486
Views
38
CrossRef citations to date
0
Altmetric
Review

Abundance matters: role of albumin in diabetes, a proteomics perspective

, , &
Pages 677-689 | Received 26 Feb 2017, Accepted 05 Jul 2017, Published online: 13 Jul 2017

References

  • Fanali G, di Masi A, Trezza V, et al. Human serum albumin: from bench to bedside. Mol Aspects Med. 2012;33:209–290.
  • Peters TJ. All about albumin: biochemistry, genetics, and medical applications. San Diego (CA): Academic Press; 1996.
  • Varshney A, Sen P, Ahmad E, et al. Ligand binding strategies of human serum albumin: how can the cargo be utilized? Chirality. 2010;22:77–87.
  • Lee P, Wu X. Review: modifications of human serum albumin and their binding effect. Curr Pharm Des. 2015;21:1862–1865.
  • Toyokuni S, Yamada S, Kashima M, et al. Serum 4-hydroxy-2-nonenal-modified albumin is elevated in patients with type 2 diabetes mellitus. Antioxid Redox Signal. 2000:681–685.
  • Rondeau P, Navarra G, Militello V, et al. On the aggregation of albumin: influences of the protein glycation. Protein Aggregation. 2011:139–159.
  • Anguizola J, Matsuda R, Barnaby OS, et al. Review: glycation of human serum albumin. Clinica Chimica Acta. 2013;425:64–76.
  • Brownlee M, Cerami A, Vlassara H. Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. New England J Med. 1988;318:1315–1321.
  • Fasano M, Curry S, Terreno E, et al. The extraordinary ligand binding properties of human serum albumin. IUBMB Life. 2005;57:787–796.
  • Ascenzi P, Fasano M. Allostery in a monomeric protein: the case of human serum albumin. Biophys Chem. 2010;148:16–22.
  • Van der Vusse GJ. Albumin as fatty acid transporter. Drug Metab Pharmacokinet. 2009;24:300–307.
  • Zunszain PA, Ghuman J, McDonagh AF, et al. Crystallographic analysis of human serum albumin complexed with 4Z,15E-bilirubin-IXalpha. J Mol Biol. 2008;381:394–406.
  • Sjoholm I, Ekman B, Kober A, et al. Binding of drugs to human serum albumin:XI. The specificity of three binding sites as studied with albumin immobilized in microparticles. Mol Pharmacol. 1979;16:767–777.
  • Ascenzi P, Fasano M. Serum heme-albumin: an allosteric protein. IUBMB Life. 2009;61:1118–1122.
  • Wang Y, Wang S, Huang M. Structure and enzymatic activities of human serum albumin. Curr Pharm Des. 2015;21:1831–1836.
  • Gundry RL, Cotter RJ. The albuminome as a tool for biomarker discovery, in Clinical Proteomics: From Diagnosis to Therapy (eds J. E. Van Eyk and M. J. Dunn), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany. 2007:263–278. doi: 10.1002/9783527622153.ch18.
  • Hastings GE, Wolf PG. The therapeutic use of albumin. Arch Fam Med. 1992;1:281–287.
  • Liyasova MS, Schopfer LM, Lockridge O. Reaction of human albumin with aspirin in vitro: mass spectrometric identification of acetylated lysines 199, 402, 519, and 545. Biochem Pharmacol. 2010;79:784–791.
  • Hawkins D, Pinckard RN, Farr RS. Acetylation of human serum albumin by acetylsalicylic acid. ScienceR (New York, NY). 1968;160:780–781.
  • Hawkins D, Pinckard RN, Crawford IP, et al. Structural changes in human serum albumin induced by ingestion of acetylsalicylic acid. J Clin Investig. 1969;48:536–542.
  • Trynda L, Przywarska-Boniecka H, Kościukiewicz T. Influence of aspirin and iron (III) tetrasulfonated phthalocyanine on bilirubin binding by human serum albumin. J Inorg Biochem. 1990;38:153–167.
  • Attallah AA, Lee JB. Indomethacin, salicyclates and prostaglandin binding. Prostaglandins. 1980;19:311–318.
  • Rendell M, Nierenberg J, Brannan C, et al. Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo. J Lab Clin Med. 1986;108:286–293.
  • Hundal RS, Petersen KF, Mayerson AB, et al. Mechanism by which high-dose aspirin improves glucose metabolism in type 2 diabetes. J Clin Invest. 2002;109:1321–1326.
  • Fang F, Lu Y, Ma D-L, et al. A meta-analysis of salicylates for type 2 diabetes mellitus. J Huazhong Univ Sci Technol [Medical Sciences]. 2013;33:1–14.
  • Vannuruswamy G, Jagadeeshaprasad MG, Kashinath K, et al. Molecules with O-acetyl group protect protein glycation by acetylating lysine residues. RSC Adv. 2016;6:65572–65578.
  • Finamore F, Priego-Capote F, Gluck F, et al. Impact of high glucose concentration on aspirin-induced acetylation of human serum albumin: an in vitro study. EuPA Open Proteomics. 2014;3:100–113.
  • Bar-Or D, Heyborne KD, Bar-Or R, et al. Cysteinylation of maternal plasma albumin and its association with intrauterine growth restriction. Prenat Diagn. 2005;25:245–249.
  • Kawakami A, Kubota K, Yamada N, et al. Identification and characterization of oxidized human serum albumin. FEBS J. 2006;273:3346–3357.
  • Boisvert MR, Koski KG, Skinner CD. Increased oxidative modifications of amniotic fluid albumin in pregnancies associated with gestational diabetes mellitus. Anal Chem. 2010;82:1133–1137.
  • Nagumo K, Tanaka M, Chuang VTG, et al. Cys34-cysteinylated human serum albumin is a sensitive plasma marker in oxidative stress-related chronic diseases. PLoS One. 2014;9:e85216.
