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CORRIGENDUM

Volume 62, July 2007

Pages F398–F407. Velez JC, Bland AM, Arthur JM, Raymond JR, Janech MG. Characterization of renin-angiotensin system enzyme activities in cultured mouse podocytes. Am J Physiol Renal Physiol 293: F398–F407 (doi:10.1152/ajprenal.00050.2007).

We previously published that the metabolism of exogenous ANG-I peptide by cultured mouse podocytes (2) leads to the predominant formation of ANG-1-7 and ANG-1-9. ANG-derived peptides were assigned identifications based on MALDI-TOF-TOF spectral interpretation. In our paper, we designated ANG-1-9 to masses of 1,181 Da and 1,183 Da in Figs. 2, 3A, 4A, and 7. Upon further analysis by MALDI-TOF-TOF and LC/MS/MS, we have determined that the peptide residing at mass 1181 corresponds to ANG-2-10 (des-Asp¹-ANG-I) instead of ANG-1-9, as indicated in the paper. As such, the predominant ANG peptides generated by mouse podocytes treated with exogenous ANG-I were ANG-1-7 and ANG-2-10, not ANG-1-9 as we concluded. Quantifications of ANG-1-9 formation should be disregarded. Of note, a previous publication using proximal tubule preparations also assigned a peptide of mass 1,181 Da as ANG-1-9 (1). We do not dispute the fact that 1181 could be ANG-1-9 in that particular study; however, reanalysis of our podocyte samples strongly supports the identification of the peptide at 1,181 Da to be ANG-2-10. Therefore, "ANG-1-9" should be read as "ANG-2-10" throughout the manuscript, except on Fig. 7A, where the 1183 peak was correctly labeled as ANG-1-9.

REFERENCES

1. Li N, Zimpelmann J, Cheng K, Wilkins JA, Burns KD. The role of angiotensin converting enzyme 2 in the generation of angiotensin 1-7 by rat proximal tubules. Am J Physiol Renal Physiol 288: F353–F362, 2005.[Abstract/Free Full Text]
2. Velez JC, Bland AM, Arthur JM, Raymond JR, Janech MG. Characterization of renin-angiotensin system enzyme activities in cultured mouse podocytes. Am J Physiol Renal Physiol 293: F390–F407, 2007.

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