Korean J Physiol Pharmacol.  2010 Jun;14(3):163-167. 10.4196/kjpp.2010.14.3.163.

Morinda citrifolia Inhibits Both Cytosolic Ca2+-dependent Phospholipase A2 and Secretory Ca2+-dependent Phospholipase A2

Affiliations
  • 1Department of Pathophysiology, College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea. simss@cau.ac.kr
  • 2Department of Pharmacology, College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea.

Abstract

This study investigated the effects of the methanol extracts of Morinda citrifolia containing numerous anthraquinone and iridoid on phospholipase A2 (PLA2) isozyme. PLA2 activity was measured using various PLA2 substrates, including 10-pyrene phosphatidylcholine, 1-palmitoyl-2-[14C]arachidonyl phosphatidylcholine ([14C]AA-PC), and [3H]arachidonic acid (AA). The methanol extracts suppressed melittin-induced [3H]AA release in a concentration-dependent manner in RAW 264.7 cells, and inhibited cPLA2/sPLA2-induced hydrolysis of [14C]AA-PC in a concentration- and time-dependent manner. A Dixon plot showed that the inhibition by methanol extracts on cPLA2 and sPLA2 appeared to be competitive with inhibition constants (Ki ) of 3.7microgram/ml and 12.6microgram/ml, respectively. These data suggest that methanol extracts of Morinda citrifolia inhibits both Ca2+-dependent PLA2 such as, cPLA2 and sPLA2. Therefore, Morinda citrifolia may possess anti-inflammatory activity secondary to Ca2+-dependent PLA2 inhibition.

Keyword

Morinda citrifolia; Phospholipase A2; Arachidonic acid

MeSH Terms

Arachidonic Acid
Cytosol
Hydrolysis
Methanol
Morinda
Phosphatidylcholines
Phospholipases
Phospholipases A2
Arachidonic Acid
Methanol
Phosphatidylcholines
Phospholipases
Phospholipases A2

Figure

  • Fig. 1. Effects of the methanol extracts on [3H]arachidonic acid (AA) release in RAW 264.7 cells stimulated by 0.5 μM melittin. Cells were incubated with the methanol extracts at 37°C for 10 min and AA release was induced by 0.5 μM melittin. Results are mean±S.D. values from 4 separate experiments. ∗p<0.05 vs melittin.

  • Fig. 2. Effects of methanol extracts on cPLA2 activity. cPLA2 activity was measured using 1-palmitoyl-2-[14C]arachidonyl phosphatidylcholine ([14C]AA-PC) as a substrate by previously methods. The methanol extracts inhibited cPLA2-induced hydrolysis of [14C]AA-PC in a concentration (A)- and time (B)-dependent manner. A Dixon plot showed that cPLA2 inhibition by methanol extracts appeared to be competitive with an inhibition constant (Ki) of 3.7 μg/ml (C). Results are mean±S.D. values from 4 separate experiments. ∗p<0.05 vs control.

  • Fig. 3. Effects of methanol extracts on sPLA2 activity. sPLA2 activity was measured using 1-palmitoyl-2-[14C]arachidonyl phosphatidylcholine ([14C]AA-PC) as a substrate by previously described methods. The methanol extracts inhibited sPLA2-induced hydrolysis of [14C]AA-PC in a concentration (A)- and time (B)-dependent manner. A Dixon plot showed that the inhibition of sPLA2 by methanol extracts appeared to be competitive with an inhibition constant (Ki) of 12.6 μg/ml (C). Results are mean±S.D. values from 4 separate experiments. ∗p<0.05 vs control.

  • Fig. 4. Effects of methanol extracts on bee venom sPLA2 activity with 10-pyrene phosphatidylcholine (10-Pyrene PC). 10-Pyrene PC hydrolyzed by purified sPLA2 was inhibited by the methanol extracts in a concentration-dependent manner. Results are mean± S.D. values from 4 separate experiments. ∗p<0.05 vs control.


Reference

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