Affiliation:
1. From the School of Biomedical Sciences, University of Leeds, Leeds, UK.
Abstract
Abstract
—Mammalian counterparts of the
Drosophila trp
gene have been suggested to encode store-operated Ca
2+
channels. These specialized channels are widely distributed and may have a general function to reload Ca
2+
into sarcoplasmic reticulum as well as specific functions, including the control of cell proliferation and muscle contraction. Heterologous expression of mammalian
trp
genes enhances or generates Ca
2+
channel activity, but the crucial question of whether any of the genes encode native subunits of store-operated channels remains unanswered. We have investigated if TrpC1 protein (encoded by
trp1
gene) is a store-operated channel in freshly isolated smooth muscle cells of resistance arterioles, arteries, and veins from human, mouse, or rabbit. Messenger RNA encoding TrpC1 was broadly expressed. TrpC1-specific antibody targeted to peptide predicted to contribute to the outer vestibule of TrpC1 channels revealed that TrpC1 is localized to the plasma membrane and has an extracellular domain. Peptide-specific binding of the antibody had a functional effect, selectively blocking store-operated Ca
2+
channel activity. The antibody is a powerful new tool for the study of mammalian
trp1
gene product. The study shows that TrpC1 is a novel physiological Ca
2+
channel subunit in arterial smooth muscle cells.
Publisher
Ovid Technologies (Wolters Kluwer Health)
Subject
Cardiology and Cardiovascular Medicine,Physiology
Cited by
331 articles.
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