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Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
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Related Experiment Video

Updated: Jun 4, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
07:31

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Quantification of Angiotensin peptides.

Q C Meng1, K H Berecek

  • 1Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, AL.

Methods in Molecular Medicine
|February 19, 2011
PubMed
Summary

Accurate measurement of kidney angiotensin peptides is crucial for understanding kidney function. We developed a simplified extraction method to overcome previous measurement challenges.

Area of Science:

  • Nephrology
  • Endocrinology
  • Biochemistry

Background:

  • The kidney possesses an endogenous renin-angiotensin system (RAS).
  • Intrarenal angiotensin II (Ang II) is vital for regulating renal hemodynamics and sodium excretion.
  • Accurate measurement of renal Ang peptides is essential for assessing the intrarenal RAS but faces significant methodologic challenges.

Purpose of the Study:

  • To address the difficulties in accurately measuring intrarenal Ang peptides.
  • To develop a simplified and reliable method for extracting Ang peptides from renal tissue.

Main Methods:

  • Review and identification of methodologic limitations in current Ang peptide measurement techniques.
  • Adaptation and validation of a recently developed simplified extraction method for brain tissue to renal tissue.

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Last Updated: Jun 4, 2026

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Published on: June 16, 2019

Peptide and Protein Quantification Using Automated Immuno-MALDI (iMALDI)
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Peptide and Protein Quantification Using Automated Immuno-MALDI (iMALDI)

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  • Focus on overcoming issues like peptide instability, incomplete extraction, and interference from metabolites.
  • Main Results:

    • Previous methods using radioimmunoassay (RIA) on crude extracts yielded inaccurate results due to interference and cross-reactivity.
    • Challenges included peptide degradation by tissue peptidases, incomplete extraction, and variable recovery during solid-phase extraction (e.g., C(18) cartridges).
    • Difficulties were also noted with high-performance liquid chromatography (HPLC) gradient elution techniques.

    Conclusions:

    • Existing methods for measuring intrarenal Ang peptides are problematic and lead to variable results.
    • A simplified extraction method is needed to accurately quantify Ang peptides in renal tissue.
    • Improved measurement techniques will facilitate a better understanding of the intrarenal RAS's role in kidney function.