Regulation of epididymal principal cell functions by basal cells: role of transient receptor potential (Trp) proteins and cyclooxygenase-1 (COX-1)

Mol Cell Endocrinol. 2004 Mar 15;216(1-2):5-13. doi: 10.1016/j.mce.2003.10.077.


The epithelia lining the epididymides of many species including the human are known to consist of several cell types. Among them, the principal cells are the most abundant and their functions most extensively studied. There are other cell types such as the narrow cells, clear cells, halo cells and basal cells which are scattered along the duct in lesser number. Although these minority cell types have not been studied to the same extent as the principal cells, it is conceivable that their presence are essential to the integrated functions of the epididymis. In the intact epididymis, basal cells can be seen adhering to the basement membrane forming close contact with the principal cells above them. Work in our laboratory has provided evidence that through local formation of prostaglandins, basal cells may regulate electrolyte and water transport by the principal cells. This regulatory process involves two proteins which are exclusively expressed by the basal cells. They are the transient receptor potential (Trp) proteins, which serve as transmembrane pathways for Ca(2+) influx, and cyclooxygenase 1 (COX-1), a key enzyme in the formation of prostaglandins. The role of the two proteins in the integrated functions of the basal cells as humoral regulators of principal cells is discussed.

Publication types

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

MeSH terms

  • Animals
  • Calcium Channels / genetics
  • Calcium Channels / metabolism*
  • Cyclooxygenase 1
  • Cyclooxygenase Inhibitors / pharmacology
  • Epididymis / cytology*
  • Epididymis / metabolism*
  • Epithelial Cells / cytology
  • Epithelial Cells / physiology*
  • Humans
  • Isoenzymes / metabolism*
  • Male
  • Membrane Potentials / drug effects
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Prostaglandin-Endoperoxide Synthases / metabolism*


  • Calcium Channels
  • Cyclooxygenase Inhibitors
  • Isoenzymes
  • Membrane Proteins
  • Cyclooxygenase 1
  • PTGS1 protein, human
  • Prostaglandin-Endoperoxide Synthases