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Ca 2+ ‐independent interaction of annexin I with phospholipid monolayers
Author(s) -
Rosengarth Anja,
Wintergalen Andreas,
Galla Hans-Joachim,
Hinz Hans-Jürgen,
Gerke Volker
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)01318-0
Subject(s) - monolayer , chemistry , phospholipid , dipalmitoylphosphatidylcholine , annexin , annexin a2 , ion , surface pressure , penetration (warfare) , phosphatidylserine , analytical chemistry (journal) , crystallography , chromatography , biochemistry , phosphatidylcholine , organic chemistry , membrane , physics , operations research , mechanics , engineering , cell
At pH 6.0, the interaction of annexin I, a proteolytic fragment of annexin I and annexin V, was studied with monolayers composed of dipalmitoylphosphatidylserine (DPPS), dipalmitoylphosphatidylcholine (DPPC) or DPPS/DPPC mixtures (molar ratio 1:4). The measurements reveal that only annexin I shows a significant increase in the surface pressure at constant surface area in the absence of Ca 2+ ions. We interpret these pressure changes as reflecting penetration of the protein. Kinetic analyses of the annexin I/monolayer interaction at pH 6.0 in the presence and absence of Ca 2+ ions show differences between the interaction mechanisms that support the occurrence of a pH‐regulated process. At pH 7.4, Ca 2+ ions are required for the interaction.