Differences between group X and group V secretory phospholipase A2 in lipolytic modification of lipoproteins

• Autorzy: Kamitani S. , Yamada K. , Yamamoto S. , Ishimoto Y. , Ono T. , Saiga A. , Hanasaki K.
• Języki publikacji: EN

Abstrakty

EN

Secretory phospholipases A2 (sPLA2s) are a diverse family of low molecular mass enzymes (13–18 kDa) that hydrolyze the sn-2 fatty acid ester bond of glycerophospholipids to produce free fatty acids and lysophospholipids. We have previously shown that group X sPLA2 (sPLA2-X) had a strong hydrolyzing activity toward phosphatidylcholine in low-density lipoprotein (LDL) linked to the formation of lipid droplets in the cytoplasm of macrophages. Here, we show that group V sPLA2 (sPLA2-V) can also cause the lipolysis of LDL, but its action differs remarkably from that of sPLA2-X in several respects. Although sPLA2-V released almost the same amount of fatty acids from LDL, it released more linoleic acid and less arachidonic acid than sPLA2-X. In addition, the requirement of Ca2+ for the lipolysis of LDL was about 10-fold higher for sPLA2-V than sPLA2-X. In fact, the release of fatty acids from human serum was hardly detectable upon incubation with sPLA2-V in the presence of sodium citrate, which contrasted with the potent response to sPLA2-X. Moreover, sPLA2-X, but not sPLA2-V, was found to specifically interact with LDL among the serum proteins, as assessed by gel-filtration chromatography as well as sandwich enzyme-immunosorbent assay using anti-sPLA2-X and anti-apoB antibodies. Surface plasmon resonance studies have revealed that sPLA2-X can bind to LDL with high-affinity (Kd = 3.1 nM) in the presence of Ca2+. Selective interaction of sPLA2-X with LDL might be involved in the efficient hydrolysis of cell surface or intracellular phospholipids during foam cell formation.

Słowa kluczowe

EN

secretory phospholipase; phospholipase A2; lipolytic modification; lipoprotein; low-density lipoprotein; high-density lipoprotein; phospholipid; calcium ion; antibody; apolipoprotein; cyclooxygenase; high performance liquid chromatography

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2012
• Tom: 17
• Numer: 3
• Opis fizyczny: p.459-478,fig.,ref.

Twórcy

autor

Kamitani S.

• Department of Molecular Bacteriology, RIMD, Osaka University, 3-1 Yamada-oka, Suita-shi, Osaka 565-0871,Japan

autor

Yamada K.

autor

Yamamoto S.

autor

Ishimoto Y.

autor

Ono T.

autor

Saiga A.

autor

Hanasaki K.

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