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Membrane interactions of mastoparan analogues related to their differential effects on protein kinase C, Na,K‐ATPase and HL60 cells
Author(s) -
Raynor Robert L.,
Kim Young-Sook,
Zheng Bin,
Vogler William R.,
Kuo J.F.
Publication year - 1992
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 - 10.1016/0014-5793(92)80694-c
Subject(s) - mastoparan , protein kinase c , membrane , phosphatidylserine , chemistry , hl60 , biochemistry , protein kinase a , axolemma , enzyme , microbiology and biotechnology , biology , g protein , signal transduction , cell , central nervous system , phospholipid , myelin , neuroscience
Membrane interactions of tetradecapeptide toxin mastoparan (MP) and analogues (MP‐3, MP‐X and polistes MP), as indicated by inhibition of various enzymatic and cellular activities, were investigated. MP‐3 was found to be the least active in inhibiting protein kinase C (PKC; activated by phosphatidylserine vesicles, synaptosomal membranes or phorbol ester), synaptosomal membrane Na.K‐ATPase and proliferation and viability or leukemia HL60 cells. MP‐3, however, was as active as others in inhibiting PKC activated by arachidonate monomers and phorbol ester binding. The unique properties or MP‐3, the [des‐lle‐Asn 2 ]‐ analogue or MP, might be related to its low functional amphiphilicity compared to others and useful in further delineating biological activities associated with or regulated by membranes.