Two-dimensional gel analysis of serum apolipoprotein A-I isoforms: preliminary analysis suggests altered ratios in individuals with heart disease.
Apolipoprotein A-I (apo A-I), the major protein component of high-density lipoprotein, is quantified in a number of ways, typically by immunochemical methods. Commercial tests do not discriminate among isoforms of apo A-I. Two-dimensional electrophoresis, however, segregates and differentiates these isoforms, primarily due to charge variations among the various species. Stained two-dimensional gels can be scanned using high-resolution laser densitometry, and the isoforms can then be quantified using image analysis software. Human sera from coronary heart disease (CHD) patients (n = 36) and sex-matched and close-age-matched individuals (n = 36) with no known CHD were analyzed, to determine the relative abundance for each isoform within a given serum. In this preliminary study, we observed statistically significant differences between the two groups, suggesting altered post-translational processing from the proapo A-I and mature apo A-I isoforms to their adjacent isoforms for patients with histories of heart disease. In two instances, the P values were less than 0.005; in two others, P values were less than 0.001.
Burgess-Cassler
A
A
Biopolymer Research Unit, National Center for Agricultural Utilization Research, USDA, Peoria, Illinois 61604-3999.
Johansen
J J
JJ
Kendrick
N C
NC
D000368:Aged; D016632:Apolipoprotein A-I / Q000378:metabolism*; D001054:Apolipoproteins A / Q000378:metabolism; D001797:Blood Protein Electrophoresis / Q000379:methods*; D003327:Coronary Disease / Q000097:blood*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D006801:Humans; D008875:Middle Aged; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D016632:Apolipoprotein A-I; D001054:Apolipoproteins A; D011498:Protein Precursors