title: Clusterin/apolipoprotein J is associated with cortical Lewy bodies: immunohistochemical study in cases with alpha-synucleinopathies.
abstract: Clusterin/apolipoprotein J protein expression in cases with "alpha-synucleinopathies", such as Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy (MSA), was investigated using an immunohistochemical method for the labeling of multiple antigens. About 50% of the cortical Lewy bodies in the cases with DLB were immunoreactive for clusterin, whereas brain-stem Lewy bodies in PD and DLB were rarely associated with clusterin. Clusterin was also immunopositive in around 10% of the glial cytoplasmic inclusions (GCIs) in the cases with MSA. Colocalization of clusterin with alpha-synuclein in such bodies or inclusions was clearly correlated with the immunostaining pattern of alpha-synuclein. Subcellular localization of clusterin was almost completely overlapped with the homogeneous immunoreaction of alpha-synuclein in the cortical Lewy bodies; however, clusterin immunoreactivity was not detected in the halo or ring-like structures of the brain-stem Lewy bodies. Furthermore, some Lewy bodies with intense immunoreactivity for clusterin showed only a weak signal for alpha-synuclein. These results suggest that clusterin may modify the formation of alpha-synuclein-positive inclusion bodies such as Lewy bodies and GCIs, through a previously proposed chaperone property of clusterin.
authors.affiliation: Department of Neuropathology, Neurological Institute, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan. ksasaki@np.med.kyushu-u.ac.jp
authors.forename: Kensuke
authors.initials: K
authors.lastname: Sasaki
authors.forename: Katsumi
authors.initials: K
authors.lastname: Doh-ura
authors.forename: Yoshinobu
authors.initials: Y
authors.lastname: Wakisaka
authors.forename: Toru
authors.initials: T
authors.lastname: Iwaki
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D001057:Apolipoproteins E / Q000096:biosynthesis; D001921:Brain / Q000378:metabolism / Q000473:pathology*; D051152:Clusterin; D006023:Glycoproteins / Q000096:biosynthesis*; D006801:Humans; D007150:Immunohistochemistry; D002479:Inclusion Bodies / Q000473:pathology; D016631:Lewy Bodies / Q000473:pathology*; D020961:Lewy Body Disease / Q000378:metabolism / Q000473:pathology*; D018832:Molecular Chaperones / Q000096:biosynthesis*; D019578:Multiple System Atrophy / Q000378:metabolism / Q000473:pathology*; D009419:Nerve Tissue Proteins / Q000096:biosynthesis*; D016874:Neurofibrillary Tangles / Q000473:pathology; D009457:Neuroglia / Q000473:pathology; D010300:Parkinson Disease / Q000378:metabolism / Q000473:pathology*; D010446:Peptide Fragments / Q000096:biosynthesis; D020774:Pick Disease of the Brain / Q000378:metabolism / Q000473:pathology; D013494:Supranuclear Palsy, Progressive / Q000378:metabolism / Q000473:pathology; D051843:Synucleins; D051844:alpha-Synuclein
chemical_list: D001057:Apolipoproteins E; C495242:CLU protein, human; D051152:Clusterin; D006023:Glycoproteins; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; C497604:SNCA protein, human; D051843:Synucleins; D051844:alpha-Synuclein; C117630:apolipoprotein E (141-155)