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ADMA metabolism and clearance.

Tom Teerlink1

  • 1Metabolic Laboratory, Department of Clinical Chemistry, VU University Medical Center, Amsterdam, The Netherlands. t.teerlink@vumc.nl

Vascular Medicine (London, England)
|February 1, 2006
PubMed
Summary

Asymmetric dimethylarginine (ADMA) levels are regulated by protein methylation, proteolysis, and degradation by dimethylarginine dimethylaminohydrolase (DDAH). ADMA is transported between organs and cleared by the liver and kidneys.

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Area of Science:

  • Biochemistry
  • Physiology
  • Molecular Biology

Background:

  • Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide synthase.
  • Protein methylation is a key post-translational modification regulating protein function.
  • ADMA is generated from the proteolysis of methylated proteins.

Purpose of the Study:

  • To review the metabolic processes regulating plasma ADMA concentration.
  • To highlight the roles of protein methylation, proteolysis, and DDAH in ADMA metabolism.
  • To discuss the interorgan transport and clearance mechanisms of ADMA.

Main Methods:

  • Review of existing literature on ADMA metabolism.
  • Analysis of cellular and organ-level processes involved in ADMA regulation.
  • Discussion of the enzymatic activity of dimethylarginine dimethylaminohydrolase (DDAH).

Main Results:

  • ADMA is formed from methylated proteins and degraded by DDAH.
  • Cationic amino acid transporters facilitate ADMA's interorgan transport.
  • The liver and kidneys play significant roles in ADMA clearance.

Conclusions:

  • ADMA metabolism involves a complex interplay of synthesis, degradation, and transport.
  • Understanding ADMA regulation is crucial for nitric oxide synthase inhibition.
  • Hepatic and renal clearance are primary routes for ADMA elimination.

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