Serum Levels and Glycosylation Changes of Alpha-1-Acid Glycoprotein According to Severity of Breast Cancer in Korean Women
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Elevated serum levels of alpha-1-acid glycoprotein (AGP) are known to be associated with several types of cancer. In addition, some reports have indicated that changes in glycosylation of AGP are associated with cancer progression. However, changes in AGP levels of serum and changes in glycosylation of AGPs in breast cancer have not been specifically studied. In the present study, serum AGP levels in benign (BN) cancer and breast cancer stage I (BC I), BC IIA, BC IIB, and BC III in Korean women were measured using an enzyme-linked immunosorbent assay (ELISA). AGP was purified from individual sera by hot phenol extraction and then subjected to AGP glycosylation analysis. Three types of AGP glycosylation (fucosylation, high-mannose-type and sialylation) were detected using enzyme-linked lectin assays (ELLAs). Serum AGP levels were higher in BC I, BC IIA, BC IIB, and BC III, than in the BN group, and the level in BC I and BC IIA was high enough to be distinguished from BN. Meanwhile, terminal fucosylation and high-mannose-type glycans appeared to be lowest in BC I. The glycosylation levels of BC I provide sensitivity and specificity that make BC I clearly distinguishable from BC IIA, BC IIB, and BC III as well as BN. Therefore, determination of serum AGP or AGP glycosylation level could be useful for detecting the early stages of breast cancer.
Abstract
Elevated serum levels of alpha-1-acid glycoprotein (AGP) are known to be associated with several types of cancer. In addition, some reports have indicated that changes in glycosylation of AGP are associated with cancer progression. However, changes in AGP levels of serum and changes in glycosylation of AGPs in breast cancer have not been specifically studied. In the present study, serum AGP levels in benign (BN) cancer and breast cancer stage I (BC I), BC IIA, BC IIB, and BC III in Korean women were measured using an enzyme-linked immunosorbent assay (ELISA). AGP was purified from individual sera by hot phenol extraction and then subjected to AGP glycosylation analysis. Three types of AGP glycosylation (fucosylation, high-mannose-type and sialylation) were detected using enzyme-linked lectin assays (ELLAs). Serum AGP levels were higher in BC I, BC IIA, BC IIB, and BC III, than in the BN group, and the level in BC I and BC IIA was high enough to be distinguished from BN. Meanwhile, terminal fucosylation and high-mannose-type glycans appeared to be lowest in BC I. The glycosylation levels of BC I provide sensitivity and specificity that make BC I clearly distinguishable from BC IIA, BC IIB, and BC III as well as BN. Therefore, determination of serum AGP or AGP glycosylation level could be useful for detecting the early stages of breast cancer.
참고문헌 (35)
- Heegaard PM, "Pig alpha1-acid glycoprotein : characterization and first description in any species as a negative acute phase protein", PLoS One, 8, pp.e68110~ (2013)
- Schmid K, "The carbohydrate units of human plasma alpha1-acid glycoprotein", Biochim. Biophys. Acta, 492, pp.291~302 (1977)
- Hochepied T, "Alpha(1)-acid glycoprotein : an acute phase protein with inflammatory and immunomodulating properties", Cytokine Growth Factor Rev, 14, pp.25~34 (2003)
- Bteich M, "An overview of albumin and alpha-1-acid glycoprotein main characteristics : highlighting the roles of amino acids in binding kinetics and molecular interactions", Heliyon, 5, pp.e02879~ (2019)
- Kwon H, "Adipokines mediate inflammation and insulin resistance", Front. Endocrinol. (Lausanne), 4, pp.71~ (2013)
- Lumeng CN, "Inflammatory links between obesity and metabolic disease", J. Clin. Invest, 121, pp.2111~2117 (2011)
- Bachtiar I, "Combination of alpha-1-acid glycoprotein and alpha-fetoprotein as an improved diagnostic tool for hepatocellular carcinoma", Clin. Chim. Acta, 399, pp.97~101 (2009)
- Ohbatake Y, "Elevated alpha1-acid glycoprotein in gastric cancer patients inhibits the anticancer effects of paclitaxel, effects restored by co-administration of erythromycin", Clin. Exp. Med, 16, pp.585~592 (2016)
