Molecular Candidates for Capacitative and Non-Capacitative Ca2+ Entry in Smooth Muscle

  1. Derek J. Chadwick Organizer and
  2. Jamie A. Goode
  1. Ryuji Inoue1 and
  2. Yasuo Mori2

Published Online: 7 OCT 2008

DOI: 10.1002/0470853050.ch7

Role Of The Sarcoplasmic Reticulum In Smooth Muscle: Novartis Foundation Symposium 246

Role Of The Sarcoplasmic Reticulum In Smooth Muscle: Novartis Foundation Symposium 246

How to Cite

Inoue, R. and Mori, Y. (2002) Molecular Candidates for Capacitative and Non-Capacitative Ca2+ Entry in Smooth Muscle, in Role Of The Sarcoplasmic Reticulum In Smooth Muscle: Novartis Foundation Symposium 246 (eds D. J. Chadwick and J. A. Goode), John Wiley & Sons, Ltd, Chichester, UK. doi: 10.1002/0470853050.ch7

Author Information

  1. 1

    Department of Pharmacology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan

  2. 2

    School of Life Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan

Publication History

  1. Published Online: 7 OCT 2008
  2. Published Print: 15 JUN 2002

Book Series:

  1. Novartis Foundation Symposia

Book Series Editors:

  1. Novartis Foundation

ISBN Information

Print ISBN: 9780470844793

Online ISBN: 9780470853054

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Summary

Recent investigations have revealed that mammalian homologues of transient receptor potential (TRP) protein (TRP1-7) are promising candidates for Ca2+ entry mechanisms (or channels) associated with various metabotropic G protein-coupled receptors (GPCRs) in smooth muscle, stimulation of which generates lipid second messengers and depletes internal stores. RT-PCR and immunocytochemical experiments have demonstrated that although the level of expression varies depending on tissues, the major TRP isoforms expressed in smooth muscle are TRP4, 6 and 7. In some vascular preparations, the significant expression of TRP1 mRNA and protein is also detected. Consistent with these findings, recent functional studies using TRP6- and TRP1-specific antisense oligonucleotides and antibodies have suggested that TRP6 is the essential component of α1-adrenoceptor activated, store depletion-independent Ca2+ entry channels, while TRP1 is partly involved in Ca2+ entry associated with store depletion or capacitative Ca2+ entry. In addition, coexpression of different TRP isoforms results in the appearance of cation channels showing novel properties reminiscent of some native GPCR-activated Ca2+-permeable non-selective cation channels. Thus, at present, TRP proteins may be the most important clues for elucidating the molecular entities of receptor- and store-operated Ca2+ entry mechanisms in smooth muscle and their roles in smooth muscle functions.