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      Functional interaction between TRP4 and CFTR in mouse aorta endothelial cells

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          Abstract

          Background

          This study describes the functional interaction between the putative Ca 2+ channel TRP4 and the cystic fibrosis transmembrane conductance regulator, CFTR, in mouse aorta endothelium (MAEC).

          Results

          MAEC cells express CFTR transcripts as shown by RT-PCR analysis. Application of a phosphorylating cocktail activated a Cl - current with characteristics similar to those of CFTR mediated currents in other cells types (slow activation by cAMP, absence of rectification, block by glibenclamide). The current is present in trp4 +/+ MAEC, but not in trp4 -/- cells, although the expression of CFTR seems unchanged in the trp4 deficient cells as judged from RT-PCR analysis.

          Conclusions

          It is concluded that TRP4 is necessary for CFTR activation in endothelium, possibly by providing a scaffold for the formation of functional CFTR channels.

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          Most cited references29

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          Identification of EBP50: A PDZ-containing Phosphoprotein that Associates with Members of the Ezrin-Radixin-Moesin Family

          David Reczek, Mark Berryman, Anthony Bretscher (1997)
          Members of the ezrin-radixin-moesin (ERM) family of membrane–cytoskeletal linking proteins have NH2- and COOH-terminal domains that associate with the plasma membrane and the actin cytoskeleton, respectively. To search for ERM binding partners potentially involved in membrane association, tissue lysates were subjected to affinity chromatography on the immobilized NH2-terminal domains of ezrin and moesin, which comprise the ezrin-radixin-moesin–association domain (N-ERMAD). A collection of polypeptides at 50–53 kD from human placenta and at 58-59 kD from bovine brain bound directly to both N-ERMADs. The 50–53-kD placental proteins migrated as a major 50-kD species after phosphatase treatment, indicating that the heterogeneity is due to different phosphorylation states. We refer to these polypeptides as ERM-binding phosphoprotein 50 (EBP50). Sequence analysis of human EBP50 was used to identify an ∼2-kb human cDNA that encodes a 357-residue polypeptide. Recombinant EBP50 binds tightly to the N-ERMADs of ezrin and moesin. Peptide sequences from the brain candidate indicated that it is closely related to EBP50. EBP50 has two PSD-95/DlgA/ZO-1–like (PDZ) domains and is most likely a homologue of rabbit protein cofactor, which is involved in the protein kinase A regulation of the renal brush border Na+/H+ exchanger. EBP50 is widely distributed in tissues, and is particularly enriched in those containing polarized epithelia. Immunofluorescence microscopy of cultured cells and tissues revealed that EBP50 colocalizes with actin and ezrin in the apical microvilli of epithelial cells, and immunoelectron microscopy demonstrated that it is specifically associated with the microvilli of the placental syncytiotrophoblast. Moreover, EBP50 and ezrin can be coimmunoprecipitated as a complex from isolated human placental microvilli. These findings show that EBP50 is a physiologically relevant ezrin binding protein. Since PDZ domains are known to mediate associations with integral membrane proteins, one mode of membrane attachment of ezrin is likely to be mediated through EBP50.
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            Properties of volume-regulated anion channels in mammalian cells.

            Bernd Nilius, Jan Eggermont, Thomas Voets … (1997)
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              Membrane targeting of cGMP-dependent protein kinase is required for cystic fibrosis transmembrane conductance regulator Cl- channel activation.

              B Tilly, A Bot, Grant Smolenski … (1998)
              A recently cloned isoform of cGMP-dependent protein kinase (cGK), designated type II, was implicated as the mediator of cGMP-provoked intestinal Cl- secretion based on its localization in the apical membrane of enterocytes and on its capacity to activate cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channels. In contrast, the soluble type I cGK was unable to activate CFTR in intact cells, although both cGK I and cGK II could phosphorylate CFTR in vitro. To investigate the molecular basis for the cGK II isotype specificity of CFTR channel gating, we expressed cGK II or cGK I mutants possessing different membrane binding properties by using adenoviral vectors in a CFTR-transfected intestinal cell line, and we examined the ability of cGMP to phosphorylate and activate the Cl- channel. Mutation of the cGK II N-terminal myristoylation site (Gly2 --> Ala) reduced cGK II membrane binding and severely impaired cGK II activation of CFTR. Conversely, a chimeric protein, in which the N-terminal membrane-anchoring domain of cGK II was fused to the N terminus of cGK Ibeta, acquired the ability to associate with the membrane and activate the CFTR Cl- channel. The potency order of cGK constructs for activation of CFTR (cGK II > membrane-bound cGK I chimer > nonmyristoylated cGK II > cGK Ibeta) correlated with the extent of 32P incorporation into CFTR observed in parallel measurements. These results strongly support the concept that membrane targeting of cGK is a major determinant of CFTR Cl- channel activation in intact cells.
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                Author and article information

                Journal
                Journal ID (nlm-ta): BMC Physiol
                Title: BMC Physiology
                Publisher: BioMed Central (London )
                ISSN (Electronic): 1472-6793
                Publication date Collection: 2001
                Publication date (Electronic): 15 May 2001
                Volume: 1
                Page: 3
                Affiliations
                [1 ]Department of Physiology, Campus Gasthuisberg, KU Leuven, Leuven, Belgium.
                [2 ]Institut für Pharmakologie und Toxikologie, Universität des Saarlandes, D-66421 Homburg, Germany.
                [3 ]Center for Human Genetics, Campus Gasthuisberg, KU Leuven, Leuven, Belgium.
                Article
                Publisher ID: 1472-6793-1-3
                PMC ID: 32182
                PubMed ID: 11356184
                SO-VID: f491e6d9-1cb2-4076-8b4b-d883fc48f0f8
                Copyright © Copyright © 2001 Wei et al, licensee BioMed Central Ltd.
                History
                Date received : 30 March 2001
                Date accepted : 15 May 2001
                Categories
                Subject: Research Article

                ScienceOpen disciplines: Anatomy & Physiology
                Data availability:
                ScienceOpen disciplines: Anatomy & Physiology

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