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Am J Physiol Cell Physiol 281: C1385-C1395, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 4, C1385-C1395, October 2001

K-Cl cotransport modulation by intracellular Mg in erythrocytes from mice bred for low and high Mg levels

Lucia De Franceschi1, Emma Villa-Moruzzi2, Laura Fumagalli3, Carlo Brugnara4, Franco Turrini5, Roland Motta6, Emanuela Veghini3, Cristina Corato3, Seth L. Alper7, and Giorgio Berton3

Departments of 1 Clinical and Experimental Medicine and 3 Pathology, Section of General Pathology, University of Verona, Verona, Italy; 2 Department of Experimental Pathology, University of Pisa, Pisa, Italy; 4 Departments of Laboratory Medicine and Pathology, Children's Hospital, Harvard Medical School, Boston 02115, and 7 Molecular Medicine and Renal Units, Beth Israel Deaconess Medical Center, and Departments of Medicine and Cell Biology, Harvard Medical School, Boston, Massachusetts 02215; 5 Department of Biochemistry, University of Torino, Torino, Italy; and 6 Laboratoire de Recherche Genetique sur les Modeles Animaux, Centre National de la Recherche Scientifique, Orleans, France

Mg is an important determinant of erythrocyte cation transport system(s) activity. We investigated cation transport in erythrocytes from mice bred for high (MGH) and low (MGL) Mg levels in erythrocytes and plasma. We found that K-Cl cotransport activity was higher in MGL than in MGH erythrocytes, and this could explain their higher mean corpuscular hemoglobin concentration, median density, and reduced cell K content. Although mouse KCC1 protein abundance was comparable in MGL and MGH erythrocytes, activities of Src family tyrosine kinases were higher in MGH than in MGL erythrocytes. In contrast, protein phosphatase (PP) isoform 1alpha (PP1alpha ) enzymatic activity, which has been suggested to play a positive regulatory role in K-Cl cotransport, was lower in MGH than in MGL erythrocytes. Additionally, we found that the Src family kinase c-Fgr tyrosine phosphorylates PP1alpha in vitro. These findings suggest that in vivo downregulation of K-Cl cotransport activity by Mg is mediated by enhanced Src family kinase activity, leading to inhibition of the K-Cl cotransport stimulator PP1.

membrane transport; tyrosine phosphorylation; Src family tyrosine kinases; protein phosphatase isoform 1alpha


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