Fetuins are blood glycoproteins manufactured in the liver and secreted into the bloodstream. These glycoproteins make up a large group of binding proteins which mediates the transit and presence of a myriad of substances in the blood stream. Serum albumin, which is the most abundant protein in adult animal plasma is best known as the representative of these carrier proteins. In bone homeostasis, it is the circulating glycoprotein that plays a critical role. It plays major roles also in prevention of vascular calcification, disruption of adipocyte function and impairment of insulin signaling. Even with its major role, it is highly dependable in preventing and/or amplifying of the above disease processes. Certain diseases have been associated with high levels of Fetuin A. Although low levels of it in the plasma assist potentially in the protective effect of artery calcification in non-Chronic Kidney Disease (CKD) patients, high levels of the glycoprotein are the greatest concern in patients at higher risk of cardiovascular disease (CVD) and diabetes. The range of serum fetuin A in healthy adults is between 0.4 and 1mg/ml serum. The most studied function of fetuin A is mediated by the D1 domain. But the domain that binds with insulin receptor is yet to be known. The B chain consists of 27 amino acid residues which are distributed unevenly among the charged and neutral portion. Fetuins are proteins highly expressed in the liver blood plasma. They bear post translational modifications in proteolytic processing, phosphorylation, complex glycosylation and sulfation. The precussors of Fetuin A in humans are single-chained to the mature circulating double-chain form. In septicaemia and bovine, human fetuin A is perceptible to further proteolytic cleavage. Since the discovery of Fetuin A as a glycoprotein that inhibits vascular calcification in early 1990s, the biologic attributed roles has increased and still increasing exponentially. Apart from the roles it plays in type II diabetes mellitus and cardiovascular disease, other roles have been noted. Other effects and roles of Fetuin A are still being researched on.
| DOI | 10.11648/j.ijbmr.20170506.12 |
| Published in | International Journal of Biomedical Materials Research (Volume 5, Issue 6, December 2017) |
| Page(s) | 72-77 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2024. Published by Science Publishing Group |
Fetuin A, Type II Diabetes Mellitus, Calcification, Atherosclerosis, Serum
| [1] | Fetuin [Internet]. [cited 2017 Oct 2]; Available from: https://en.wikipedia.org/wiki/Fetuin. |
| [2] | Spiro RG. ARTICLE : a Glycoprotein of Fetal Serum *. J Biol Chem 1960; 225 (10): 2860–2869. |
| [3] | Annie A, Peter W, Bane AA, Grandjean PW. The Role of Fetuin-A in Disease Processes Prevalent in Postmenopausal Women El papel de la fetuina A en los procesos de enfermedad prevalentes en mujeres posmenopáusicas. 2015; |
| [4] | Häusler M, Schäfer C, Osterwinter C, Jahnen-Dechent W. The physiologic development of fetuin-a serum concentrations in children. Pediatr Res 2009; 66 (6): 660–664. |
| [5] | Sindhu S, Akhter N, Shenouda S, Wilson A, Ahmad R. Plasma fetuin-A/α2-HS-glycoprotein correlates negatively with inflammatory cytokines, chemokines and activation biomarkers in individuals with type-2 diabetes. BMC Immunol [Internet] 2016; 17 (1): 33. Available from: http://bmcimmunol.biomedcentral.com/articles/10.1186/s12865-016-0171-y. |
| [6] | Sakwe AM, Koumangoye R, Goodwin SJ, Ochieng J. Fetuin-A (α2HS-glycoprotein) is a major serum adhesive protein that mediates growth signaling in breast tumor cells. J Biol Chem 2010; 285 (53): 41827–41835. |
| [7] | Neurath Hans. The Proteins: Composition, Structure, and Function. Volume III. Elsevier; 2012. |
| [8] | Spiro RG, Bhoyroo VD. Structure of the O-Glvcosidicallv Linked Carbohydrates of Fetuin. J Biol Chem 1974; 249 (18): 5704–5717. |
| [9] | Dabrowska AM, Tarach JS, Wojtysiak-Duma B, Duma D. Fetuin-A (AHSG) and its usefulness in clinical practice. Review of the literature. Biomed Pap 2015; 159 (3): 352–359. |
| [10] | Singh M, Sharma PK, Garg VK, Mondal SC, Singh AK, Kumar N. Role of fetuin-A in atherosclerosis associated with diabetic patients. J Pharm Pharmacol 2012; 64 (12): 1703–1706. |
| [11] | Eleni P., Despina S. P., Spiridon P. VSN. Role of fetuin A in the diagnosis and treatment of joint arthritis. World J Orthop [Internet] 2017; 8 (6): 461–464. Available from: https://www.wjgnet.com/2218-5836/full/v8/i6/WJO-8-461-g001.htm. |
| [12] | Jahnen-Dechent W, Heiss A, Schäfer C, Ketteler M. Fetuin-A regulation of calcified matrix metabolism. Circ Res 2011; 108 (12): 1494–1509. |
