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Serum Amyloid A (SAA) is an acute phase protein complex consisting of several abundant isoforms. The N- terminus of SAA is critical to its function in amyloid formation. SAA is frequently truncated, either missing an arginine or an arginine-serine dipeptide, resulting in isoforms that may influence the capacity to form amyloid. However, the relative abundance of truncated SAA in diabetes and chronic kidney disease is not known.
Methods: Using mass spectrometric immunoassay, the abundance of SAA truncations relative to the native variants was examined in plasma of 91 participants with type 2 diabetes and chronic kidney disease and 69 participants without diabetes.
Results: The ratio of SAA 1.1 (missing N-terminal arginine) to native SAA 1.1 was lower in diabetics compared to non-diabetics (p = 0.004), and in males compared to females (p<0.001). This ratio was negatively correlated with glycated hemoglobin (r = −0.32, p<0.001) and triglyceride concentrations (r = −0.37, p<0.001), and positively correlated with HDL cholesterol concentrations (r = 0.32, p<0.001).
Conclusion: The relative abundance of the N-terminal arginine truncation of SAA1.1 is significantly decreased in diabetes and negatively correlates with measures of glycemic and lipid control.
- Yassine, Hussein N. (Author)
- Trenchevska, Olgica (Author)
- He, Huijuan (Author)
- Borges, Chad (Author)
- Nedelkov, Dobrin (Author)
- Mack, Wendy (Author)
- Kono, Naoko (Author)
- Koska, Juraj (Author)
- Reaven, Peter D. (Author)
- Nelson, Randall (Author)
- Biodesign Institute (Contributor)
Yassine, H. N., Trenchevska, O., He, H., Borges, C. R., Nedelkov, D., Mack, W., . . . Nelson, R. W. (2015). Serum Amyloid A Truncations in Type 2 Diabetes Mellitus. Plos One, 10(1). doi:10.1371/journal.pone.0115320
- 2017-04-14 02:14:17
- 2021-12-09 03:39:51
- 2 years 11 months ago