Adding myofibroblasts to the lacrimal pump

Acta Histochem. 2020 May;122(4):151536. doi: 10.1016/j.acthis.2020.151536. Epub 2020 Mar 8.

Abstract

The lacrimal sac (LS) empties in the nasolacrimal duct to drain the tears in the inferior nasal meatus. Different studies indicated the role of the lacrimal pump in the lacrimal drainage. Although controversial, the lacrimal pump mechanism is an extrinsic one, either active, or passive. An intrinsic contractile potential of the LS was not documented previously. We thus aimed a retrospective immunohistochemical study to test the alpha-smooth muscle actin (α-SMA) and h-caldesmon expression in the LS wall. We used archived paraffin-embedded samples of LS from ten adult patients. The α-SMA + phenotype was detected in basal epithelial cells, in subepithelial ribbons of stromal cells, in vascular smooth muscle cells, as well as in pericytes. H-caldesmon was exclusively expressed in pericytes, vascular smooth muscle cells and myoepithelial cells of the subepithelial glands. The most striking feature we found in all samples was a consistent stromal network of α-SMA+/h-caldesmon- myofibroblasts. This finding supports an intrinsic scaffold useful for the lacrimal pump.

Keywords: Alpha-smooth muscle actin; Caldesmon; Immunohistochemistry; Lacrimal drainage system; Lacrimal pump; MALT; Myofibroblasts.

MeSH terms

  • Actins / biosynthesis
  • Calmodulin-Binding Proteins / biosynthesis
  • Epithelial Cells / metabolism
  • Female
  • Humans
  • Lacrimal Apparatus / anatomy & histology
  • Lacrimal Apparatus / cytology
  • Lacrimal Apparatus / physiology*
  • Male
  • Middle Aged
  • Muscle Contraction / physiology
  • Myocytes, Smooth Muscle / metabolism
  • Myofibroblasts / physiology*
  • Myofibroblasts / ultrastructure
  • Pericytes / metabolism
  • Retrospective Studies

Substances

  • ACTA2 protein, human
  • Actins
  • Calmodulin-Binding Proteins