title: Apoptosis in human compressive myelopathy due to metastatic neoplasia.
abstract: METHODS
  Immunohistochemical assessment of apoptotic markers in human cases of compressive myelopathy due to neoplastic compression.
  
  
  OBJECTIVE
  To characterize the role of apoptosis in neoplastic compressive myelopathy in human postmortem tissue with extramedullary tumor involvement.
  
  
  BACKGROUND
  Neoplasms, whether primary or metastatic, may lead to compression of the spinal cord and development of a compressive myelopathy syndrome. Apoptotic processes of cell death are thought to contribute to cell death in chronic compressive myelopathy because of degenerative spondylosis, but this has not previously been described in neoplastic compression.
  
  
  METHODS
  Six postmortem cases of human neoplastic compressive myelopathy were assessed for apoptosis using a panel of immunohistochemical markers including Fas, B-cell lymphoma 2 (Bcl-2), caspase-3 and 9, DNA-dependent protein kinase catalytic subunit (DNA-PKcs), poly (ADP-ribose) polymerase (PARP), apoptosis-inducing factor (AIF), and terminal deoxynucleotide transferase dUTP Nick End Labeling (TUNEL).
  
  
  RESULTS
  Apoptosis was maximal at the site of tumor compression. Glial cells, predominantly oligodendrocytes, were immunopositive for DNA-PKcs, PARP, AIF, and TUNEL. Axons were immunopositive for caspase 3, DNA-PKcs, and AIF. Neurons were immunopositive for DNA-PKcs, PARP, AIF, and TUNEL.
  
  
  CONCLUSIONS
  The current study demonstrates that apoptosis plays a role in human neoplastic compressive myelopathy. Necrosis dominates the severe end of the spectrum of compression. The prominent oligodendroglial involvement is suggestive that apoptosis may be important in the ongoing remodeling of white matter due to sustained compression.
  
  
  METHODS
  4.
authors: *School of Medical Sciences, University of Adelaide, Adelaide, Australia †SA Pathology, Hanson Institute Centre for Neurological Diseases and Schools of Medical and Veterinary Science, University of Adelaide, Adelaide, Australia ‡Division of Health Sciences, University of South Australia, Adelaide, Australia.
authors: Rowena E A
authors: RE
authors: Newcombe
authors: John W
authors: JW
authors: Finnie
authors: Anna V
authors: AV
authors: Leonard
authors: Jim
authors: J
authors: Manavis
authors: Peter L
authors: PL
authors: Reilly
authors: Robert
authors: R
authors: Vink
authors: Peter C
authors: PC
authors: Blumbergs
mesh_terms: D000368:Aged; D017209:Apoptosis; D051033:Apoptosis Inducing Factor / Q000032:analysis; D001369:Axons / Q000737:chemistry*; D053148:Caspase 3 / Q000032:analysis; D053453:Caspase 9 / Q000032:analysis; D051747:DNA-Activated Protein Kinase / Q000032:analysis; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D020287:In Situ Nick-End Labeling; D008297:Male; D008875:Middle Aged; D009362:Neoplasm Metastasis; D009369:Neoplasms / Q000150:complications*; D009687:Nuclear Proteins / Q000032:analysis; D009836:Oligodendroglia / Q000737:chemistry*; D011065:Poly(ADP-ribose) Polymerases / Q000032:analysis; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000032:analysis; D013117:Spinal Cord Compression / Q000209:etiology* / Q000473:pathology; D055815:Young Adult; D019014:fas Receptor / Q000032:analysis
chemical_list: D051033:Apoptosis Inducing Factor; C491901:FAS protein, human; D009687:Nuclear Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D019014:fas Receptor; D011065:Poly(ADP-ribose) Polymerases; D051747:DNA-Activated Protein Kinase; C497263:PRKDC protein, human; D053148:Caspase 3; D053453:Caspase 9