AGP (α1-acid glycoprotein) is an acute phase plasma protein synthesized by the liver. It functions to regulate the interaction between blood cells and endothelial cells, and together with haptoglobin and C reactive protein, it also mediates the extravasation of cells during infection and inflammation. Expression of AGP is induced by acute-phase stimulatory agents such as bacterial lipopolysaccharides. AGP has a high affinity, low capacity binding for basic drugs at physiological pH. In human plasma, AGP is found at levels of 0.5-1.4 mg/ml, though this is elevated during acute inflammation, and, as a result, levels of this protein can be used to diagnose inflammatory conditions. AGP-1 and AGP-2 contain five and six potential N-glycosylation sites, respectively. Abnormal expression of the APG-1 gene is linked to sarcoidosis and other immunogenetic diseases, while mutations in the APG-2 gene are associated with different types of carcinomas.
Background References
1. Fitos I et al. Selective binding of imatinib to the genetic variants of human alpha1-acid glycoprotein. Biochim Biophys Acta 1760:1704-1712 (2006).
2. Zsila F et al. The drug binding site of human alpha1-acid glycoprotein: insight from induced circular dichroism and electronic absorption spectra. Biochim Biophys Acta 1770:797-809 (2007).
Sequence Similarity
Belongs to the calycin superfamily. Lipocalin family.
Tissue Specificity
Expressed by the liver and secreted in plasma.
Post-translational Modification
N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).