sPLA₂ (human, recombinant Type X)

Secretory phospholipase A₂ (sPLA₂) (Type X) is a calcium-dependent PLA₂ superfamily member that is encoded by PLA2G10 in humans.¹ It is composed of an N-terminal signal peptide, a highly-conserved calcium-binding loop, a catalytic domain, sPLA₂ Type I- and II-specific disulfides that provide stability, and a C-terminal extension. sPLA₂ (Type X) is expressed in spleen, thymus, peripheral blood leukocytes, pancreas, lung, and colon, as well as neutrophils and keratinocytes.^2,3,4 Upon activation, sPLA₂ (Type X) is released into the extracellular space where it acts in a paracrine or autocrine manner and preferentially catalyzes the hydrolysis of phosphatidylethanolamine (PE) and phosphatidylcholine (PC) over phosphatidylserine (PS) at the sn-2 position, liberating the free fatty acid and lysophospholipid, which serve as substrates for the synthesis of bioactive lipid metabolites.^2,1 sPLA₂ (Type X) increases arachidonic acid (Item Nos. 90010 | 90010.1 | 10006607) release from HEK293 cells and prostaglandin E₂ (Item No. 14010) levels in HEK293 cells expressing human COX-2 but not COX-1.⁵ Pla2g10^-/- mice have decreased inflammatory cell infiltration and airway edema in a model of ovalbumin-induced allergic asthma.⁶ Airway lining fluid levels of sPLA₂ (Type X) are increased in patients with asthma.⁷ Cayman’s sPLA₂ (human, recombinant Type X) protein can be used for enzyme activity assays. The specific activity of Cayman's sPLA₂ (human, recombinant Type X) was established using Cayman’s sPLA₂ Assay Kit (Item No. 765001) with 1.48 mM 1,2-bis(heptanoylthio) glycerophosphocholine (Item No. 62235) as the substrate.

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1. Murakami, M., Taketomi, Y., Sato, H., et al. Secreted phospholipase A₂ revisited. J. Biochem. 150(3), 233-255 (2011).

2. Cupillard, L., Koumanov, K., Mattéi, M.G., et al. Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A₂. The Journal of Biological Chemisty 272(25), 15745-15752 (1997).

3. Degousee, N., Ghomashchi, F., Stefanski, E., et al. Groups IV, V, and X phospholipases A₂s in human neutrophils. Role in eicosanoid production and Gram-negative bacterial phospholipid hydrolysis. The Journal of Biological Chemisty 277(7), 5061-5073 (2002).

4. Schadow, A., Scholz-Pedretti, K., Lambeau, G., et al. Characterization of group X phospholipase A₂ as the major enzyme secreted by human keratinocytes and its regulation by the phorbol ester TPA. J. Invest. Dermatol. 116(1), 31-39 (2001).

5. Bezzine, S., Koduri, R.S., Valentin, E., et al. Exogenously added human group X secreted phospholipase A₂ but not the group I B, I I A, and V enzymes effeciently release arachidonic acid from adherent mammalian cells. The Journal of Biological Chemisty 275, 3179-3191 (2000).

6. Henderson, W.R., Jr., Chi, E.Y., Bollinger, J.G., et al. Importance of group X-secreted phospholipase A₂ in allergen-induced airway inflammation and remodeling in a mouse asthma model. J. Exp. Med. 204(4), 865-877 (2007).

7. Hallstrand, T.S., Lai, Y., Altemeier, W.A., et al. Regulation and function of epithelial secreted phospholipase A₂ group X in asthma. Am. J. Respir. Crit. Care Med. 188(1), 42-50 (2013).