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Drug Binding to Blood Components

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When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
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Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
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Related Experiment Video

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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
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Structure-function of DHEA binding proteins.

Barbara J Clark1, Carolyn M Klinge1

  • 1Department of Biochemistry & Molecular Genetics, Center for Integrative Environmental Health Sciences (CIEHS), University of Louisville School of Medicine, Louisville, KY, United States.

Vitamins and Hormones
|September 17, 2023
PubMed
Summary

Dehydroepiandrosterone (DHEA) and its metabolite DHEA-S are abundant steroids influencing multiple body systems. This review details their diverse molecular mechanisms, including receptor binding and channel interactions.

Keywords:
DHEADHEA-SIon channelsNeurosteroidNuclear receptorsReceptorsReviewSignal transduction

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Area of Science:

  • Endocrinology
  • Neurobiology
  • Molecular Biology

Background:

  • Dehydroepiandrosterone (DHEA) and its sulfated form (DHEA-S) are the most prevalent circulating steroids.
  • These steroids serve as crucial precursors for potent sex hormones like estradiol and testosterone.
  • DHEA exhibits a wide array of physiological effects across the central nervous system, cardiovascular system, and metabolic tissues.

Purpose of the Study:

  • To provide an updated review of the physiological, biochemical, and molecular mechanisms underlying DHEA and DHEA-S activity.
  • To elucidate the diverse pathways through which DHEA and DHEA-S exert their biological effects.
  • To consolidate current knowledge on DHEA and DHEA-S interactions with various cellular receptors and ion channels.

Main Methods:

  • Review of existing literature and previous research findings on DHEA and DHEA-S.
  • Analysis of DHEA and DHEA-S interactions with plasma membrane receptors (e.g., GPCRs, GABA(A), NMDA, S1R).
  • Examination of DHEA and DHEA-S binding to nuclear receptors (AR, ERα, ERβ, GPER1) and activation of other pathways (CAR, PPARα, ion channels, TRPM3).

Main Results:

  • DHEA and DHEA-S engage multiple receptor types, including specific PM receptors and neuroreceptors.
  • They exhibit lower affinity for nuclear androgen and estrogen receptors compared to cognate hormones, highlighting the role of conversion to active hormones.
  • DHEA and DHEA-S modulate ion channel activity and activate nuclear receptors like CAR and PPARα through indirect mechanisms.

Conclusions:

  • DHEA and DHEA-S possess multifaceted biological activities mediated by diverse molecular targets.
  • Understanding these mechanisms is essential, considering both direct receptor interactions and conversion to active sex steroids.
  • This review synthesizes the latest findings on the complex physiological roles of DHEA and DHEA-S.