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Lupus. 1995 Feb;4 Suppl 1:S3-5.

Structure and function of beta 2-glycoprotein I: with special reference to the interaction with phospholipid.

Author information

1
Faculty of Science, University of Osaka, Toyonaka, Japan.

Abstract

beta 2-Glycoprotein I (beta 2-GPI) is a cofactor in the recognition of a phospholipid antigen, cardiolipin, by anticardiolipin antibodies in autoimmune diseases such as systemic lupus erythematosus. We examined the interaction of various forms of bovine beta 2-GPI, such as its intact form, desialylated form (Asialo beta 2-GPI), N-terminal domain (domain I) and the modified forms of beta 2-GPI and Asialo beta 2-GPI with nicks in their C-terminal domains (domain 5), with phospholipid liposomes under different conditions of pH and ionic strength. We found that at neutral pH and low ionic strength beta 2-GPI bound to liposome membranes containing cardiolipin with a dissociation constant (Kd) of 10(-8) M. Phosphatidylglycerol, phosphatidylserine, phosphatidic acid or phosphatidylinositol bound to beta 2-GPI, but phosphatidylcholine did not. We also found that domain I and Asialo beta 2-GPI bound to cardiolipin with Kd values of 10(-6) and 10(-8) M, respectively. At neutral pH and both low and high ionic strengths, the affinities of nicked forms of beta 2-GPI and Asialo beta 2-GPI for cardiolipin were lower than those of intact forms but similar to that of domain 1.

PMID:
7757108
DOI:
10.1177/096120339400400102
[Indexed for MEDLINE]

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