Ca2+-independent interaction of annexin I with phospholipid monolayers.
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.
Rosengarth
A
A
Institut für Medizinische Biochemie, Münster, Germany.
Wintergalen
A
A
Galla
H J
HJ
Hinz
H J
HJ
Gerke
V
V
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry*; D000818:Animals; D017305:Annexin A1 / Q000737:chemistry* / Q000378:metabolism; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008081:Liposomes / Q000737:chemistry*; D010718:Phosphatidylserines / Q000737:chemistry*; D011312:Pressure; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013499:Surface Properties; D013552:Swine
D017305:Annexin A1; D008081:Liposomes; D010718:Phosphatidylserines; D011994:Recombinant Proteins; D015060:1,2-Dipalmitoylphosphatidylcholine; C038694:dipalmitoylphosphatidylserine; D002118:Calcium