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PMID:1903064
| Citation |
James, RW, Hochstrasser, AC, Borghini, I, Martin, B, Pometta, D and Hochstrasser, D Characterization of a human high density lipoprotein-associated protein, NA1/NA2. Identity with SP-40,40, an inhibitor of complement-mediated cytolysis. Arterioscler. Thromb. 11:645-52 |
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| Abstract |
Two peptides, NA1 and NA2, which we previously suggested to be associated with high density lipoproteins (HDLs), have been purified. Polyclonal antibodies against each peptide and a monoclonal antibody against NA2 have been used to further characterize them and their association with HDL. Immunoblotting studies revealed that the peptides form a complex of molecular mass of approximately 80 kd. Agarose gel filtration showed coelution of NA1/NA2 and apolipoprotein (apo) A-I, the structural protein of HDL. This was confirmed by fast protein liquid chromatography, which further indicated that up to 60% of NA1/NA2 was located within the lower density range of the HDL spectrum. Complementary studies with anti-apo A-I immunoaffinity columns provided evidence that at least 40% of NA1/NA2 was associated with HDL, an association easily disrupted by ultracentrifugal manipulation. Finally, partial amino acid sequences showed virtually complete homology with a recently identified protein, SP-40,40, or cytolysis inhibitor. The protein is suggested to have a powerful inhibitory effect on complement-mediated cell lysis. Our results could thus furnish an explanation for the previously observed modulating influence of HDL on complement activity. |
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| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Apolipoprotein A-I; Apolipoproteins A/immunology; Blood Proteins/chemistry; Blood Proteins/isolation & purification; Chromatography, Affinity; Chromatography, Gel; Clusterin; Glycoproteins; Humans; Immunoassay; Immunoblotting; Lipoproteins, HDL/analysis; Molecular Chaperones; Molecular Sequence Data; Molecular Weight; Sequence Homology, Nucleic Acid |
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