Ca2+‐independent interaction of annexin I with phospholipid monolayers

FEBS Letters

Wintergalen, Andreas²  Gerke, Volker¹  Galla, Hans-Joachim²  Rosengarth, Anja¹  Hinz, Hans-Jürgen³ 

[1] Institut für Medizinische Biochemie, Von-Esmarch-Str. 56, 48149 Münster, Germany;Institut für Biochemie, Wilhelm-Klemm-Str. 2, 48149 Münster, Germany;Institut für Physikalische Chemie, Schloßplatz 4/7, 48149 Münster, Germany

关键词: Annexin I;    Calcium;    Phospholipid monolayer;    Surface pressure/area isotherm;    Protein penetration;    CD;    circular dichroism;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide gel electrophoresis;    ϵ280 nm;    molar extinction coefficient at 280 nm;    DPPS;    dipalmitoylphosphatidylserine;    DPPC;    dipalmitoylphosphatidylcholine;   

DOI  :  10.1016/S0014-5793(98)01318-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺ 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 Ca²⁺ ions show differences between the interaction mechanisms that support the occurrence of a pH-regulated process. At pH 7.4, Ca²⁺ ions are required for the interaction.

【 授权许可】

Unknown