Lubricin and smooth muscle α-actin-containing myofibroblasts in the pseudomembranes around loose hip and knee prostheses

Acta Biomater. 2013 Mar;9(3):5751-8. doi: 10.1016/j.actbio.2012.11.010. Epub 2012 Nov 19.

Abstract

The objective was to evaluate the presence and distribution of the lubricating and anti-adhesion glycoprotein lubricin and cells containing the contractile isoform smooth muscle α-actin (SMA) in pseudomembranes around loose hip prostheses. Periprosthetic tissue was obtained at revision arthroplasty of eight aseptic, loose hip implants, and for comparison three loose knee prostheses. Immunohistochemical analysis was performed in 3 zones: zone 1, within 300μm of the edge of the implant-tissue interface; zone 2, between zones 1 and 3; zone 3, within 300μm of the resected/trimmed edge. The presence of lubricin was extensive in all samples: (1) as a discrete layer at the implant-tissue interface; (2) within the extracellular matrix (ECM); (3) intracellularly. There was significantly more high grade (>50%) lubricin surface staining at the implant-tissue interface compared with the resected edge. While there was also a significant effect of location of high grade ECM lubricin staining, there was no significant effect of implant type (i.e. hip versus knee). All but two hip pseudomembrane samples showed the presence of many SMA-containing cells. There was a significant effect of location on the number of SMA-expressing cells, but not of implant type. These findings might explain why the management of loose prosthesis is so challenging.

Publication types

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

MeSH terms

  • Actins / metabolism*
  • Adult
  • Aged
  • Aged, 80 and over
  • Extracellular Matrix / metabolism
  • Glycoproteins / metabolism*
  • Hip Prosthesis*
  • Humans
  • Immunohistochemistry
  • Implants, Experimental
  • Knee Prosthesis*
  • Membranes / metabolism
  • Membranes / pathology
  • Middle Aged
  • Myofibroblasts / metabolism*
  • Myofibroblasts / pathology*
  • Staining and Labeling

Substances

  • ACTA2 protein, human
  • Actins
  • Glycoproteins
  • lubricin