Eintrag weiter verarbeiten
Verfügbar über Online-Ressource

Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel

Gespeichert in:

Bibliographische Detailangaben
Zeitschriftentitel: Proceedings of the National Academy of Sciences
Personen und Körperschaften: Yildirim, Eda, Kawasaki, Brian T., Birnbaumer, Lutz
In: Proceedings of the National Academy of Sciences, 102, 2005, 9, S. 3307-3311
Format: E-Article
Sprache: Englisch
veröffentlicht:
Proceedings of the National Academy of Sciences
Schlagwörter:
Multidisciplinary
author_facet Yildirim, Eda
Kawasaki, Brian T.
Birnbaumer, Lutz
Yildirim, Eda
Kawasaki, Brian T.
Birnbaumer, Lutz
author Yildirim, Eda
Kawasaki, Brian T.
Birnbaumer, Lutz
spellingShingle Yildirim, Eda
Kawasaki, Brian T.
Birnbaumer, Lutz
Proceedings of the National Academy of Sciences
Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
Multidisciplinary
author_sort yildirim, eda
spelling Yildirim, Eda Kawasaki, Brian T. Birnbaumer, Lutz 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0409908102 <jats:p> AK032317 is the GenBank accession no. of a full-length RIKEN mouse cDNA. It encodes a putative variant of the C3-type TRPC (transient receptor potential channel) that differs from the previously cloned murine TRPC3 cDNA in that it has a 5′ extension stemming from inclusion of an additional exon (exon 0). The extended cDNA adds 62 aa to the sequence of the murine TRPC3. Here, we report the cloning of a cDNA encoding the human homologue of this extended TRPC3 having a highly homologous 73-aa N-terminal extension, referred to as hTRPC3a. A query of the GenBank genomic database predicts the existence of a similar gene product also in rats. Transient expression of the longer TRPC3a in human embryonic kidney (HEK) cells showed that it mediates Ca <jats:sup>2+</jats:sup> entry in response to stimulation of the Gq–phospholipase C β pathway, which is similar to that mediated by the shorter hTRPC3. However, after isolation of HEK cells expressing hTRPC3 in stable form, TRPC3a gave rise to Ca <jats:sup>2+</jats:sup> -entry channels that are not only activated by the Gq–phospholipase C β pathway (receptor-activated Ca entry) but also by thapsigargin triggered store depletion. In conjunction with findings from our and other laboratories that TRPC1, TRPC2, TRPC4, TRPC5, and TRPC7, can each mediate store-depletion-activated Ca <jats:sup>2+</jats:sup> entry in mammalian cells, our findings with hTRC3a support our previous proposal that TRPCs form capacitative Ca-entry channels. </jats:p> Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel Proceedings of the National Academy of Sciences
doi_str_mv 10.1073/pnas.0409908102
facet_avail Online
Free
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA3My9wbmFzLjA0MDk5MDgxMDI
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA3My9wbmFzLjA0MDk5MDgxMDI
institution DE-Brt1
DE-D161
DE-Zwi2
DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
DE-105
DE-14
DE-Ch1
DE-L229
DE-D275
DE-Bn3
imprint Proceedings of the National Academy of Sciences, 2005
imprint_str_mv Proceedings of the National Academy of Sciences, 2005
issn 1091-6490
0027-8424
issn_str_mv 1091-6490
0027-8424
language English
mega_collection Proceedings of the National Academy of Sciences (CrossRef)
match_str yildirim2005molecularcloningoftrpc3aannterminallyextendedstoreoperatedvariantofthehumanc3transientreceptorpotentialchannel
publishDateSort 2005
publisher Proceedings of the National Academy of Sciences
recordtype ai
record_format ai
series Proceedings of the National Academy of Sciences
source_id 49
title Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_unstemmed Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_full Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_fullStr Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_full_unstemmed Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_short Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_sort molecular cloning of trpc3a, an n-terminally extended, store-operated variant of the human c3 transient receptor potential channel
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.0409908102
publishDate 2005
physical 3307-3311
description <jats:p> AK032317 is the GenBank accession no. of a full-length RIKEN mouse cDNA. It encodes a putative variant of the C3-type TRPC (transient receptor potential channel) that differs from the previously cloned murine TRPC3 cDNA in that it has a 5′ extension stemming from inclusion of an additional exon (exon 0). The extended cDNA adds 62 aa to the sequence of the murine TRPC3. Here, we report the cloning of a cDNA encoding the human homologue of this extended TRPC3 having a highly homologous 73-aa N-terminal extension, referred to as hTRPC3a. A query of the GenBank genomic database predicts the existence of a similar gene product also in rats. Transient expression of the longer TRPC3a in human embryonic kidney (HEK) cells showed that it mediates Ca <jats:sup>2+</jats:sup> entry in response to stimulation of the Gq–phospholipase C β pathway, which is similar to that mediated by the shorter hTRPC3. However, after isolation of HEK cells expressing hTRPC3 in stable form, TRPC3a gave rise to Ca <jats:sup>2+</jats:sup> -entry channels that are not only activated by the Gq–phospholipase C β pathway (receptor-activated Ca entry) but also by thapsigargin triggered store depletion. In conjunction with findings from our and other laboratories that TRPC1, TRPC2, TRPC4, TRPC5, and TRPC7, can each mediate store-depletion-activated Ca <jats:sup>2+</jats:sup> entry in mammalian cells, our findings with hTRC3a support our previous proposal that TRPCs form capacitative Ca-entry channels. </jats:p>
container_issue 9
container_start_page 3307
container_title Proceedings of the National Academy of Sciences
container_volume 102
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792333942448193543
geogr_code not assigned