- Katnik I, "Microheterogeneity of alpha 1-acid glycoprotein in the sera of patients with cancer or inflammatory states of the ovaries", Arch. Immunol. Ther. Exp. (Warsz), 36, pp.1~6 (1988)
- Piver MS, "Serum alpha 1-acid glycoprotein in epithelial ovarian cancer", Gynecol. Oncol, 29, pp.305~308 (1988)
- Fernandes CL, "Structural glycobiology of human alpha1-acid glycoprotein and its implications for pharmacokinetics and inflammation", Glycobiology, 25, pp.1125~1133 (2015)
- Nakano M, "Detailed structural features of glycan chains derived from alpha1-acid glycoproteins of several different animals : the presence of hypersialylated, O-acetylated sialic acids but not disialyl residues", Glycobiology, 14, pp.431~441 (2004)
- Zhang D, "Glycosylation change of alpha-1-acid glycoprotein as a serum biomarker for hepatocellular carcinoma and cirrhosis", Biomark. Med, 11, pp.423~430 (2017)
- Hashimoto S, "alpha1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis", Cancer, 101, pp.2825~2836 (2004)
- Balmana M, "Increased alpha1-3 fucosylation of alpha-1-acid glycoprotein(AGP)in pancreatic cancer", J. Proteomics, 132, pp.144~154 (2016)
- Yazawa S, "Fucosylated glycans in alpha1-acid glycoprotein for monitoring treatment outcomes and prognosis of cancer patients", PLoS One, 11, pp.e0156277~ (2016)
- "Breast cancer" (2019)[URL]
- Youlden DR, "Incidence and mortality of female breast cancer in the Asia-Pacific region", Cancer Biol. Med, 11, pp.101~115 (2014)
- Harris L, "American society of clinical oncology 2007 update of recommendations for the use of tumor markers in breast cancer", J. Clin. Oncol, 25, pp.5287~5312 (2007)
- Saldova R, "Association of N-glycosylation with breast carcinoma and systemic features using high-resolution quantitative UPLC", J. Proteome Res, 13, pp.2314~2327 (2014)
- Chan J, "One-step isolation of alpha 1-acid glycoprotein", Protein Exp. Purif, 2, pp.34~36 (1991)
- Kim HJ, "The choice of resin-bound ligand affects the structure and immunogenicity of columnpurified human papillomavirus type 16 virus-like particles", PLoS One, 7, pp.e35893~ (2012)
- Min-Hye Park, "IgG and IgM responses to human papillomavirus L1 virus-like particle as a function of dosing schedule and vaccine formulation", The Journal of Microbiology, 57(9), pp.821~827 (2019), 한국미생물학회[DOI]
- Giuliano AE, "Breast cancer-major changes in the American Joint Committee on Cancer eighth edition cancer staging manual", CA. Cancer J. Clin, 67, pp.290~303 (2017)
- Durham M, "Targeted glycoproteomics : serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome", J. Chromatogr. A, 1132, pp.165~173 (2006)
- Choi JW, "Use of CA153 for screening breast cancer : An antibodylectin sandwich assay for detecting glycosylation of CA153 in sera", Oncol. Rep, 40, pp.145~154 (2018)
- Stowell SR, "Protein glycosylation in cancer", Annu. Rev. Pathol, 10, pp.473~510 (2015)
- Hulsmeier AJ, "N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry", Mol. Cell Proteomics, 6, pp.2132~2138 (2007)
- Lee CS, "Unmasking heavily O-Glycosylated serum proteins using perchloric acid : identification of serum proteoglycan 4 and protease C1 inhibitor as molecular indicators for screening of breast cancer", PLoS One, 11, pp.e0149551~ (2016)
- Kremer JM, "Drug binding to human alpha-1-acid glycoprotein in health and disease", Pharmacol. Rev, 40, pp.1~47 (1988)
- McCurdy TR, "Comparison of methods for the purification of alpha-1 acid glycoprotein from human plasma", J. Biomed. Biotechnol, 2011, pp.578207~ (2011)
- Mackiewicz A, "Glycoforms of serum alpha 1-acid glycoprotein as markers of inflammation and cancer", Glycoconj. J, 12, pp.241~247 (1995)
- Pos O, "Con A-nonreactive human alpha 1-acid glycoprotein(AGP)is more effective in modulation of lymphocyte proliferation than Con A-reactive AGP serum variants", Inflammation, 14, pp.133~141 (1990)
- Shiyan SD, "Carbohydrate composition and immunomodulatory activity of different glycoforms of alpha1-acid glycoprotein", Glycoconj. J, 14, pp.631~638 (1997)
- Bories PN, "Human alpha 1-acid glycoprotein-exposed macrophages release interleukin 1 inhibitory activity", Biochem. Biophys. Res. Commun, 147, pp.710~715 (1987)