| [13] | Wang H, Sama AE. Anti-inflammatory role of fetuin-A in injury and infection. Curr Mol Med [Internet] 2012; 12 (5): 625–33. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3349766&tool=pmcentrez&rendertype=abstract. |
| [14] | Ix JH, Wassel-fyr C, Kanaya A, et al. NIH Public Access. 2009; 300 (2): 182–188. |
| [15] | Anton-Scott Goustin ABA-S. The “thrifty” gene encoding Ahsg/Fetuin-A meets the insulin receptor: Insights into the mechanism of insulin resistance. Cell Signal [Internet] 2011; 23 (6): 980–990. Available from: http://www.sciencedirect.com/science/article/pii/S0898656810003153?via%3Dihub. |
| [16] | Rochette C. N, Rosenfeldt S., Heiss A, Narayanan T, Ballauff M J-DW. A shielding topology stabilizes the early stage protein-mineral complexes of fetuin-A and calcium phosphate: a time-resolved small-angle X-ray study. Chembiochem An Eur J Chem Biol 2009; 10 (4): 735–740. |
| [17] | Sun Q, Cornelis MC, Manson JE, Hu FB. Plasma levels of fetuin-A and hepatic enzymes and risk of type 2 diabetes in women in the U.S. Diabetes 2013; 62 (1): 49–55. |
| [18] | Mathews ST, Singh GP, Ranalletta M, et al. Improved insulin sensitivity and resistance to weight gain in mice null for the Ahsg gene. Diabetes 2002; 51 (8): 2450–2458. |
| [19] | Laughlin GA, Barrett-Connor E, Cummins KM, Daniels LB, Wassel CL, Ix JH. Sex-specific association of fetuin-a with type 2 diabetes in older community-dwelling adults: The Rancho Bernardo study. Diabetes Care 2013; 36 (7): 1994–2000. |
| [20] | Stefan N, Fritsche A, Weikert C, Boeing H, Joost H, Schulze MB. Plasma Fetuin-A Levels and the Risk of Type 2 Diabetes. Diabetes 2008; 57 (10): 2762–2767. |
| [21] | Baumann M, Richart T, Sollinger D, et al. Association between carotid diameter and the advanced glycation end product N-epsilon-carboxymethyllysine (CML). Cardiovasc Diabetol [Internet] 2009; 8: 45. Available from: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19660101%5Cnhttp://www.cardiab.com/content/pdf/1475-2840-8-45.pdf. |
| [22] | Ahmed L, Khalaa MA-E, Mohamed NE-G, Mousa S, Yousry Z. Fetuin-A and type II diabetes mellitus. Egypt J Intern Med [Internet] 2014; 26 (4): 157. Available from: http://www.esim.eg.net/text.asp?2014/26/4/157/148140. |
| [23] | Song A, Xu M, Bi Y, et al. Serum fetuin-A associates with type 2 diabetes and insulin resistance in Chinese adults. PLoS One 2011; 6 (4). |
| [24] | Vörös K, Cseh K, Kalabay L. The role of fetuin-A in cardiovascular diseases. Orv Hetil [Internet] 2014; 155 (1): 16–23. Available from: http://www.akademiai.com/doi/abs/10.1556/OH.2014.29793. |
| [25] | Chen HY, Lin CC, Chiu YL, et al. Serum fetuin A and chemerin levels correlate with hepatic steatosis and regional adiposity in maintenance hemodialysis patients. PLoS One 2012; 7 (7): 1–9. |
| [26] | Laughlin GA, Cummins KM, Wassel CL, Daniels LB, Ix JH. The association of fetuin-A with cardiovascular disease mortality in older community-dwelling adults: The Rancho Bernardo study. J Am Coll Cardiol 2012; 59 (19): 1688–1696. |
| [27] | Aroner SA, St-Jules DE, Mukamal KJ, et al. Fetuin-A, glycemic status, and risk of cardiovascular disease: The Multi-Ethnic Study of Atherosclerosis. Atherosclerosis [Internet] 2016; 248: 224–229. Available from: http://dx.doi.org/10.1016/j.atherosclerosis.2016.03.029. |
APA Style
Chukwunonso Livinus Udeh. (2017). Fetuin-A: A Biomarker for Type II Diabetes Mellitus. International Journal of Biomedical Materials Research, 5(6), 72-77. https://doi.org/10.11648/j.ijbmr.20170506.12
ACS Style
Chukwunonso Livinus Udeh. Fetuin-A: A Biomarker for Type II Diabetes Mellitus. Int. J. Biomed. Mater. Res. 2017, 5(6), 72-77. doi: 10.11648/j.ijbmr.20170506.12
AMA Style
Chukwunonso Livinus Udeh. Fetuin-A: A Biomarker for Type II Diabetes Mellitus. Int J Biomed Mater Res. 2017;5(6):72-77. doi: 10.11648/j.ijbmr.20170506.12
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Download@article{10.11648/j.ijbmr.20170506.12,
author = {Chukwunonso Livinus Udeh},
title = {Fetuin-A: A Biomarker for Type II Diabetes Mellitus},
journal = {International Journal of Biomedical Materials Research},
volume = {5},
number = {6},
pages = {72-77},
doi = {10.11648/j.ijbmr.20170506.12},
url = {https://doi.org/10.11648/j.ijbmr.20170506.12},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijbmr.20170506.12},
