title: Tubedown-1 (Tbdn-1) suppression in oxygen-induced retinopathy and in retinopathy of prematurity.
abstract: OBJECTIVE
  Identification of unique proteins involved in retinopathy of prematurity (ROP) may facilitate new and more effective diagnostic tools and molecular-based treatments for ROP. Tubedown-1 (Tbdn-1), a novel homeostatic protein which copurifies with an acetyltransferase activity, is expressed in normal retinal endothelium and is specifically suppressed in retinal endothelial cells from patients with proliferative diabetic retinopathy. Furthermore, recent in vivo knockdown studies in mice have revealed that Tbdn-1 is important for retinal blood vessel homeostasis and for preventing retinal neovascularization in adults. The purpose of the present study was to determine if the expression pattern of Tbdn-1 is altered during oxygen-induced retinal neovascularization in mice and in a specimen of stage 3 human ROP.
  
  
  METHODS
  Specimens of oxygen-induced retinal neovascularization in mice, and a single specimen of active stage 3 ROP were studied by immunohistochemistry and digital image analysis using antibodies raised against Tbdn-1 and other blood vessel markers.
  
  
  RESULTS
  The pattern of Tbdn-1 expression during the course of oxygen-induced retinal neovascularization in mice suggests a regulating role in neonatal retinopathy. Retinal lesions from oxygen-induced retinal neovascularization in mice display suppression of retinal endothelial Tbdn-1 protein expression in conjunction with an increase in expression of proliferating cell nuclear antigen (a marker of proliferation) and alpha smooth muscle actin (a marker of myofibroblastic cells). Abnormal blood vessels within vitreoretinal neovascular lesions in a human specimen of active stage 3 ROP did not show Tbdn-1 protein expression.
  
  
  CONCLUSIONS
  These results suggest that the loss of retinal endothelial Tbdn-1 expression may be a contributing factor in retinal blood vessel proliferation in ROP.
authors.affiliation: Division of Basic Medical Sciences, Department of Medicine, Memorial University of Newfoundland, St. John's, Newfoundland, Canada. rgendron@mun.ca
authors.forename: Robert L
authors.initials: RL
authors.lastname: Gendron
authors.forename: William V
authors.initials: WV
authors.lastname: Good
authors.forename: Ewa
authors.initials: E
authors.lastname: Miskiewicz
authors.forename: Stephanie
authors.initials: S
authors.lastname: Tucker
authors.forename: Dale L
authors.initials: DL
authors.lastname: Phelps
authors.forename: Helene
authors.initials: H
authors.lastname: Paradis
mesh_terms: D000123:Acetyltransferases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D006801:Humans; D007150:Immunohistochemistry; D007231:Infant, Newborn; D051379:Mice; D008810:Mice, Inbred C57BL; D009130:Muscle, Smooth / Q000378:metabolism; D010100:Oxygen; D018809:Proliferating Cell Nuclear Antigen / Q000378:metabolism; D015861:Retinal Neovascularization / Q000139:chemically induced* / Q000150:complications / Q000378:metabolism*; D012178:Retinopathy of Prematurity / Q000209:etiology / Q000378:metabolism*
chemical_list: D000199:Actins; D018809:Proliferating Cell Nuclear Antigen; D000123:Acetyltransferases; D010100:Oxygen