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Effects of mastoparan B and its analogs on the phospholipase D activity in L1210 cells
Author(s) -
Lee Sang Yoon,
Park Nam Gyu,
Choi Myung-Un
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00831-x
Subject(s) - mastoparan , phospholipase d , phosphatidylethanol , chemistry , peptide , stimulation , phospholipase , biochemistry , membrane , g protein , phosphatidic acid , enzyme , biology , phospholipid , endocrinology , receptor
Mastoparan B (MP‐B), an amphiphilic α‐helical peptide isolated from hornet venom, and its Ala‐substituted analogs were examined for their effectiveness on phospholipase D (PLD) activity in L1210 cells. PLD activity was determined by measuring phosphatidylethanol produced from [ 3 H]myristate‐labelled cells in the presence of ethanol. PLD activity was stimulated by MP‐B, 4MP‐B (Lys 4 →Ala), and 12MP‐B (Lys 12 →Ala), but not by 3MP‐B (Leu 3 →Ala) and 9MP‐B (Trp 9 →Ala). Other MPs including mastoparan 7 also stimulated the PLD activity, but inactive mastoparan 17 did not. The stimulatory effect of various MP analogs could be correlated with their α‐helical contents. The PLD activity stimulated by MP‐B was not affected by G‐protein blocking chemicals. The extent of PLD stimulation by various MP‐Bs, as well as by digitonin and β‐escin, correlated with the permeability of the membrane to ethidium bromide. These results suggest that the stimulation of PLD activity by MP‐B in L1210 cells is probably coupled with membrane perturbation brought about by the peptide.