title: Comparative proteomic tissue analysis in patients with ossification of the posterior longitudinal ligament.
abstract: OBJECTIVE
  The ossification of the posterior longitudinal ligament (OPLL) involves the ligament that lines the posterior surface of the spinal vertebral bodies. Hormonal and metabolic factors as well as hereditary factors have been proposed to be involved in pathologic ligamentous OPLL. However, there are currently no definitive serological biomarkers for OPLL that might be used to achieve a more convenient and economic diagnosis. To find an easier and simpler diagnostic method and to identify pathogenic proteins associated with OPLL, we assessed PLL tissues from patients with OPLL for proteomic alterations.
  
  
  METHODS
  OPLL tissues were collected from 12 patients with OPLL, and non-OPLL tissues were collected from 12 healthy subjects without OPLL. To minimize individual variations, we matched the sex and age of the patients in the healthy and OPLL groups. The two-dimensional electrophoresis patterns of tissue from 12 OPLL patients and 12 healthy subjects were compared.
  
  
  RESULTS
  We found 25 proteins that were significantly and consistently different on the two-dimensional electrophoresis gels between the group of ossified PLL tissues from the patients with OPLL and the group of nonossified PLL tissues from the healthy subjects. Among them, 21 proteins were up-regulated in the patients with OPLL, whereas the remaining four proteins were down-regulated.
  
  
  CONCLUSIONS
  The information obtained via this proteomic analysis will be very useful in understanding the pathophysiology of OPLL as well as in finding protein candidates to serve as new diagnostic biomarkers of OPLL.
authors.affiliation: Department of Neurosurgery, Research Institute of Clinical Medicine, Chonbuk National University Medical School and Hospital, Jeonju, Korea.
authors.forename: Young-Min
authors.initials: YM
authors.lastname: Oh
authors.affiliation: Department of Neurosurgery, Research Institute of Clinical Medicine, Chonbuk National University Medical School and Hospital, Jeonju, Korea.
authors.forename: Woo-Jong
authors.initials: WJ
authors.lastname: Lee
authors.affiliation: Department of Pharmacology, Research Institute of Clinical Medicine, Chonbuk National University Medical School and Hospital, Jeonju, Korea.
authors.forename: Min-Gul
authors.initials: MG
authors.lastname: Kim
authors.affiliation: Department of Hematology, Yambian University Hospital, Yanji Jilin, People's Republic of China.
authors.forename: Tian-Ze
authors.initials: TZ
authors.lastname: Ma
authors.affiliation: Department of Pharmacology, Research Institute of Clinical Medicine, Chonbuk National University Medical School and Hospital, Jeonju, Korea. Electronic address: ygkwak@jbnu.ac.kr.
authors.forename: Yong-Geun
authors.initials: YG
authors.lastname: Kwak
authors.affiliation: Department of Neurosurgery, Research Institute of Clinical Medicine, Chonbuk National University Medical School and Hospital, Jeonju, Korea. Electronic address: spineeun@jbnu.ac.kr.
authors.forename: Jong-Pil
authors.initials: JP
authors.lastname: Eun
mesh_terms: D000328:Adult; D015415:Biomarkers / Q000032:analysis; D015536:Down-Regulation; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D006801:Humans; D006868:Hydrolysis; D007091:Image Processing, Computer-Assisted; D008279:Magnetic Resonance Imaging; D008297:Male; D008875:Middle Aged; D017887:Ossification of Posterior Longitudinal Ligament / Q000235:genetics*; D040901:Proteomics / Q000379:methods*; D016622:Silver Staining; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014057:Tomography, X-Ray Computed; D014357:Trypsin / Q000737:chemistry; D015854:Up-Regulation
chemical_list: D015415:Biomarkers; D014357:Trypsin
keywords: Biomarker; Enthesopathy; Mass spectrometry; Ossification of posterior longitudinal ligament; Proteomics