Abstract
Our results confirm the presence of N-glycosylation of hm-apoA1 in patients with AMI, as described by Cubedo et al. The results further show that these N-glycosylated hm-apoA1 can be detected in other cardiovascular diseases (UAP and SAP) and in healthy donors.
However, we have also found that N-glycosylated hm-apoA1 patterns vary among the different groups, in particular, between the acute coronary syndrome patients (AMI and UAP) compared with the SAP patients and the control group. This difference is very likely related to the qualitative properties of hm-apoA1, that is, to the site(s) of glycosylation and to the carbohydrate chains' composition.
We are confident that these observations will be very important and should be followed up by precise hm-apoA1 characterization and validation.