Apolipoprotein H Is Not Affected by In Vitro Glycosylation |
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Authors: | Roberto Gambino Gianluca Ruiu Gianfranco Pagano Maurizio Cassader |
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Affiliation: | (1) Dipartimento di Medicina Interna, Universita' di Torino, 10126 Torino, Italy;(2) Laboratorio Centrale Baldi e Riberi,, Azienda Ospedaliera S. Giovanni Battista, Torino, Italy |
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Abstract: | Increased nonenzymatic glycosylation of all major classes of apolipoproteins has been demonstrated in diabetes. In this work we deal with the in vitro nonenzymatic glycosylation of apolipoprotein H, whose role in lipid metabolism is still poorly understood and whose levels increase in diabetes. Apolipoprotein H was isolated from human plasma and purified through a combination of affinity chromatography and continuous elution electrophoresis. The in vitro glycosylation was performed by incubating purified apolipoprotein H with high concentration of glucose. Our results indicate that the in vitro nonenzymatic glycosylation has no effect on the physical properties of apolipoprotein H, despite the fact that this apolipoprotein contains a high number of lysine residues. Since the in vitro concentration of glucose was far higher than the levels normally found in diabetic subjects, it is unlikely for apolipoprotein H to become glycosylated in diabetes. |
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Keywords: | Apolipoprotein H nonenzymatic glycosylation affinity chromatography diabetes mellitus |
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