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Reduced expression of MAb6B4 epitopes on chondroitin sulfate proteoglycan aggrecan in perineuronal nets from cerebral cortices of SAMP10 mice: A model for age‐dependent neurodegeneration
Author(s) -
Saitoh Yuko,
Matsui Fumiko,
Chiba Yoichi,
Kawamura Noriko,
Keino Hiromi,
Satoh Mamoru,
Kumagai Naoko,
Ishii Sanae,
Yoshikawa Keisuke,
Shimada Atsuyoshi,
Maeda Nobuaki,
Oohira Atsuhiko,
Hosokawa Masanori
Publication year - 2007
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.21582
Subject(s) - perineuronal net , epitope , aggrecan , proteoglycan , neurodegeneration , chondroitin sulfate proteoglycan , biology , monoclonal antibody , glycoprotein , immunostaining , microbiology and biotechnology , neuroscience , antibody , pathology , immunology , immunohistochemistry , central nervous system , medicine , alternative medicine , disease , extracellular matrix , osteoarthritis , articular cartilage
The accelerated senescence‐prone SAMP10 mouse strain is a model for age‐dependent neurodegeneration and is characterized by brain atrophy and deficits in learning and memory. Because perineuronal nets play an important role in the synaptic plasticity of adult brains, we examined the distributions of molecules that constitute perineuronal nets in SAMP10 mouse brain samples and compared them with those in control SAMR1 mouse samples. Proteoglycan‐related monoclonal antibody 6B4 (MAb6B4) clearly immunostained perineuronal nets in SAMR1 mice cortices, but the corresponding immunostaining in SAMP10 mice was very faint. MAb6B4 recognizes phosphacan/PTPζ in immature brains. However, this antibody recognized several protein bands, including a 400‐kDa core glycoprotein from chondroitin sulfate proteoglycan in homogenates of mature cortices from SAMR1 mice. The 400‐kDa band was also recognized by antiaggrecan antibodies. The aggrecan core glycoprotein band was also detectable in samples from SAMP10 mice, but this glycoprotein was faintly immunostained by MAb6B4. Because MAb6B4 recognized the same set of protein bands that the monoclonal antibody Cat‐315 recognized in mature cerebral cortices of SAMR1 mice, the MAb6B4 epitope appears to be closely related to that of Cat‐315 and presumably represents a novel type of oligosaccharide that attaches to aggrecans. The Cat‐315 epitope colocalized with aggrecan in perineuronal nets from SAMR1 mouse brain samples, whereas its expression was prominently reduced in SAMP10 mouse brain samples. The biological significance of the MAb6B4/Cat‐315 epitope in brain function and its relationship to the neurodegeneration and learning disabilities observed in SAMP10 mice remain to be elucidated. © 2007 Wiley‐Liss, Inc.