title: Upregulated expression of 14-3-3 proteins in astrocytes from human cerebrovascular ischemic lesions.
abstract: OBJECTIVE
  Several types of chaperone proteins, such as heat shock proteins, have been reported to be associated with brain ischemia. The purpose of this study was to investigate whether an abnormal expression of 14-3-3 proteins, a novel type of molecular chaperones, occurs in human gray and white matter ischemic lesions.
  
  
  METHODS
  We prepared formalin-fixed, paraffin-embedded sections from 33 autopsied brains, consisting of 7 normal controls, 4 cases with cerebral thrombosis, 5 cases with cerebral embolism, 8 cases with multiple lacunar infarctions, and 9 cases with Binswanger disease. Deparaffinized sections from all cases were immunostained with anti-14-3-3 antibodies using the avidin-biotin-peroxidase complex method, and some sections were also double-immunostained for 14-3-3 and glial markers.
  
  
  RESULTS
  In the normal control brains, 14-3-3 immunoreactivity was mainly localized to the neuronal somata and processes. Strongly 14-3-3-immunopositive astrocytes were distributed in the infarct lesions and were particularly abundant in infarcts at the chronic stage. Intensely 14-3-3-immunolabeled astrocytes were also observed in the ischemic white matter lesions, and in the severely affected white matter lesions from patients with Binswanger disease, dense 14-3-3 immunoreactivity was found in clasmatodendritic astroglia as well as in reactive astrocytes.
  
  
  CONCLUSIONS
  Our results suggest that 14-3-3 proteins may be induced mainly in astrocytes from human cerebrovascular ischemic lesions, and that the upregulated expression of 14-3-3 proteins in astrocytes may be involved in the formation of astrogliosis.
authors.affiliation: Department of Neurology, Faculty of Medicine, Kyoto University, Japan. kawamoto@kuhp.kyoto-u.ac.jp
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Kawamoto
authors.forename: Ichiro
authors.initials: I
authors.lastname: Akiguchi
authors.forename: Hidekazu
authors.initials: H
authors.lastname: Tomimoto
authors.forename: Yoshitomo
authors.initials: Y
authors.lastname: Shirakashi
authors.forename: Yasuyuki
authors.initials: Y
authors.lastname: Honjo
authors.forename: Herbert
authors.initials: H
authors.lastname: Budka
mesh_terms: D048948:14-3-3 Proteins / Q000096:biosynthesis*; D000368:Aged; D000369:Aged, 80 and over; D001253:Astrocytes / Q000378:metabolism*; D001344:Autopsy; D001921:Brain / Q000033:anatomy & histology / Q000473:pathology; D020520:Brain Infarction / Q000473:pathology; D002540:Cerebral Cortex / Q000473:pathology; D002561:Cerebrovascular Disorders / Q000378:metabolism* / Q000473:pathology; D015140:Dementia, Vascular / Q000473:pathology; D005260:Female; D005625:Frontal Lobe / Q000473:pathology; D005786:Gene Expression Regulation; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D006801:Humans; D020766:Intracranial Embolism / Q000473:pathology; D020767:Intracranial Thrombosis / Q000473:pathology; D007511:Ischemia / Q000473:pathology*; D008297:Male; D008875:Middle Aged; D009457:Neuroglia / Q000473:pathology; D020033:Protein Isoforms; D012044:Regression Analysis; D015854:Up-Regulation; D014746:Vimentin / Q000378:metabolism
chemical_list: D048948:14-3-3 Proteins; D005904:Glial Fibrillary Acidic Protein; D020033:Protein Isoforms; D014746:Vimentin