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Expression, location and cross-reactivity of two antigenic sites on the amino terminal region of rabbit and human apolipoprotein A-I.

Abstract：

:Rabbit apolipoprotein A-I (apo A-I) of molecular weight 27,612 contained 241 amino acids. In contrast to its human counterpart which has 3 methionine residues, the rabbit protein possesses only one and therefore produces 2 fragments after CNBr cleavage (CNBr I and II, NH2- and COOH-terminal, respectively). From a series of monoclonal antibodies raised against human apo A-I, 2 (A05 and A16) cross-reacted with rabbit apo A-I. In the present study, we show that A05 recognizes the rabbit CNBr I fragment while the integrity of the intermediate region between the 2 CNBr fragments (including the methionine residue) is required for the expression of the A16 antigenic determinant. Competition experiments were performed between human 125I-labelled high density lipoprotein (HDL) and a variety of preparations of human and rabbit apo A-I (including the purified and delipidated protein, complexes of dimyristoylphosphatidylcholine (DMPC) containing apo A-I, HDL subfractions and whole serum). The A05 antigenic determinant was expressed identically in all these fractions of both species. In contrast the A16 showed poor reactivity with delipidated apo A-I, the apparent affinity constant being about 100 times less than for HDL. These data suggest that phospholipids improve the recognition of apo A-I by the A16 antibody. The similar immunoreactivity of the human and rabbit proteins in the present study is consistent with the view that the NH2-terminal region contains the major portion activating lecithin:cholesterol acyltransferase.

journal_name

Atherosclerosis

journal_title

Atherosclerosis

authors

Leroy A,Vu-Dac N,Theret N,Pio F,Fruchart JC

doi

10.1016/0021-9150(89)90028-2

subject

Has Abstract

pub_date

1989-09-01 00:00:00

pages

9-19

issue

1

eissn

0021-9150

issn

1879-1484

pii

0021-9150(89)90028-2

journal_volume

79

pub_type

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