TY - JOUR
T1 - Switching of platelet-activating factor acetylhydrolase catalytic subunits in developing rat brain
AU - Manya, Hiroshi
AU - Aoki, Junken
AU - Watanabe, Masahiko
AU - Adachi, Tomoya
AU - Asou, Hiroaki
AU - Inoue, Yoshirou
AU - Arai, Hiroyuki
AU - Inoue, Keizo
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1998/7/17
Y1 - 1998/7/17
N2 - In a previous study, we demonstrated that Platelet-activating Factor (PAF) acetylhydrolase purified from bovine brain cortical cytosol consists of two mutually homologous catalytic subunits(α1 and α2) and one putative regulatory β subunit. The latter is a product of the LIS1 gene, which is defective in the Miller-Dicker syndrome, a form of lissencephaly. In this study, we examined the expression patterns of these three subunits in the developing rat brain. All three subunits were expressed in embryonic brain, whereas only α2 and β subunit were detected in the adult brain by Western blotting. Biochemical analyses revealed that the α1/α2 heterodimer and α2/α2 homodimer are major catalytic units of embryonic and adult brain PAF acetylhydrolases, respectively. The α1 transcript and protein were detected predominantly in embryonic and postnatal neural tissues, such as the brain and spinal cord. Furthermore, we found using primary cultured cells isolated from neonatal rat brain that α1 protein were expressed only in neurons but not in glial cells and fibroblasts. In contrast, α2 and β transcripts and proteins were detected both in neural and non-neural tissues, and their expression level was almost constant from fetal stages through adulthood. These results indicate that α1 expression is restricted to actively migrating neurons in rats and that switching of catalytic subunits from the α1/α2 heterodimer to the α2/α2 homodimer occurred in these cells during brain development, suggesting that PAF acetylhydrolase plays a role(s) in neuronal migration.
AB - In a previous study, we demonstrated that Platelet-activating Factor (PAF) acetylhydrolase purified from bovine brain cortical cytosol consists of two mutually homologous catalytic subunits(α1 and α2) and one putative regulatory β subunit. The latter is a product of the LIS1 gene, which is defective in the Miller-Dicker syndrome, a form of lissencephaly. In this study, we examined the expression patterns of these three subunits in the developing rat brain. All three subunits were expressed in embryonic brain, whereas only α2 and β subunit were detected in the adult brain by Western blotting. Biochemical analyses revealed that the α1/α2 heterodimer and α2/α2 homodimer are major catalytic units of embryonic and adult brain PAF acetylhydrolases, respectively. The α1 transcript and protein were detected predominantly in embryonic and postnatal neural tissues, such as the brain and spinal cord. Furthermore, we found using primary cultured cells isolated from neonatal rat brain that α1 protein were expressed only in neurons but not in glial cells and fibroblasts. In contrast, α2 and β transcripts and proteins were detected both in neural and non-neural tissues, and their expression level was almost constant from fetal stages through adulthood. These results indicate that α1 expression is restricted to actively migrating neurons in rats and that switching of catalytic subunits from the α1/α2 heterodimer to the α2/α2 homodimer occurred in these cells during brain development, suggesting that PAF acetylhydrolase plays a role(s) in neuronal migration.
UR - http://www.scopus.com/inward/record.url?scp=0032541046&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032541046&partnerID=8YFLogxK
U2 - 10.1074/jbc.273.29.18567
DO - 10.1074/jbc.273.29.18567
M3 - Article
C2 - 9660828
AN - SCOPUS:0032541046
VL - 273
SP - 18567
EP - 18572
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 29
ER -