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J Biol Chem, Vol. 274, Issue 11, 7172-7181, March 12, 1999
From the Department of Pathology, Queen's University and the Syl
and Molly Apps Research Center, Kingston General Hospital,
Kingston, Ontario K7L 3N6, Canada
Serum amyloid A isoforms, apoSAA1
and apoSAA2, are apolipoproteins of unknown function that become major
components of high density lipoprotein (HDL) during the acute phase of
an inflammatory response. ApoSAA is also the precursor of
inflammation-associated amyloid, and there is strong evidence that the
formation of inflammation-associated and other types of amyloid is
promoted by heparan sulfate (HS). Data presented herein demonstrate
that both mouse and human apoSAA contain binding sites that are
specific for heparin and HS, with no binding for the other major
glycosaminoglycans detected. Cyanogen bromide-generated peptides of
mouse apoSAA1 and apoSAA2 were screened for heparin binding activity.
Two peptides, an apoSAA1-derived 80-mer (residues 24-103) and a
smaller carboxyl-terminal 27-mer peptide of apoSAA2 (residues 77-103),
were retained by a heparin column. A synthetic peptide corresponding to
the CNBr-generated 27-mer also bound heparin, and by substituting or
deleting one or more of its six basic residues (Arg-83, His-84, Arg-86,
Lys-89, Arg-95, and Lys-102), their relative importance for heparin and HS binding was determined. The Lys-102 residue appeared to be required
only for HS binding. The residues Arg-86, Lys-89, Arg-95, and Lys-102
are phylogenetically conserved suggesting that the heparin/HS binding
activity may be an important aspect of the function of apoSAA. HS
linked by its carboxyl groups to an Affi-Gel column or treated with
carbodiimide to block its carboxyl groups lost the ability to bind
apoSAA. HDL-apoSAA did not bind to heparin; however, it did bind to HS,
an interaction to which apoA-I contributed. Results from binding
experiments with Congo Red-Sepharose 4B columns support the conclusions
of a recent structural study which found that heparin binding domains
have a common spatial distance of about 20 Å between their two outer
basic residues. Our present work provides direct evidence that apoSAA
can associate with HS (and heparin) and that the occupation of its
binding site by HS, and HS analogs, likely caused the previously
reported increase in amyloidogenic conformation (
-sheet) of apoSAA2
(McCubbin, W. D., Kay, C. M., Narindrasorasak, S., and
Kisilevsky, R. (1988) Biochem. J. 256, 775-783) and their
amyloid-suppressing effects in vivo (Kisilevsky, R.,
Lemieux, L. J., Fraser, P. E., Kong, X., Hultin, P. G.,
and Szarek, W. A. (1995) Nat. Med. 1, 143-147), respectively.
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