title: Increased expression of HDJ-2 (hsp40) in carotid artery atherosclerosis: a novel heat shock protein associated with luminal stenosis and plaque ulceration.
abstract: OBJECTIVE
  Evidence suggests that both humoral and cellular autoimmune processes directed toward heat shock proteins (hsp) contribute to the pathogenesis of atherosclerosis. We characterized a human hsp distinct from those previously characterized in atherosclerotic lesions, termed HDJ-2.
  
  
  METHODS
  To determine the role of HDJ-2 in atherosclerosis, we compared the level of HDJ-2 mRNA expression with the level of hsp60 and hsp70 mRNA expression in 26 carotid endarterectomy specimens and 17 normal arteries. The level of expression of HDJ-2 mRNA was also correlated to the presence of plaque ulceration and the degree of luminal stenosis associated with the lesion.
  
  
  RESULTS
  The expression of HDJ-2 and hsp70 was significantly higher in carotid artery plaques as compared with normal arteries: HDJ-2, 6.7 +/- 1.6 vs 0.1 +/- 0.04, (P =.001); hsp70, 9.5 +/- 0.9 vs 3.7 +/- 0.8, (P =.002). There was no significant difference in hsp60 expression between carotid artery plaques and normal arteries (21.0 +/- 0.9 vs 20.6 +/- 0.8, P =.65). Increased HDJ-2 expression in carotid artery plaques was independent of hsp70 (Pearson correlation, r = 0.11; Bartlett chi(2) analysis, P =.71). Within the ulcerated plaque group, there was a correlation between degree of stenosis and high HDJ-2 mRNA expression (r = 0.896, P =.016). However, there was no correlation between degree of stenosis and high HDJ-2 mRNA expression within the nonulcerated plaque group (r = 0.530, P =.076) or within the entire group of patients (r = 0.0085, P =.97).
  
  
  CONCLUSIONS
  These results demonstrate that expression of HDJ-2 is significantly increased in atherosclerotic carotid artery plaques as compared with hsp60 and hsp70 and correlates with luminal stenosis in ulcerated atherosclerotic carotid artery plaques.
authors.affiliation: Department of Surgery, Washington University School of Medicine, St Louis, MO, USA.
authors.forename: T Q
authors.initials: TQ
authors.lastname: Nguyen
authors.forename: A
authors.initials: A
authors.lastname: Jaramillo
authors.forename: R W
authors.initials: RW
authors.lastname: Thompson
authors.forename: S
authors.initials: S
authors.lastname: Dintzis
authors.forename: W F
authors.initials: WF
authors.lastname: Oppat
authors.forename: B T
authors.initials: BT
authors.lastname: Allen
authors.forename: G A
authors.initials: GA
authors.lastname: Sicard
authors.forename: T
authors.initials: T
authors.lastname: Mohanakumar
mesh_terms: D001161:Arteriosclerosis / Q000378:metabolism* / Q000473:pathology; D015139:Blotting, Southern; D002339:Carotid Arteries / Q000737:chemistry* / Q000473:pathology; D002340:Carotid Artery Diseases / Q000378:metabolism* / Q000473:pathology; D016893:Carotid Stenosis / Q000209:etiology / Q000378:metabolism; D018834:Chaperonin 60 / Q000032:analysis; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis; D006360:Heat-Shock Proteins / Q000032:analysis*; D006801:Humans; D007150:Immunohistochemistry; D012333:RNA, Messenger / Q000032:analysis; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D018834:Chaperonin 60; C494647:DNAJB1 protein, human; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D012333:RNA, Messenger