Molecular cloning and immunolocalization of a novel vertebrate trp homologue from Xenopus.
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.
Bobanovic
L K
LK
Laboratory of Molecular Signalling, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK.
Laine
M
M
Petersen
C C
CC
Bennett
D L
DL
Berridge
M J
MJ
Lipp
P
P
Ripley
S J
SJ
Bootman
M D
MD
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D001483:Base Sequence; D002148:Calmodulin-Binding Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D002462:Cell Membrane / Q000737:chemistry; D003001:Cloning, Molecular; D029721:Drosophila Proteins; D015723:Gene Library; D006367:HeLa Cells; D006801:Humans; D007150:Immunohistochemistry; D008565:Membrane Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009865:Oocytes / Q000166:cytology / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D050051:Transient Receptor Potential Channels; D014982:Xenopus laevis / Q000235:genetics*
D000906:Antibodies; D002148:Calmodulin-Binding Proteins; D029721:Drosophila Proteins; D008565:Membrane Proteins; D050051:Transient Receptor Potential Channels; C074192:trpl protein, Drosophila