Function of cystic fibrosis-deficient protein
Researchers at Carver School of Medicine at the University of Iowa recently discovered the function of a protein. When the protein is defective or missing in the cell, it will cause cystic fibrosis (CF). This research report was published in the Journal of Biological Chemistry on December 18.
Cystic fibrosis is a chronic genetic disease that can affect the functions of multiple organs, such as lung function and digestive system function. The protein expressed by the CF-deficient gene cannot participate in the normal transmembrane transport of salt ions in the cell. The body then produces a large amount of mucus that blocks the trachea and causes chronic cough and lung infection. Intestinal involvement in food digestion.
The protein expressed by the defective gene is called cystic fibrosis transmembrane conductance regulator (CFTR) and was first discovered in 1989. Although there are great advances in the treatment of CF, the treatment can only relieve symptoms.
According to researcher Chen, to fundamentally treat cystic fibrosis, two things need to be done: one, if the CFTR is missing, the exogenous CFTR protein needs to be supplemented to the correct site of function on the cell membrane; second, if The functional defect of CFTR protein needs to restore its normal function.
CFTR protein is a small ion channel on the cell surface, responsible for the transport of chloride ions across the membrane and can regulate the transport of bicarbonate. By regulating the transport process of these molecules to maintain the acid-base balance inside and outside the cell. In this subject, the researchers confirmed that when the cells are in an acidic environment, CFTR can stimulate the transport of chloride ions, while in an alkaline environment, CFTR can inhibit the transport of chloride ions. (Bioon.com)
Bio Valley recommends the original source:
JBC July 30, 2009, doi: 10.1074 / jbc.M109.001669
Slc26a9 Is Inhibited by the R-region of the Cystic Fibrosis Transmembrane Conductance Regulator via the STAS Domain *
Min-Hwang Chang? §, 1, Consuelo Plata ??, 1, Aleksandra Sindic? §, 1, 2, Wasantha K. Ranatunga§, An-Ping Chen§, Kambiz Zandi-Nejad‖, Kim W. Chan ?, 3 , James Thompson§, David B. Mount‖ ** and Michael F. Romero? §, 4
From the? Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106,
the §Department of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, Rochester, Minnesota 55905,
the? Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, México City 14000, Mexico,
the ‖Renal Division, Brigham and Womens Hospital, Boston, Massachusetts 02115, and
the ** Renal Division, Veterans Affairs Boston Healthcare System, West Roxbury, Massachusetts 02132
SLC26 proteins function as anion exchangers, channels, and sensors. Previous cellular studies have shown that Slc26a3 and Slc26a6 interact with the R-region of the cystic fibrosis transmembrane conductance regulator (CFTR), (R) CFTR, via the Slc26-STAS (sulfate transporter anti-sigma) domain, resulting in mutual transport activation. We recently showed that Slc26a9 has both nCl? -HCO3? exchanger and Cl? channel function. In this study, we show that the purified STAS domain of Slc26a9 (a9STAS) binds purified (R) CFTR. When Slc26a9 and (R) CFTR fragments are co-expressed in Xenopus oocytes, both Slc26a9-mediated nCl? -HCO3? Exchange and Cl? Currents are almost fully inhibited. Deletion of the Slc26a9 STAS domain (a9-ΔSTAS ) virtually eliminated the Cl? currents with only a modest affect on nCl? -HCO3? exchange activity. Co-expression of a9-ΔSTAS and the (R) CFTR fragment did not alter the residual a9-ΔSTAS function. Replacing the Slc26a9 STAS domain with the Slc26a6 STAS domain (a6-a9-a6) doe s not change Slc26a9 function and is no longer inhibited by (R) CFTR. These data indicate that the Slc26a9-STAS domain, like other Slc26-STAS domains, binds CFTR in the R-region. However, unlike previously reported data, this binding interaction inhibits Slc26a9 ion transport activity. These results imply that Slc26-STAS domains may all interact with (R) CFTR but that the physiological outcome is specific to differing Slc26 proteins, allowing for dynamic and acute fine tuning of ion transport for various epithelia.
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