Biomarker genes for detecting estrogenic activity of endocrine disruptors via estrogen receptors

Int J Environ Res Public Health. 2012 Mar;9(3):698-711. doi: 10.3390/ijerph9030698. Epub 2012 Feb 24.


Endocrine disruptors (EDs) are compounds used in various industrial products, drugs, and cosmetics. They can be found in the environment and disturb the endocrine and reproductive systems, resulting in adverse effects to humans and wildlife such as birth defects and developmental disorders. Since several EDs have a structure similar to that of endogenous steroid hormones such as estrogens, they intend to have an affinity for steroid hormone receptors and alter hormone-mediated metabolism by binding to these receptors. EDs are therefore a global concern and assays should be developed to efficiently determine whether these compounds are detrimental to biological systems. Diverse experimental methods may help determine the endocrine disrupting potential of EDs and evaluate the adverse effects of a single and/or combination of these reagents. Currently, biomarkers have been employed to objectively measure EDs potency and understand the underlying mechanisms. Further studies are required to develop ideal screening methods and biomarkers to determine EDs potency at environmentally relevant concentrations. In this review, we describe the biomarkers for estrogenicity of EDs identified both in vitro and in vivo, and introduce a biomarker, cabindin-D(9k) (CaBP-9k), that may be used to assess estrogenic activity of EDs.

Keywords: biomarker; calbindin-D9k; endocrine disruptors; estrogen activity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biomarkers / metabolism
  • Calbindins
  • Endocrine Disruptors / toxicity*
  • Estrogens, Non-Steroidal / toxicity*
  • Gene Expression
  • Humans
  • Receptors, Estrogen / metabolism*
  • S100 Calcium Binding Protein G / genetics


  • Biomarkers
  • Calbindins
  • Endocrine Disruptors
  • Estrogens, Non-Steroidal
  • Receptors, Estrogen
  • S100 Calcium Binding Protein G