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Role of the TRPC4 proline rich region in regulation of the endothelial store‐operated calcium entry
Author(s) -
Wang Xiaogan,
Chen Hairu,
Wu Songwei,
Cioffi Donna L.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.1130.8
Subject(s) - trpc , trpc3 , transient receptor potential channel , phosphorylation , trpc1 , trpc5 , microbiology and biotechnology , chemistry , voltage dependent calcium channel , calcium , biology , biochemistry , receptor , organic chemistry
Endothelial cells line blood vessels and form a semi‐permeable barrier between blood and underlying tissues. Calcium entry through store‐operated calcium (SOC) channels mediates endothelial gap formation. The endothelial I SOC channel is a calcium‐selective SOC channel, and transient receptor potential canonical (TRPC) proteins are subunit candidates. While it is known that phosphorylation negatively regulates TRPC3 channel activity, the role of TRPC phosphorylation in regulation of the endothelial I SOC channel is unknown. Therefore we performed the Phos‐tag™‐based detection of phosphorylation with rat pulmonary artery endothelial cells (PAEC). We found that among TRPC1, TRPC3 and TRPC4, TRPC4 is the major phosphorylation target in the endothelial I SOC channel. TRPC4 carries a conserved serine in the proline rich region (PRR) as a putative phosphorylation site close to the channel pore. Transfection of the TRPC4 PRR peptide into PAECs suppressed the SOC entry and I SOC current. Collectively these data suggest that TRPC4 PRR regulates the endothelial SOC entry possibly through phosphorylation at the serine residue. Supported by 5R00HL089361.