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Chemical science2018; 10(6); 1607-1618; doi: 10.1039/c8sc04397c

Testosterone meets albumin – the molecular mechanism of sex hormone transport by serum albumins.

Abstract: Serum albumin is the most abundant protein in mammalian blood plasma and is responsible for the transport of metals, drugs, and various metabolites, including hormones. We report the first albumin structure in complex with testosterone, the primary male sex hormone. Testosterone is bound in two sites, neither of which overlaps with the previously suggested Sudlow site I. We determined the binding constant of testosterone to equine and human albumins by two different methods: tryptophan fluorescence quenching and ultrafast affinity extraction. The binding studies and similarities between residues comprising the binding sites on serum albumins suggest that testosterone binds to the same sites on both proteins. Our comparative analysis of albumin complexes with hormones, drugs, and other biologically relevant compounds strongly suggests interference between a number of compounds present in blood and testosterone transport by serum albumin. We discuss a possible link between our findings and some phenomena observed in human patients, such as low testosterone levels in diabetic patients.
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Publication Date: 2018-12-17 PubMed ID: 30842823PubMed Central: PMC6371759DOI: 10.1039/c8sc04397cGoogle Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research article studies how testosterone, the primary male hormone, binds with serum albumin, which is the most common protein found in blood plasma. Scientists had discovered that testosterone binds in two distinct locations on the protein and this could affect the way that testosterone is transported in the body, potentially explaining some health issues like low testosterone levels in diabetic patients.

Process for Studying Testosterone’s Binding with Serum Albumin

  • The researchers in this study have presented the first albumin structure with testosterone. It’s a huge leap because it allows other scientists to understand how exactly the hormone fits in with the protein.
  • The testosterone/serum albumin complex was studied using two methods: tryptophan fluorescence quenching and ultrafast affinity extraction. These are techniques used to measure how tightly a molecule binds to a protein, in this case, how well testosterone binds to serum albumin.

The Binding of Testosterone to Serum Albumin

  • The researchers discovered that testosterone binds to albumin at two separate sites. This is important, as it shows that testosterone can interact with serum albumin in more than one way and potentially at the same time.
  • The locations of these two binding sites do not overlap with the previously suggested Sudlow site I. This indicates that these are entirely new sites from what scientists had initially thought.

The Implication on Testosterone Transport

  • The structural analysis of albumin complexes with other hormones and biologically relevant compounds strongly indicates possible interference with testosterone transport by serum albumin. This suggests that the presence of other compounds in the blood might affect how testosterone is carried around the body.
  • Such interference could be key to explaining particular phenomena observed in patients, such as low testosterone levels seen in diabetic patients. This finding could provide valuable insights into the biological processes behind certain diseases and conditions.

Conclusion

  • This research provides a crucial step towards understanding the molecular mechanism of sex hormone transport. New therapeutic strategies could be designed to compensate for the interference between medications or metabolites with testosterone transport, especially for conditions like diabetes where testosterone levels are typically impacted.

Cite This Article

APA
Czub MP, Venkataramany BS, Majorek KA, Handing KB, Porebski PJ, Beeram SR, Suh K, Woolfork AG, Hage DS, Shabalin IG, Minor W. (2018). Testosterone meets albumin – the molecular mechanism of sex hormone transport by serum albumins. Chem Sci, 10(6), 1607-1618. https://doi.org/10.1039/c8sc04397c

Publication

Chemical science
ISSN: 2041-6520
NlmUniqueID: 101545951
Country: England
Language: English
Volume: 10
Issue: 6
Pages: 1607-1618

Researcher Affiliations

Czub, Mateusz P
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
  • Center for Structural Genomics of Infectious Diseases (CSGID) , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA.
Venkataramany, Barat S
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
Majorek, Karolina A
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
Handing, Katarzyna B
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
Porebski, Przemyslaw J
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
  • Center for Structural Genomics of Infectious Diseases (CSGID) , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA.
Beeram, Sandya R
  • Department of Chemistry , University of Nebraska-Lincoln , Lincoln , Nebraska 68588 , USA . Email: dhage1@unl.edu.
Suh, Kyungah
  • Department of Chemistry , University of Nebraska-Lincoln , Lincoln , Nebraska 68588 , USA . Email: dhage1@unl.edu.
Woolfork, Ashley G
  • Department of Chemistry , University of Nebraska-Lincoln , Lincoln , Nebraska 68588 , USA . Email: dhage1@unl.edu.
Hage, David S
  • Department of Chemistry , University of Nebraska-Lincoln , Lincoln , Nebraska 68588 , USA . Email: dhage1@unl.edu.
Shabalin, Ivan G
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
  • Center for Structural Genomics of Infectious Diseases (CSGID) , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA.
Minor, Wladek
  • Department of Molecular Physiology and Biological Physics , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA . Email: wladek@iwonka.med.virginia.edu ; Email: ivan_s@iwonka.med.virginia.edu.
  • Center for Structural Genomics of Infectious Diseases (CSGID) , University of Virginia , 1340 Jefferson Park Avenue , Charlottesville , VA 22908 , USA.

Grant Funding

  • R01 GM117080 / NIGMS NIH HHS
  • R01 GM117325 / NIGMS NIH HHS
  • R01 GM132595 / NIGMS NIH HHS

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