title: Cerebellar Purkinje cells exhibit increased expression of HMGB-1 and apoptosis in congenital hydrocephalic H-Tx rats.
abstract: BACKGROUND
  Highly integrated anatomic and functional interactions between the cerebrum and the cerebellum during development have been reported. In our previous study, we conducted a proteome analysis to identify the proteins present in the congenital noncommunicating hydrocephalus in the cerebellum. We found higher expression of high-mobility group box-1 protein (HMGB-1) in hydrocephalic H-Tx rats.
  
  
  OBJECTIVE
  We studied the expression pattern of HMGB-1 in the cerebellum.
  
  
  METHODS
  We studied congenital hydrocephalic H-Tx rats aged 1 day and 7 days along with age-matched nonhydrocephalic H-Tx and Sprague-Dawley rats as controls. Gene and protein expressions of HMGB-1 in the cerebellum were assayed by real-time polymerase chain reaction and Western blotting, respectively; furthermore, immunohistochemical analyses were performed by using HMGB-1 (indicator of apoptosis), single-stranded DNA; adhesion factor related to cell migration, HNK-1; and the Purkinje cell-specific antibody, calbindin.
  
  
  RESULTS
  Cytoplasmic HMGB-1 expression observed in Purkinje cells in the 1-day-old hydrocephalic group was stronger than that in the nonhydrocephalic and Sprague-Dawley groups. Double fluorescent staining with single-stranded DNA confirmed that Purkinje cells were undergoing apoptosis. HNK-1 expression was lower in the Purkinje cell layer in the 7-day-old rats in the hydrocephalic group, and Purkinje cells were disrupted in comparison with the control groups. Morphological changes in the cerebellum were observed in the 7-day-old rats in the hydrocephalic group in comparison with the control groups.
  
  
  CONCLUSIONS
  Our results suggest that cerebellar neuronal cell damage in the early postnatal period may be related to the higher expression of HMGB-1 in the Purkinje cells.
authors.affiliation: Department of Neurosurgery and Research Institute for Diseases of Old Age, Juntendo University School of Medicine, Tokyo, Japan. mitsuya.med-juntendo@tamanan-hp.com
authors.forename: Mitsuya
authors.initials: M
authors.lastname: Watanabe
authors.forename: Masakazu
authors.initials: M
authors.lastname: Miyajima
authors.forename: Ikuko
authors.initials: I
authors.lastname: Ogino
authors.forename: Madoka
authors.initials: M
authors.lastname: Nakajima
authors.forename: Hajime
authors.initials: H
authors.lastname: Arai
mesh_terms: D000704:Analysis of Variance; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D015153:Blotting, Western; D002531:Cerebellum / Q000473:pathology; D005455:Fluorescent Antibody Technique; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D024243:HMGB1 Protein / Q000096:biosynthesis*; D006849:Hydrocephalus / Q000151:congenital / Q000378:metabolism* / Q000473:pathology; D007150:Immunohistochemistry; D011689:Purkinje Cells / Q000378:metabolism* / Q000473:pathology; D051381:Rats; D017207:Rats, Sprague-Dawley; D060888:Real-Time Polymerase Chain Reaction; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000378:metabolism
chemical_list: D024243:HMGB1 Protein; C104200:Hbp1 protein, rat; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases