Antigen: mouse group V sPLA₂ amino acids 79-94 (CAIRTQSYDYRYTNGL) · Host: rabbit · Application(s): WB · Phospholipase A₂ (PLA₂) catalyzes the hydrolysis of fatty acids at the sn-2 position of glycerophospholipids. PLA₂ (Type V) is a secretory PLA₂ (sPLA₂) of approximately 14 kDa and is one of the isoforms in the growing list of the PLA₂ enzyme family.¹ This enzyme, rather than the sPLA₂ (Type II), is responsible for arachidonic acid mobilization leading to prostaglandin production in macrophages and mast cells.^2,3,4 Consistent with this role, sPLA₂ (Type V) is associated with the golgi apparatus, nuclear envelope, and plasma membrane in mouse bone marrow-derived mast cells.⁵ sPLA₂ (Type V) has been cloned from a variety of species including human, mouse, and rat.^6,7,8 The enzyme is expressed in heart, lung, placenta, spleen, as well as mouse P388D1 macrophages and mast cells.^2,3,6,8

1 Dennis, E.A. The growing phospholipase A₂ superfamily of signal transduction enzymes. Trends Biochem Sci 22 1-2 (1997).

2 Balboa, M.A., Balsinde, J., Winstead, M.V., et al. Novel group V phospholipase A₂ involved in arachidonic acid mobilization in murine P388D1 macrophages. J Biol Chem 271 32381-32384 (1996).

3 Reddy, S.T., Winstead, M.V., Tischfield, J.A., et al. Analysis of the secretory phospholipase A₂ that mediates prostaglandin production in mast cells. J Biol Chem 272 13591-13596 (1997).

4 Bingham, C.O., Murakami, M., Fujishima, H., et al. A heparin-sensitive phospholipase A₂ and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase of prostaglandin D₂ generation in mouse bone marrow-derived mast cells. J Biol Chem 271 25936-25944 (1996).

5 Bingham, C.O., Fijneman, R.J.A., Friend, D.S., et al. Low molecular weight group IIA and group V phospholipase A₂ enzymes have different intracellular locations in mouse bone marrow-derived mast cells. J Biol Chem 274 31476-31484 (1999).

6 Chen, J., Engle, S.J., Seilhamer, J.J., et al. Cloning and recombinant expression of a novel human low molecular weight Ca2+-dependent phospholipase A₂. J Biol Chem 269 2365-2368 (1994).

7 Tischfield, J.A., Xia, Y., Shih, D.M., et al. Low-molecular-weight, calcium-dependent phospholipase A₂ genes are linked and map to homologous chromosome regions in mouse and human. Genomics 32 328-333 (1996).

8 Chen, J., Engle, S.J., Seilhamer, J.J., et al. Cloning, expression and partial characterization of a novel rat phospholipase A₂. Biochim Biophys Acta 1215 115-120 (1994).

Balboa, M.A., Balsinde, J., Winstead, M.V., et al. Novel group V phospholipase A₂ involved in arachidonic acid mobilization in murine P388D1 macrophages. J Biol Chem 271 32381-32384 (1996).

Dennis, E.A. The growing phospholipase A₂ superfamily of signal transduction enzymes. Trends Biochem Sci 22 1-2 (1997).

Reddy, S.T., Winstead, M.V., Tischfield, J.A., et al. Analysis of the secretory phospholipase A₂ that mediates prostaglandin production in mast cells. J Biol Chem 272 13591-13596 (1997).

Chen, J., Engle, S.J., Seilhamer, J.J., et al. Cloning, expression and partial characterization of a novel rat phospholipase A₂. Biochim Biophys Acta 1215 115-120 (1994).

Chen, J., Engle, S.J., Seilhamer, J.J., et al. Cloning and recombinant expression of a novel human low molecular weight Ca2+-dependent phospholipase A₂. J Biol Chem 269 2365-2368 (1994).

Bingham, C.O., Fijneman, R.J.A., Friend, D.S., et al. Low molecular weight group IIA and group V phospholipase A₂ enzymes have different intracellular locations in mouse bone marrow-derived mast cells. J Biol Chem 274 31476-31484 (1999).

Tischfield, J.A., Xia, Y., Shih, D.M., et al. Low-molecular-weight, calcium-dependent phospholipase A₂ genes are linked and map to homologous chromosome regions in mouse and human. Genomics 32 328-333 (1996).

Cupillard, L., Koumanov, K., Mattéi, M., et al. Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A₂. J Biol Chem 272 15745-15752 (1997).

Bingham, C.O., Murakami, M., Fujishima, H., et al. A heparin-sensitive phospholipase A₂ and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase of prostaglandin D₂ generation in mouse bone marrow-derived mast cells. J Biol Chem 271 25936-25944 (1996).

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