That's Swell! The Role of Aquaporin in an Inflammatory Response

Abstract

Death due to lung inflammation has increased 31 percent over the last 35 years. A protein that influences this mortality rate is aquaporin‐4. This tetramer protein is a water channel that is water permeable. This integral protein, made up of six transmembrane helices and two pore helices, creates an hourglass shape. The structure of aquaporin is vital to its function due to pore helices preventing large molecules from passing through the membrane, only facilitating the movement of water molecules or small solutes. These two pore helices allow one molecule to pass at a time, making the net water movement facilitation easier. All types of aquaporins have NPA (asparagine‐proline‐alanine) motifs which are located in the central channel and are responsible for water permeation and intracellular processing. In aquaporin‐4, there are two NPA motifs at residues 97–99 and 213–215. Scientists discovered that aquaporin's response to bacterial stimuli can alter its pore size. Trauma, toxins or injury to tissue can cause a cell to become hypotonic. Aquaporin‐4 is specifically related to lung injury and inflammation because it is highly expressed in humans. The HUHS MAPS Team (Modeling A Protein Story) has designed a model of the wild form of AQP4 with 3D printing technology to investigate structure‐function relationships. The extensive research on aquaporins in relation to lung inflammation can contribute to the scientific and medical world and eventually target new pharmacological therapies.Support or Funding InformationThe MSOE Center for BioMolecular Modeling would like to acknowledge and thank the National Institutes of Health Clinical and Translational Science Award (NIH_CTSA UL1RR031973) and the Milwaukee School of Engineering for their support in funding the 2018_2019 SMART Team program.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.