Formation of Two-dimensional Arrays of Annexin V on Phosphatidylserine-containing Liposomes

Pigault, Claire; Follenius-Wund, Anny; Schmutz, Marc; Freyssinet, Jean‐Marie; Brisson, Alain

doi:10.1006/jmbi.1994.1129

Cited by 135 publications

(96 citation statements)

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“…One annexin V molecule can cover an area of membrane corresponding to as many as fifty phospholipid molecules 16,24,25 and, due to the formation of arrays, eight annexin V molecules can bind per PS residue. 16,26 Therefore, inhibition of phagocytosis by annexin V could be the result of steric hindrance to access of other recognition molecules or to non-specific inhibition of phagocytosis. To test this possibility, Fc receptormediated phagocytosis was measured in the presence of annexin V. Erythrocytes were pretreated with anti-glycophorin antibody and their phagocytosis by both activated and unactivated macrophages was measured.…”

Section: Resultsmentioning

confidence: 99%

Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages

et al. 1999

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Although different macrophages exploit different cell surface receptors to recognize apoptotic lymphocytes, indirect evidence suggested that the phosphatidylserine (PS) that appears on the surface of lymphocytes undergoing apoptosis participates in specific recognition by all types of macrophages. To test this possibility directly, annexin V, a protein that specifically binds to PS, was used to mask this phospholipid on the apoptotic cell surface. Preincubation of apoptotic lymphocytes with annexin V blocked phagocytosis by elicited mouse peritoneal macrophages, macrophages of the mouse J774 cell line and mouse bone marrow macrophages. Similarly, annexin V was able to inhibit phagocytosis of lipid-symmetric erythrocytes, another target cell upon which PS is exposed. Together these results demonstrate directly that macrophages of all types depend on the PS exposed on the surface of apoptotic lymphocytes for recognition and phagocytosis.

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Section: Resultsmentioning

confidence: 99%

Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages

et al. 1999

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“…As previously discussed, annexin V binds to PS with a very low K d and is unlikely to be displaced by the virus. Furthermore, the area of the phospholipid head of PS is 0.7 nm 2 compared to an annexin V molecule at 25.5 nm 2 , so one annexin V molecule is thought to cover an area of the plasma membrane containing 35 lipid molecules (22). Therefore, we feel confident that when cells are treated with a saturating concentration of annexin V, no other large compound, especially a bulky VSV virion, can access the PS in the cell membrane.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidylserine Is Not the Cell Surface Receptor for Vesicular Stomatitis Virus

Coil

Miller²

2004

J Virol

149

109

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The envelope protein from vesicular stomatitis virus (VSV) has become an important tool for gene transfer and gene therapy. It is widely used mainly because of its ability to mediate virus entry into all cell types tested to date. Consistent with the broad tropism of the virus, the receptor for VSV is thought to be a ubiquitous membrane lipid, phosphatidylserine (PS). However, the evidence for this hypothesis is indirect and incomplete. Here, we have examined the potential interaction of VSV and PS at the plasma membrane in more detail. Measurements of cell surface levels of PS show a wide range across cell types from different organisms. We demonstrate that there is no correlation between the cell surface PS levels and VSV infection or binding. We also demonstrate that an excess of annexin V, which binds specifically and tightly to PS, does not inhibit infection or binding by VSV. While the addition of PS to cells does allow increased virus entry, we show that this effect is not specific to the VSV envelope. We conclude that PS is not the cell surface receptor for VSV, although it may be involved in a postbinding step of virus entry.

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“…Regardless of the site of action, i.e., the cytoplasmic or exoplasmic leaflets of cell membranes, the mechanistic basis of annexin A5 activity is mostly linked to its ability to form two-dimensional crystals on planar lipid bilayers. This has been demonstrated by electron and atomic force microscopic studies in situ (6,55,64,65) and could be the basis of a protective annexin A5 shield on syncytiotrophoblasts, which can be disrupted by antiphospholipid antibodies (58).…”

Section: Annexin A5mentioning

confidence: 89%

Expression and functions of annexins in the kidney

Markoff¹,

Gerke²

2005

American Journal of Physiology-Renal Physiology

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This review article summarizes current knowledge about the locations and possible functions of annexin family members in the kidney. Beginning with an introduction on common structural and biochemical features as well as general functional characteristics of annexins, the paper focuses on individual members with documented and/or proposed physiological relevance for renal development, structure, and functions. Three main aspects of annexin function in kidney epithelia emerge from the available experimental data. First, annexins are required for membrane organization and membrane transport events required for the establishment/maintenance of epithelial polarity. Second, there is accumulating evidence of an association of annexins with ion channels, as membrane-guiding auxiliary proteins or modulators of channel activity. Last but not least, some annexins seem to work as extracellular autocrine modulators of receptor function under different physiological conditions.

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Formation of Two-dimensional Arrays of Annexin V on Phosphatidylserine-containing Liposomes

Cited by 135 publications

References 0 publications

Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages

Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages

Phosphatidylserine Is Not the Cell Surface Receptor for Vesicular Stomatitis Virus

Expression and functions of annexins in the kidney

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