Cellular expression and subcellular localization of autotaxin, a lysophosphatidic acid-generating enzyme, in the adult and developing mouse brain

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Authors: Masanori Tachikawa, Masahiro Fukaya, Eriko Miura, Zhengyu Zhang, Shinichi Okudaira, Chihiro Takasaki, Ken‐ichi Hosoya, Junken Aoki, Masahiko Watanabe
Cited by: 1
References: 73

Abstract

Autotaxin (ATX) is a lysophosphatidic acid-producing enzyme. In this study, we describe the cellular expression and subcellular localization of ATX in the mouse brain, thereby providing a fundamental framework for understanding lysophosphatidic acid signaling in vivo . High expression levels of ATX in the choroid plexus were observed in both developing and adult brains. ATX was localized predominantly at the cerebrospinal fluid (CSF)—facing apical side of choroid plexus epithelial cells, suggesting preferential secretion of ATX towards the CSF. High ATX expression was detected in oligodendrocytes and low-to-moderate levels were detected in neurons and astrocytes. ATX was preferentially localized in vesicle- and endoplasmic reticulum–rich regions of the cytoplasm. In the embryonic and early postnatal brain, ATX immunolabeling was intensely detected in neuronal perikarya and processes, whereas it was faint in the radial glia/astrocyte lineage. A marked upregulation of ATX in oligodendrocytes was observed during the active myelination stage that persisted into adulthood. The highly regulated, cell type–dependent expression of ATX suggests that ATX is a key regulatory factor for lysophosphatidic acid signaling in brain development and function. • ATX shows predominant localization at the CSF-facing apical side of choroid plexus. • Quantitative proteomics determines the absolute expression level of ATX in the CSF. • ATX is detected in neuronal processes of embryonic and early postnatal brains. • ATX expression in oligodendrocytes is upregulated during active myelination stage.

Fields of Study & Subjects

Sphingolipid Metabolism and Signaling Bone Metabolism and Diseases ATP Synthase and ATPases Research

Publication details

Journal / source
Neuroscience Research
Publisher
Elsevier BV
Volume
227
Pages
105062–105062
Publication date
27 April 2026
Language
EN