusion Proteins ◽  
Transient Receptor Potential ◽  
Splice Variants ◽  
Receptor Potential ◽  
Calcium Entry ◽  
Transient Receptor Potential Channels ◽  
Protein Fusion ◽  
Hek 293 ◽  
Transient Receptor

Transient receptor potential channels (TRPCs) are known as candidate molecular correlates of receptor-activated or store-operated calcium entry. While functional roles for most TRPCs have been suggested, the physiological relevance of TRPC2 remains obscure. Whereas human and bovine TRPC2 are candidate pseudogenes, full-length rodent TRPC2 transcripts have been reported. There is, however, considerable controversy concerning mRNA splicing, tissue distribution and the function of these proteins. We report the molecular cloning of two novel murine TRPC2 splice variants, mTRPC2α and mTRPC2β. mTRPC2α RNA is expressed at low levels in many tissues and cell systems, while mTRPC2β is exclusively and abundantly expressed in the vomeronasal organ (VNO). When expressed in human embryonic kidney (HEK)-293 cells, mTRPC2 did not enhance receptor- or store-activated calcium entry. In order to investigate the basis of such a functional defect, mTRPC2–green fluorescent protein fusion proteins were examined by confocal microscopy. Fusion proteins were retained in endomembranes when expressed in HEK-293 or other cells of epithelial or neuronal origin. Co-expression of TRPC2 with other TRPCs did not restore plasma-membrane trafficking. We conclude that TRPC2 may form functional channels in the cellular context of the VNO, but is unlikely to have a physiological function in other tissues. The sequences of mTRPC2α and mTRPC2β have been submitted to GenBank under the accession numbers AF230802 and AF230803 respectively.

scholarly journals Cell-Derived Vesicles as TRPC1 Channel Delivery Systems for the Recovery of Cellular Respiratory and Proliferative Capacities

2020 ◽  
Author(s):  
Felix Kurth ◽  
Yee Kit Tai ◽  
Dinesh Parate ◽  
Marc van Oostrum ◽  
Yannick R. F. Schmid ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Trp Channels ◽  
Surface Membrane ◽  
Receptor Potential ◽  
Calcium Entry ◽  
Wild Type ◽  
Clonal Cell Lines ◽  
Cellular Machinery ◽  
Pulsed Electromagnetic ◽  
Transient Receptor

AbstractPulsed electromagnetic fields (PEMFs) are capable of specifically activating a TRPC1-mitochondrial axis underlying cell expansion and mitohormetic survival adaptations. This study characterizes cell-derived vesicles (CDVs) generated from C2C12 murine myoblasts and shows that they are equipped with the sufficient molecular machinery to confer mitochondrial respiratory capacity and associated proliferative responses upon their fusion with recipient cells. CDVs derived from wild type C2C12 myoblasts include the cation-permeable transient receptor potential (TRP) channels, TRPC1 and TRPA1, and directly respond to PEMF exposure with TRPC1-mediated calcium entry. By contrast, CDVs derived from C2C12 muscle cells in which TRPC1 had been genetically knocked-down using CRISPR/Cas9 genome editing, do not. Wild type C2C12-derived CDVs are also capable of restoring PEMF-induced proliferative and mitochondrial activation in two C2C12-derived TRPC1 knockdown clonal cell lines in accordance to their endogenous degree of TRPC1 suppression. C2C12 wild type CDVs respond to menthol with calcium entry and accumulation, likewise verifying TRPA1 functional gating and further corroborating compartmental integrity. Proteomic and lipidomic analyses confirm the surface membrane origin of the CDVs providing an initial indication of the minimal cellular machinery required to recover mitochondrial function. CDVs hence possess the potential of restoring respiratory and proliferative capacities to senescent cells and tissues.

Sign in / Sign up

Export Citation Format

Share Document