GPR34 is a receptor for lysophosphatidylserine with a fatty acid at the sn-2 position
Abstract
GPR34 is a G protein-coupled receptor belonging to the P2Y family. Here, we attempted to resolve conflicting reports about whether it is a functional lysophosphatidylserine (LysoPS) receptor. In HEK293 cells expressing human, mouse or rat GPR34 and Gα chimera between Gαq and Gαi1(Gq/i1), LysoPS quickly elevated intracellular Ca(2+) ion levels ([Ca(2+)](i)). LysoPS also stimulated alkaline phosphatase (AP)-tagged TGFα (AP-TGFα) release in GPR34-expressing HEK293 cells and induced the migration of CHO-K1 cells expressing GPR34. Other lysophospholipids did not induce these actions. Replacement of the serine residue of LysoPS abolished the reactivity of LysoPS with GPR34, indicating that GPR34 strictly recognizes the serine head group of LysoPS. Recombinant phosphatidylserine-specific phospholipase A(1) (PS-PLA(1)) that deacylates fatty acid at the sn-1 position of PS and produces 2-acyl-LysoPS, but not catalytically inactive mutant PS-PLA(1), stimulated the release of AP-TGFα from GPR34-expressing cells. Consistent with the result, LysoPS was detected in the cells treated with wild-type PS-PLA(1) but not with the mutant PS-PLA(1). PS treated with PLA(1) was much more effective at stimulating AP-TGFα release than PS treated with PLA(2). In addition, migration-resistant 2-acyl-1-deoxy-LysoPS, a 2-acyl-LysoPS analogue, was much more potent than 1-acyl-2-deoxy-LysoPS. The present studies confirm that GPR34 is a cellular receptor for LysoPS, especially with a fatty acid at the sn-2 position.
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The function and importance of Gpr34 and its protein product remain largely undetermined, though its suspected role in detecting short chain fatty acids may implicate it in both metabolic and immune pathways.
“The function and importance of Gpr34 and its protein product remain largely undetermined, though its suspected role in detecting short chain fatty acids may implicate it in both metabolic and immune pathways (45, 98).”
From The Transcriptional Landscape of Microglial Genes in Aging and Neurodegenerative Disease (2019) · cites this paper as [98]
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Additional file 3 of Glioblastoma hijacks microglial gene expression to support tumor growth
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- Authors
- Kitamura, H., Makide, K., Shuto, A., Ikubo, M., Inoue, A., Suzuki, K., Sato, Y., Nakamura, S., Otani, Y., Ohwada, T., & Aoki, J.
- Affiliations
- Tohoku University (JP)
- Corresponding author
- Ohwada, Tomohiko
- Venue
- The Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 2012-02-16
- Volume
- 151
- Issue
- 5
- Pages
- 511-518
- ISSN
- 0021-924X (ISSN-L)
- 1756-2651
- OpenAlex
- W1999367048
- Cited by
- 86
- References
- 23
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 7 · 2023: 9 · 2022: 4 · 2021: 6 · 2020: 13 · 2019: 4 · 2018: 4 · 2017: 2 · 2016: 6 · 2015: 5 · 2014: 7 · 2013: 9 · 2012: 2
- FWCI
- 2.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Japan Society for the Promotion of Science (21390015, 24659025, 23790006, 21770102, 22659013)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- GPR34, lysophosphatidylserine, G protein-coupled receptors, P2Y receptors, phospholipase A1, phosphatidylserine, intracellular calcium, cell migration, receptor specificity, lysophospholipids
- MeSH terms
- Animals, Cell Movement, Cells, Cultured, Fatty Acids, Cricetinae, Humans, Lysophospholipids, Molecular Structure, CHO Cells, Receptors, Lysophospholipid, Mice, Rats, HEK293 Cells
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