Molecular cloning of Bral2, a novel brain-specific link protein, and immunohistochemical colocalization with brevican in perineuronal nets.
The hyaluronan binding chondroitin sulphate proteoglycans, called lecticans, are the abundant extracellular matrix molecules in the developing and/or adult brain. The link proteins (LPs) are also known to be coordinately present in brain. We report here the molecular cloning and expression analysis of a novel member of LPs: Bral2, predominantly expressed in brain. The Bral2 mRNA expression is first detected at P20 and continued through adulthood, suggesting its functional importance and association with adult-type lecticans. The substantial immunoreactivity of Bral2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern. In situ hybridization revealed that Bral2 is synthesized by these neurons themselves, especially by the GABAergic neurons in the cerebellar cortex. Interestingly, the colocalization and synergic importance of Bral2 and brevican in the perineuronal nets is indicated by the comparative immunohistochemical analysis using wild-type and brevican-deficient mouse brain. Our results suggest that Bral2 is involved in the formation of extracellular matrix contributing to perineuronal nets and facilitate the understanding of a functional role of these extracellular matrices.
Bekku
Yoko
Y
Department of Molecular Biology and Biochemistry, Okayama University Graduate School of Medicine and Dentistry, Okayama 700-8558, Japan.
Su
Wei-Dong
WD
Hirakawa
Satoshi
S
Fässler
Reinhard
R
Ohtsuka
Aiji
A
Kang
Jeong Suk
JS
Sanders
Jennifer
J
Murakami
Takuro
T
Ninomiya
Yoshifumi
Y
Oohashi
Toshitaka
T
D000818:Animals; D001370:Axonal Transport / Q000502:physiology; D001921:Brain / Q000166:cytology / Q000378:metabolism*; D058581:Brevican; D002531:Cerebellum / Q000166:cytology / Q000378:metabolism; D011508:Chondroitin Sulfate Proteoglycans / Q000172:deficiency / Q000235:genetics; D002874:Chromosome Mapping; D002888:Chromosomes, Human, Pair 19; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000302:isolation & purification*; D006801:Humans; D007150:Immunohistochemistry; D037181:Lectins, C-Type; D051379:Mice; D008807:Mice, Inbred BALB C; D018345:Mice, Knockout; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000172:deficiency / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D017729:Presynaptic Terminals / Q000378:metabolism; D011509:Proteoglycans / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D053675:Versicans; D000099249:Proteoglycan Link Protein
D058581:Brevican; D011508:Chondroitin Sulfate Proteoglycans; D018076:DNA, Complementary; D016326:Extracellular Matrix Proteins; D037181:Lectins, C-Type; D009419:Nerve Tissue Proteins; D011509:Proteoglycans; D012333:RNA, Messenger; D053675:Versicans; C546938:BCAN protein, human; C553057:Bcan protein, mouse; C415863:HAPLN2 protein, human; D000099249:Proteoglycan Link Protein; C480571:HAPLN4 protein, human; C485934:Hapln2 protein, mouse; C480570:Hapln4 protein, mouse; C508322:VCAN protein, human; C508323:Vcan protein, mouse