We investigated the membrane trafficking of AQP3 induced by epinephrine in Caco-2 cells to clarify the digestive absorption of glycerol permeated by AQP3. Epinephrine was found to promote within 60 min the translocation of AQP3 from the cytoplasmic fraction to the plasma membrane. This increased trafficking of AQP3 was suppressed by phospholipase C and protein kinase C (PKC) inhibitors and a phorbol ester accelerated the trafficking of AQP3 to the membrane fraction. In contrast, adenylyl cyclase (AC) and protein kinase A (PKA) inhibitors did not have any effect on the increased in trafficking of AQP3 by epinephrine and an AC activator did not affect the trafficking of AQP3. Phosphorylation of a threonine (514) residue in PKC was detected upon the treatment with epinephrine and the temporal transitional pattern of this phosphorylation paralleled that of the increased trafficking of AQP3. These results suggest that PKC modulates the trafficking of AQP3.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bbrc.2008.06.086 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Tamoxifen Affects Aquaporin-3 Expression and Subcellular Localization in Rat and Human Renal Collecting Ducts.
Cells
April 2023
Department of Clinical Medicine, Aarhus University, 8200 Aarhus N, Denmark.
Sex hormones play an important role in the regulation of water homeostasis, and we have previously shown that tamoxifen (TAM), a selective estrogen receptor modulator (SERM), affects the regulation of aquaporin (AQP)-2. In this study, we investigated the effect of TAM on the expression and localization of AQP3 in collecting ducts using various animal, tissue, and cell models. The impact of TAM on AQP3 regulation was studied in rats subjected to 7 days of unilateral ureteral obstruction (UUO), with the rats fed a lithium-containing diet to induce nephrogenic diabetes insipidus (NDI), as well as in human precision-cut kidney slices (PCKS).
View Article and Find Full Text PDFAQP2 trafficking in health and diseases: an updated overview.
Int J Biochem Cell Biol
August 2022
Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, Aldo Moro, Italy; Istituto Nazionale di Biostrutture e Biosistemi (I.N.B.B.), Italy. Electronic address:
Renal collecting duct principal cells play a key role in controlling body water balance. Principal cells express the water channels AQP2, AQP3, and AQP4 that mediate renal water reabsorption. AQP3 and AQP4 are expressed at the basolateral membrane constitutively.
View Article and Find Full Text PDFImmunolocalization of Metabolite Transporter Proteins in a Model Cnidarian-Dinoflagellate Symbiosis.
Appl Environ Microbiol
June 2022
School of Biological Sciences, Victoria University of Wellingtongrid.267827.e, Wellington, New Zealand.
Bidirectional nutrient flow between partners is integral to the cnidarian-dinoflagellate endosymbiosis. However, our current knowledge of the transporter proteins that regulate nutrient and metabolite trafficking is nascent. Four transmembrane transporters that likely play an important role in interpartner nitrogen and carbon exchange were investigated with immunocytochemistry in the model sea anemone ("Aiptasia"; strain NZ1): ammonium transporter 1 (AMT1), V-type proton ATPase (VHA), facilitated glucose transporter member 8 (GLUT8), and aquaporin-3 (AQP3).
View Article and Find Full Text PDFAn uncharacterized region within the N-terminus of mouse TMC1 precludes trafficking to plasma membrane in a heterologous cell line.
Sci Rep
October 2019
Department of Otolaryngology - HNS, Case Western Reserve University, Cleveland, OH, USA.
Mechanotransduction by hair cell stereocilia lies at the heart of sound detection in vertebrates. Considerable effort has been put forth to identify proteins that comprise the hair cell mechanotransduction apparatus. TMC1, a member of the transmembrane channel-like (TMC) family, was identified as a core protein of the mechanotransduction complex in hair cells.
View Article and Find Full Text PDFMolecular mechanisms regulating aquaporin-2 in kidney collecting duct.
Am J Physiol Renal Physiol
December 2016
Department of Biochemistry and Cell Biology, School of Medicine, Kyungpook National University, Taegu, Korea
The kidney collecting duct is an important renal tubular segment for regulation of body water homeostasis and urine concentration. Water reabsorption in the collecting duct principal cells is controlled by vasopressin, a peptide hormone that induces the osmotic water transport across the collecting duct epithelia through regulation of water channel proteins aquaporin-2 (AQP2) and aquaporin-3 (AQP3). In particular, vasopressin induces both intracellular translocation of AQP2-bearing vesicles to the apical plasma membrane and transcription of the Aqp2 gene to increase AQP2 protein abundance.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!