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      Association of Plasminuria with Overhydration in Patients with CKD

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          Abstract

          Hypervolemia is a common feature of patients with CKD and associated with hypertension. Recent work has shown stimulation of sodium retention by urinary plasmin during nephrotic syndrome. However, it is unclear whether plasminuria plays a role in patients with stable CKD and non-nephrotic proteinuria.

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          Plasmin in nephrotic urine activates the epithelial sodium channel.

          Per Svenningsen, Claus Bistrup, Ulla G Friis … (2009)
          Proteinuria and increased renal reabsorption of NaCl characterize the nephrotic syndrome. Here, we show that protein-rich urine from nephrotic rats and from patients with nephrotic syndrome activate the epithelial sodium channel (ENaC) in cultured M-1 mouse collecting duct cells and in Xenopus laevis oocytes heterologously expressing ENaC. The activation depended on urinary serine protease activity. We identified plasmin as a urinary serine protease by matrix-assisted laser desorption/ionization time of-flight mass spectrometry. Purified plasmin activated ENaC currents, and inhibitors of plasmin abolished urinary protease activity and the ability to activate ENaC. In nephrotic syndrome, tubular urokinase-type plasminogen activator likely converts filtered plasminogen to plasmin. Consistent with this, the combined application of urokinase-type plasminogen activator and plasminogen stimulated amiloride-sensitive transepithelial sodium transport in M-1 cells and increased amiloride-sensitive whole-cell currents in Xenopus laevis oocytes heterologously expressing ENaC. Activation of ENaC by plasmin involved cleavage and release of an inhibitory peptide from the ENaC gamma subunit ectodomain. These data suggest that a defective glomerular filtration barrier allows passage of proteolytic enzymes that have the ability to activate ENaC.
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            ENaC at the cutting edge: regulation of epithelial sodium channels by proteases.

            Marcelo Carattino, Thomas Kleyman, Rebecca Hughey (2009)
            Epithelial Na+ channels facilitate the transport of Na+ across high resistance epithelia. Proteolytic cleavage has an important role in regulating the activity of these channels by increasing their open probability. Specific proteases have been shown to activate epithelial Na+ channels by cleaving channel subunits at defined sites within their extracellular domains. This minireview addresses the mechanisms by which proteases activate this channel and the question of why proteolysis has evolved as a mechanism of channel activation.
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              Activation of the epithelial sodium channel (ENaC) by serine proteases.

              M. Stutts, Bernard C Rossier (2008)
              The study of human monogenic diseases [pseudohypoaldosteronism type 1 (PHA-1) and Liddle's syndrome] as well as mouse models mimicking the salt-losing syndrome (PHA-1) or salt-sensitive hypertension (Liddle's syndrome) have established the epithelial sodium channel ENaC as a limiting factor in vivo in the control of ionic composition of the extracellular fluid, regulation of blood volume and blood pressure, lung alveolar clearance, and airway mucociliary clearance. In this review, we discuss more specifically the activation of ENaC by serine proteases. Recent in vitro and in vivo experiments indicate that membrane-bound serine proteases are of critical importance in the activation of ENaC in different organs, such as the kidney, the lung, or the cochlea. Progress in understanding the basic mechanism of proteolytic activation of ENaC is accelerating, but uncertainty about the most fundamental aspects persists, leaving numerous still-unanswered questions.
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                Author and article information

                Journal
                Title: Clinical Journal of the American Society of Nephrology
                Abbreviated Title: Clinical Journal of the American Society of Nephrology
                Publisher: American Society of Nephrology (ASN)
                ISSN (Print): 1555-9041
                ISSN (Electronic): 1555-905X
                Publication date Created: May 09 2016
                Publication date (Print): March 01 2016
                Volume: 11
                Issue: 5
                Pages: 761-769
                Article
                DOI: 10.2215/CJN.12261115
                PMC ID: 4858495
                PubMed ID: 26933188
                SO-VID: facc88fd-b610-4acc-8a4a-f401302bedbc
                Copyright © © 2016
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