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Research Article Free access | 10.1172/JCI116651

A molecular map of G protein alpha chains in microdissected rat nephron segments.

S I Senkfor, G L Johnson, and T Berl

Department of Medicine, University of Colorado School of Medicine, Denver 80262.

Find articles by Senkfor, S. in: PubMed | Google Scholar

Department of Medicine, University of Colorado School of Medicine, Denver 80262.

Find articles by Johnson, G. in: PubMed | Google Scholar

Department of Medicine, University of Colorado School of Medicine, Denver 80262.

Find articles by Berl, T. in: PubMed | Google Scholar

Published August 1, 1993 - More info

Published in Volume 92, Issue 2 on August 1, 1993
J Clin Invest. 1993;92(2):786–790. https://doi.org/10.1172/JCI116651.
© 1993 The American Society for Clinical Investigation
Published August 1, 1993 - Version history
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Abstract

Membrane-associated guanine nucleotide binding proteins regulate many receptor-mediated signals. Heterogeneity of biochemical and functional properties in nephron segments could be due to differences in G protein expression. To ascertain whether such heterogeneity of G proteins is present in various nephron segments, this study examines the distribution and relative abundance of G protein alpha chains in microdissected medullary thick ascending limb, cortical collecting tubules, outer medullary collecting tubules, proximal inner medullary tubules, and distal inner medullary tubules. Reverse transcription and polymerase chain reactions were employed using oligonucleotides encoding highly conserved regions of all known alpha chains. The cDNA was sequenced for alpha chain identification. The alpha i2 versus alpha s distribution was different in the outer medullary collecting tubules, when compared with the medullary thick ascending limb (P < 0.001) or the cortical collecting tubule, the proximal inner medullary tubules, and the distal inner medullary tubules (P < 0.05). These latter four segments did not significantly differ from each other. A similar analysis was applied to the frequently used line of kidney cells, LLC-PK1, whose exact cellular origin remains unclear. Interestingly, we detected both alpha i2 and alpha i3, while only alpha i2 was detected in the rat distal nephron. No alpha o or alpha z reverse transcription PCR products were detected. In contrast alpha 11 and alpha 14 members of the more recently described alpha q family were detected in the outer medullary collecting tubules and the proximal inner medullary tubules, respectively. We conclude that the majority of nephron segments have a relatively constant distribution of G protein alpha chains.

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