abstract = {Fetuins are blood glycoproteins manufactured in the liver and secreted into the bloodstream. These glycoproteins make up a large group of binding proteins which mediates the transit and presence of a myriad of substances in the blood stream. Serum albumin, which is the most abundant protein in adult animal plasma is best known as the representative of these carrier proteins. In bone homeostasis, it is the circulating glycoprotein that plays a critical role. It plays major roles also in prevention of vascular calcification, disruption of adipocyte function and impairment of insulin signaling. Even with its major role, it is highly dependable in preventing and/or amplifying of the above disease processes. Certain diseases have been associated with high levels of Fetuin A. Although low levels of it in the plasma assist potentially in the protective effect of artery calcification in non-Chronic Kidney Disease (CKD) patients, high levels of the glycoprotein are the greatest concern in patients at higher risk of cardiovascular disease (CVD) and diabetes. The range of serum fetuin A in healthy adults is between 0.4 and 1mg/ml serum. The most studied function of fetuin A is mediated by the D1 domain. But the domain that binds with insulin receptor is yet to be known. The B chain consists of 27 amino acid residues which are distributed unevenly among the charged and neutral portion. Fetuins are proteins highly expressed in the liver blood plasma. They bear post translational modifications in proteolytic processing, phosphorylation, complex glycosylation and sulfation. The precussors of Fetuin A in humans are single-chained to the mature circulating double-chain form. In septicaemia and bovine, human fetuin A is perceptible to further proteolytic cleavage. Since the discovery of Fetuin A as a glycoprotein that inhibits vascular calcification in early 1990s, the biologic attributed roles has increased and still increasing exponentially. Apart from the roles it plays in type II diabetes mellitus and cardiovascular disease, other roles have been noted. Other effects and roles of Fetuin A are still being researched on.},
year = {2017}
}
TY - JOUR T1 - Fetuin-A: A Biomarker for Type II Diabetes Mellitus AU - Chukwunonso Livinus Udeh Y1 - 2017/12/27 PY - 2017 N1 - https://doi.org/10.11648/j.ijbmr.20170506.12 DO - 10.11648/j.ijbmr.20170506.12 T2 - International Journal of Biomedical Materials Research JF - International Journal of Biomedical Materials Research JO - International Journal of Biomedical Materials Research SP - 72 EP - 77 PB - Science Publishing Group SN - 2330-7579 UR - https://doi.org/10.11648/j.ijbmr.20170506.12 AB - Fetuins are blood glycoproteins manufactured in the liver and secreted into the bloodstream. These glycoproteins make up a large group of binding proteins which mediates the transit and presence of a myriad of substances in the blood stream. Serum albumin, which is the most abundant protein in adult animal plasma is best known as the representative of these carrier proteins. In bone homeostasis, it is the circulating glycoprotein that plays a critical role. It plays major roles also in prevention of vascular calcification, disruption of adipocyte function and impairment of insulin signaling. Even with its major role, it is highly dependable in preventing and/or amplifying of the above disease processes. Certain diseases have been associated with high levels of Fetuin A. Although low levels of it in the plasma assist potentially in the protective effect of artery calcification in non-Chronic Kidney Disease (CKD) patients, high levels of the glycoprotein are the greatest concern in patients at higher risk of cardiovascular disease (CVD) and diabetes. The range of serum fetuin A in healthy adults is between 0.4 and 1mg/ml serum. The most studied function of fetuin A is mediated by the D1 domain. But the domain that binds with insulin receptor is yet to be known. The B chain consists of 27 amino acid residues which are distributed unevenly among the charged and neutral portion. Fetuins are proteins highly expressed in the liver blood plasma. They bear post translational modifications in proteolytic processing, phosphorylation, complex glycosylation and sulfation. The precussors of Fetuin A in humans are single-chained to the mature circulating double-chain form. In septicaemia and bovine, human fetuin A is perceptible to further proteolytic cleavage. Since the discovery of Fetuin A as a glycoprotein that inhibits vascular calcification in early 1990s, the biologic attributed roles has increased and still increasing exponentially. Apart from the roles it plays in type II diabetes mellitus and cardiovascular disease, other roles have been noted. Other effects and roles of Fetuin A are still being researched on. VL - 5 IS - 6 ER -
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