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Annexin V forms calcium-dependent trimeric units on phospholipid vesicles.
N O Concha1, J F Head, M A Kaetzel
1Department of Physiology, Boston University School of Medicine, MA 02118-2394.
FEBS Letters
|December 14, 1992
Summary
Calcium triggers annexin V (a phospholipid-binding protein) to form aggregates on membranes. This oligomerization, crucial for annexin-vesicle binding, may alter cell membrane properties.
Area of Science:
- Biochemistry
- Cell Biology
- Structural Biology
Background:
- Annexin V is a calcium-dependent phospholipid-binding protein.
- Its quaternary structure and function in cellular processes are not fully understood.
Purpose of the Study:
- To investigate the quaternary structure of annexin V.
- To understand the conditions and mechanisms of annexin V oligomerization.
Main Methods:
- Chemical cross-linking was employed to study annexin V structure.
- Experiments were conducted in the presence and absence of calcium and anionic phospholipids.
Main Results:
- Calcium induced the formation of trimers, hexamers, and higher aggregates of annexin V.
- Oligomerization was dependent on the presence of anionic phospholipids.
- Annexin V aggregation occurred under conditions similar to annexin-vesicle binding.
Conclusions:
- A model is proposed where cell stimulation induces calcium-dependent organization of annexin V arrays on the inner membrane surface.
- This organization may alter membrane properties like permeability and fluidity.