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Am J Physiol Renal Physiol 276: F535-F543, 1999;
0363-6127/99 $5.00
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Vol. 276, Issue 4, F535-F543, April 1999

Modulation of renal tubular cell function by RGS3

W. Grüning1, T. Arnould1, F. Jochimsen1, L. Sellin1, S. Ananth1, E. Kim2, and G. Walz1

1 Renal Division, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston 02215; and 2 Laboratory of Molecular and Developmental Neuroscience, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts 02114

The recently discovered family of regulators of G protein signaling (RGS) accelerates the intrinsic GTPase activity of certain Galpha subunits, thereby terminating G protein signaling. Particularly high mRNA levels of one family member, RGS3, are found in the adult kidney. To establish the temporal and spatial renal expression pattern of RGS3, a polyclonal antiserum was raised against the COOH terminus of RGS3. Staining of mouse renal tissue at different gestational stages revealed high levels of RGS3 within the developing and mature tubular epithelial cells. We tested whether RGS3 can modulate tubular migration, an important aspect of tubular development, in response to G protein-mediated signaling. Several mouse intermedullary collecting duct (mIMCD-3) cell lines were generated that expressed RGS3 under the control of an inducible promoter. Lysophosphatidic acid (LPA) is a potent chemoattractant that mediates its effects through heterotrimeric G proteins. We found that induction of RGS3 significantly reduced LPA-mediated cell migration in RGS3-expressing mIMCD-3 clones, whereas chemotaxis induced by hepatocyte growth factor remained unaffected by RGS3. Our findings suggest that RGS3 modulates tubular functions during renal development and in the adult kidney.

renal tubular epithelial cells; kidney development; chemotaxis; G protein; regulators of G protein signaling


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