title: Identification by a differential proteomic approach of heat shock protein 27 as a potential marker of atherosclerosis.
abstract: BACKGROUND
  We hypothesized that normal and pathological vessel walls display a differential pattern of secreted proteins. We have recently set up the conditions for comparing secretomes from carotid atherosclerotic plaques and control arteries using a proteomic approach to assess whether differentially secreted proteins could represent markers for atherosclerosis.
  
  
  RESULTS
  Normal endartery segments and different regions of endarterectomy pieces (noncomplicated/complicated plaques) were incubated in protein-free medium, and the released proteins were analyzed by 2D electrophoresis (2-DE). Among the differently secreted proteins, we have identified heat shock protein-27 (HSP27). Surprisingly, compared with control arteries, HSP27 release was drastically decreased in atherosclerotic plaques and barely detectable in complicated plaque supernatants. HSP27 was expressed primarily by intact vascular cells of normal arteries and carotid plaques (immunohistochemistry). Plasma detection of soluble HSP27 showed that circulating HSP27 levels are significantly decreased in the blood of patients with carotid stenosis relative to healthy subjects (0.19 [0.1 to 1.95] versus 83 [71.8 to 87.8]) ng/mL, P<0.0001).
  
  
  CONCLUSIONS
  HSP27 secretion is decreased in complicated atherosclerotic plaques, and sHSP27 plasma levels are decreased in atherosclerotic patients compared with healthy subjects. Plasma sHSP27 levels could be a potential index of atherosclerosis, although further validation is needed in large patient cohorts.
authors.affiliation: Vascular Research Laboratory, Autónoma University, Madrid, Spain.
authors.forename: Jose Luis
authors.initials: JL
authors.lastname: Martin-Ventura
authors.forename: Mari Carmen
authors.initials: MC
authors.lastname: Duran
authors.forename: Luis Miguel
authors.initials: LM
authors.lastname: Blanco-Colio
authors.forename: Olivier
authors.initials: O
authors.lastname: Meilhac
authors.forename: Anne
authors.initials: A
authors.lastname: Leclercq
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Michel
authors.forename: Ole N
authors.initials: ON
authors.lastname: Jensen
authors.forename: Sergio
authors.initials: S
authors.lastname: Hernandez-Merida
authors.forename: José
authors.initials: J
authors.lastname: Tuñón
authors.forename: Fernando
authors.initials: F
authors.lastname: Vivanco
authors.forename: Jesús
authors.initials: J
authors.lastname: Egido
mesh_terms: D000368:Aged; D002339:Carotid Arteries / Q000378:metabolism / Q000473:pathology; D002340:Carotid Artery Diseases / Q000097:blood / Q000503:physiopathology* / Q000601:surgery; D002846:Chromatography, Affinity; D017077:Culture Media, Conditioned / Q000737:chemistry; D016894:Endarterectomy, Carotid; D005260:Female; D005263:Femoral Artery / Q000378:metabolism / Q000473:pathology; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000097:blood / Q000172:deficiency / Q000378:metabolism*; D006801:Humans; D008297:Male; D008875:Middle Aged; D018832:Molecular Chaperones; D009363:Neoplasm Proteins / Q000097:blood / Q000172:deficiency / Q000378:metabolism*; D009924:Organ Culture Techniques; D010766:Phosphorylation; D020033:Protein Isoforms / Q000032:analysis; D011499:Protein Processing, Post-Translational; D040901:Proteomics; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D017077:Culture Media, Conditioned; D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D020033:Protein Isoforms