Intragraft activation of genes encoding cytotoxic T lymphocyte effector molecules precedes the histological evidence of rejection in human cardiac transplantation

Transplantation. 2001 Nov 27;72(10):1705-8. doi: 10.1097/00007890-200111270-00025.

Abstract

Background: The purpose of the present study was to investigate transcripts of perforin, granzyme B, and Fas ligand (FasL) in heart transplants undergoing rejection.

Methods: Quantitative reverse transcriptase-polymerase chain reaction was applied for mRNA detection in 29 endomyocardial biopsy specimens from 11 cardiac allograft recipients.

Results: The mRNA levels of granzyme B, perforin, and FasL were higher (P<0.05) in biopsy specimens with rejection than in biopsy specimens without rejection (granzyme B, 0.53 vs. 0.09; perforin, 0.34 vs. 0; FasL, 0.57 vs. 0.36). In prerejection biopsy specimens, granzyme B and FasL levels were significantly higher than in biopsy specimens without rejection. Any two of the three transcripts were increased in 100% of prerejection, in 92% of rejection, and in 36% of no rejection biopsy specimens (P<0.04).

Conclusions: The assessment of intragraft levels of cytotoxic T lymphocyte effector molecule mRNA represents a valuable tool in the monitoring of cardiac allograft rejection, especially considering the predictive value for warning of impending acute rejection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fas Ligand Protein
  • Gene Expression Regulation*
  • Graft Rejection*
  • Granzymes
  • Heart Transplantation / immunology*
  • Humans
  • Membrane Glycoproteins / genetics*
  • Perforin
  • Pore Forming Cytotoxic Proteins
  • RNA, Messenger / analysis
  • Reverse Transcriptase Polymerase Chain Reaction
  • Serine Endopeptidases / genetics*
  • T-Lymphocytes, Cytotoxic / physiology*

Substances

  • FASLG protein, human
  • Fas Ligand Protein
  • Membrane Glycoproteins
  • Pore Forming Cytotoxic Proteins
  • RNA, Messenger
  • Perforin
  • GZMB protein, human
  • Granzymes
  • Serine Endopeptidases