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A Novel Calcium-independent Phospholipase A2, cPLA2-γ, That Is Prenylated and Contains Homology to cPLA2
Open accessAbstract
We report the cloning and characterization of a novel membrane-bound, calcium-independent PLA2, named cPLA2-gamma. The sequence encodes a 541-amino acid protein containing a domain with significant homology to the catalytic domain of the 85-kDa cPLA2 (cPLA2-alpha). cPLA2-gamma does not contain the regulatory calcium-dependent lipid binding (CaLB) domain found in cPLA2-alpha. However, cPLA2-gamma does contain two consensus motifs for lipid modification, a prenylation motif (-CCLA) at the C terminus and a myristoylation site at the N terminus. We present evidence that the isoprenoid precursor [3H]mevalonolactone is incorporated into the prenylation motif of cPLA2-gamma. Interestingly, cPLA2-gamma demonstrates a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid. cPLA2-gamma encodes a 3-kilobase message, which is highly expressed in heart and skeletal muscle, suggesting a specific role in these tissues. Identification of cPLA2-gamma reveals a newly defined family of phospholipases A2 with homology to cPLA2-alpha.
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Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943
Clark, J. D., Lin, L.-L., Kriz, R. W., Ramesha, C. S., Sultzman, L. A., Lin, A. Y., Milona, N., & Knopf, J. L. (1991) · Cell · doi:10.1016/0092-8674(91)90556-e · Cited by 1,688
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Physiology of cell volume regulation in vertebrates
Hoffmann, E. K., Lambert, I. H., & Pedersen, S. F. (2009) · Physiological Reviews · doi:10.1152/physrev.00037.2007 · Cited by 1,441
The phospholipase A2 superfamily and its group numbering system
Schaloske, R. H., & Dennis, E. A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.07.011 · Cited by 936
Burke, J. E., & Dennis, E. A. (2009) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-008-6132-9 · Cited by 431
The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease
Long, J. Z., & Cravatt, B. F. (2011) · Chemical Reviews · doi:10.1021/cr200075y · Cited by 425
Schaeffer, E. L., Forlenza, O. V., & Gattaz, W. F. (2009) · Psychopharmacology · doi:10.1007/s00213-008-1351-0 · Cited by 71
Metadata
- Authors
- Underwood, K. W., Song, C., Kriz, R. W., Chang, X. J., Knopf, J. L., & Lin, L.-L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-08
- Volume
- 273
- Issue
- 34
- Pages
- 21926-21932
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2027145809
- Cited by
- 224
- References
- 2
- FWCI
- 10.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Underwood, K. W., Song, C., Kriz, R. W., Chang, X. J., Knopf, J. L., & Lin, L.-L. (1998). A Novel Calcium-independent Phospholipase A2, cPLA2-γ, That Is Prenylated and Contains Homology to cPLA2. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.34.21926
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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