We have recently purified and partially sequenced a
microfibrillar protein from human aortic adventitia (
aneurysm-associated antigenic
protein, 40 kDa [AAAP-40]) that is immunoreactive with
immunoglobulin (
IgG) from the wall of
abdominal aortic aneurysms (AAAs). It shares motifs with Ig kappa (which may act as a binding site for interaction with
integrins), cytomegalovirus (which may be a molecular mimic in the pathogenesis of AAA), and
vitronectin and the
fibrinogens. A cDNA library was constructed from the aortic adventitia of a AAA. The library was screened with either rabbit anti-
vitronectin antibody or rabbit anti-
fibrinogen antibody. Positive plaques were purified and expressed in a strain of Escherichia coli. The clone sequences were analyzed. The expressed
proteins were separated by SDS/PAGE and the immunoblots were probed with either AAA
IgG or anti-human Ig kappa antibody. Experimental cell lines, transfected with the clones (clones 1 and 5), synthesized
recombinant proteins (rAAAP-CL1 and rAAAP-CL5), detectable in Western immunoblots with AAA
IgG. A prediction of the tertiary structure resembles well-characterized
cell adhesion molecules. These findings suggest that there is a novel family of matrix
proteins that may use
immunoglobulin motifs as binding sites for cellular
integrins and that there are matrix
proteins in addition to
AAAP-40 that may serve as
autoantigens in the pathogenesis of AAA disease.