last_indexed 2024-03-01T14:20:46.742Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Molecular+cloning+of+TRPC3a%2C+an+N-terminally+extended%2C+store-operated+variant+of+the+human+C3+transient+receptor+potential+channel&rft.date=2005-03-01&genre=article&issn=1091-6490&volume=102&issue=9&spage=3307&epage=3311&pages=3307-3311&jtitle=Proceedings+of+the+National+Academy+of+Sciences&atitle=Molecular+cloning+of+TRPC3a%2C+an+N-terminally+extended%2C+store-operated+variant+of+the+human+C3+transient+receptor+potential+channel&aulast=Birnbaumer&aufirst=Lutz&rft_id=info%3Adoi%2F10.1073%2Fpnas.0409908102&rft.language%5B0%5D=eng
SOLR
_version_ 1792333942448193543
author Yildirim, Eda, Kawasaki, Brian T., Birnbaumer, Lutz
author_facet Yildirim, Eda, Kawasaki, Brian T., Birnbaumer, Lutz, Yildirim, Eda, Kawasaki, Brian T., Birnbaumer, Lutz
author_sort yildirim, eda
container_issue 9
container_start_page 3307
container_title Proceedings of the National Academy of Sciences
container_volume 102
description <jats:p> AK032317 is the GenBank accession no. of a full-length RIKEN mouse cDNA. It encodes a putative variant of the C3-type TRPC (transient receptor potential channel) that differs from the previously cloned murine TRPC3 cDNA in that it has a 5′ extension stemming from inclusion of an additional exon (exon 0). The extended cDNA adds 62 aa to the sequence of the murine TRPC3. Here, we report the cloning of a cDNA encoding the human homologue of this extended TRPC3 having a highly homologous 73-aa N-terminal extension, referred to as hTRPC3a. A query of the GenBank genomic database predicts the existence of a similar gene product also in rats. Transient expression of the longer TRPC3a in human embryonic kidney (HEK) cells showed that it mediates Ca <jats:sup>2+</jats:sup> entry in response to stimulation of the Gq–phospholipase C β pathway, which is similar to that mediated by the shorter hTRPC3. However, after isolation of HEK cells expressing hTRPC3 in stable form, TRPC3a gave rise to Ca <jats:sup>2+</jats:sup> -entry channels that are not only activated by the Gq–phospholipase C β pathway (receptor-activated Ca entry) but also by thapsigargin triggered store depletion. In conjunction with findings from our and other laboratories that TRPC1, TRPC2, TRPC4, TRPC5, and TRPC7, can each mediate store-depletion-activated Ca <jats:sup>2+</jats:sup> entry in mammalian cells, our findings with hTRC3a support our previous proposal that TRPCs form capacitative Ca-entry channels. </jats:p>
doi_str_mv 10.1073/pnas.0409908102
facet_avail Online, Free
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA3My9wbmFzLjA0MDk5MDgxMDI
imprint Proceedings of the National Academy of Sciences, 2005
imprint_str_mv Proceedings of the National Academy of Sciences, 2005
institution DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3
issn 1091-6490, 0027-8424
issn_str_mv 1091-6490, 0027-8424
language English
last_indexed 2024-03-01T14:20:46.742Z
match_str yildirim2005molecularcloningoftrpc3aannterminallyextendedstoreoperatedvariantofthehumanc3transientreceptorpotentialchannel
mega_collection Proceedings of the National Academy of Sciences (CrossRef)
physical 3307-3311
publishDate 2005
publishDateSort 2005
publisher Proceedings of the National Academy of Sciences
record_format ai
recordtype ai
series Proceedings of the National Academy of Sciences
source_id 49
spelling Yildirim, Eda Kawasaki, Brian T. Birnbaumer, Lutz 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0409908102 <jats:p> AK032317 is the GenBank accession no. of a full-length RIKEN mouse cDNA. It encodes a putative variant of the C3-type TRPC (transient receptor potential channel) that differs from the previously cloned murine TRPC3 cDNA in that it has a 5′ extension stemming from inclusion of an additional exon (exon 0). The extended cDNA adds 62 aa to the sequence of the murine TRPC3. Here, we report the cloning of a cDNA encoding the human homologue of this extended TRPC3 having a highly homologous 73-aa N-terminal extension, referred to as hTRPC3a. A query of the GenBank genomic database predicts the existence of a similar gene product also in rats. Transient expression of the longer TRPC3a in human embryonic kidney (HEK) cells showed that it mediates Ca <jats:sup>2+</jats:sup> entry in response to stimulation of the Gq–phospholipase C β pathway, which is similar to that mediated by the shorter hTRPC3. However, after isolation of HEK cells expressing hTRPC3 in stable form, TRPC3a gave rise to Ca <jats:sup>2+</jats:sup> -entry channels that are not only activated by the Gq–phospholipase C β pathway (receptor-activated Ca entry) but also by thapsigargin triggered store depletion. In conjunction with findings from our and other laboratories that TRPC1, TRPC2, TRPC4, TRPC5, and TRPC7, can each mediate store-depletion-activated Ca <jats:sup>2+</jats:sup> entry in mammalian cells, our findings with hTRC3a support our previous proposal that TRPCs form capacitative Ca-entry channels. </jats:p> Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel Proceedings of the National Academy of Sciences
spellingShingle Yildirim, Eda, Kawasaki, Brian T., Birnbaumer, Lutz, Proceedings of the National Academy of Sciences, Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel, Multidisciplinary
title Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_full Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_fullStr Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_full_unstemmed Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_short Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
title_sort molecular cloning of trpc3a, an n-terminally extended, store-operated variant of the human c3 transient receptor potential channel
title_unstemmed Molecular cloning of TRPC3a, an N-terminally extended, store-operated variant of the human C3 transient receptor potential channel
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.0409908102