Abstract: The annexin family of proteins, first recognized in 1990, consists of several hundred different annexins, which include 10 in mammalian cells, and the remainder in other organisms including a wide range of plants. Their canonical structure consists of repetitive homologous domains of about 70 amino acids, with almost all of the annexins having four of these domains. Annexin-V is a potent anticoagulant protein whose activity is a consequence of its high affinity for the anionic phospholipids and the inhibition of phospholipid-dependent coagulation reactions. Interference with annexin-V function, either by autoantibody-mediated recognition of the protein itself or by competition of antibodies against phospholipids (aPL)-cofactor antibodies for the phospholipid surface, have been proposed and investigated as potential mechanisms for thrombosis in the APS. Annexin-V appears to play a thrombomodulatory role in the placental circulation where it is necessary for the maintenance of placental integrity. Some patients with the APS have the evidence for the antibodies that specifically recognize annexin-V and other annexins. The presence of antibodies against annexin-V has been reported to be increased in patients with recurrent miscarriages. Since both aPL and annexin-V have affinity for anionic phospholipids, it was hypothesized that the aPL antibodies, without anti-annexin-V specificities, might interfere with the assembly of the antithrombotic annexin-V shield over phospholipids on the apical cytoplasmic membranes.
Publication Year: 2002
Publication Date: 2002-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 2
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