  • Temple A, Yen T-Y, Gronert S. Identification of specific protein carbonylation sites in model oxidations of human serum albumin. J Am Soc Mass Spectrom. 2006;17:1172–1180.
  • Colombo G, Aldini G, Orioli M, et al. Water-soluble α, β-unsaturated aldehydes of cigarette smoke induce carbonylation of human serum albumin. Antioxid Redox Signal. 2006;12:349–364.
  • Aldini G, Regazzoni L, Orioli M, et al. A tandem MS precursor-ion scan approach to identify variable covalent modification of albumin Cys34: a new tool for studying vascular carbonylation. J Mass Spectrom. 2008;43:1470–1481.
  • Brownlee M. Advanced protein glycosylation in diabetes and aging. Annu Rev Med. 1995;46:223–234.
  • Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J. 1999;344:109–116.
  • Lu L, Pu LJ, Zhang Q, et al. Increased glycated albumin and decreased esRAGE levels are related to angiographic severity and extent of coronary artery disease in patients with type 2 diabetes. Atherosclerosis. 2009;206:540–545.
  • Shaklai N, Garlick RL, Bunn HF. Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J Biol Chem. 1984;259:3812–3817.
  • Barnaby OS, Cerny RL, Clarke W, et al. Comparison of modification sites formed on human serum albumin at various stages of glycation. Clinica Chimica Acta. 2011;412:277–285.
  • Wa C, Cerny RL, Clarke WA, et al. Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Clinica Chimica Acta. 2007;385:48–60.
  • Kisugi R, Kouzuma T, Yamamoto T, et al. Structural and glycation site changes of albumin in diabetic patient with very high glycated albumin. Clinica Chimica Acta. 2007;382:59–64.
  • Nakajou K, Watanabe H, Kragh-Hansen U, et al. The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants. Biochimica et Biophysica Acta (BBa)-General Subjects. 2003;1623:88–97.
  • Layton GJ, Jerums G. Effect of glycation of albumin on its renal clearance in normal and diabetic rats. Kidney Int. 1988;33:673–676.
  • Gugliucci A, Bendayan M. Renal fate of circulating advanced glycated end products (AGE): evidence for reabsorption and catabolism of AGE-peptides by renal proximal tubular cells. Diabetologia. 1996;39:149–160.
  • Bucala R, Makita Z, Vega G, et al. Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency. Proc Natl Acad Sci. 1994;91:9441–9445.
  • Dobrian A, Simionescu M. Irreversibly glycated albumin alters the physico-chemical characteristics of low density lipoproteins of normal and diabetic subjects. Biochimica et Biophysica Acta (BBa)-Molecular Basis of Disease. 1995;1270:26–35.
  • Thornalley PJ. Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs. Cell Mol Biol (Noisy-Le-Grand). 2003;44:1013–1023.
  • Horiuchi S, Sakamoto Y, Sakai M. Scavenger receptors for oxidized and glycated proteins. Amino Acids. 2003;25:283–292.
  • Vlassara H, Brownlee M, Cerami A. High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proc Natl Acad Sci. 1985;82:5588–5592.
  • Ohgami N, Nagai R, Miyazaki A, et al. Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products. J Biol Chem. 2001;276:13348–13355.
  • Ohgami N, Nagai R, Ikemoto M, et al. Cd36, a member of the class b scavenger receptor family, as a receptor for advanced glycation end products. J Biol Chem. 2001;276:3195–3202.
  • Von Zastrow M, Sorkin A. Signaling on the endocytic pathway. Curr Opin Cell Biol. 2007;19:436–445.
  • Platta HW, Stenmark H. Endocytosis and signaling. Curr Opin Cell Biol. 2011;23:393–403.
  • Grimm S, Horlacher M, Catalgol BL, et al. Cathepsins D and L reduce the toxicity of advanced glycation end products. Free Radic Biol Med. 2012;52:1011–1023.
  • Vlassara H. The AGE receptor in the pathogenesis of diabetic complications. Diabetes Metab Res Rev. 2001;17:436–443.
  • H-J Y, Y-H L, Kim SR, et al. Glycated albumin and the risk of micro-and macrovascular complications in subjects with type 1 diabetes. Cardiovasc Diabetol. 2015;14:53.
  • Miyata S, Liu B-F, Shoda H, et al. Accumulation of pyrraline-modified albumin in phagocytes due to reduced degradation by lysosomal enzymes. J Biol Chem. 1997;272:4037–4042.
  • Ghiggeri GM, Candiano G, Delfino G, et al. Glycosyl albumin and diabetic microalbuminuria: demonstration of an altered renal handling. Kidney Int. 1984;25:565–570.
  • Nicoloff G, Baydanoff S, Petrova C, et al. Antibodies to advanced glycation end products in children with diabetes mellitus. Vascul Pharmacol. 2002;39:39–45.
  • Lopes-Virella MF, Baker NL, Hunt KJ, et al. High concentrations of AGE-LDL and oxidized LDL in circulating immune complexes are associated with progression of retinopathy in type 1 diabetes. Diabetes Care. 2012;35:1333–1340.
  • Schalkwijk CG, Ligtvoet N, Twaalfhoven H, et al. Amadori albumin in type 1 diabetic patients: correlation with markers of endothelial function, association with diabetic nephropathy, and localization in retinal capillaries. Diabetes. 1999;48:2446–2453.
  • Khan MWA, Qadrie ZL, Khan WA. Antibodies against gluco-oxidatively modified human serum albumin detected in diabetes-associated complications. Int Arch Allergy Immunol. 2010;153:207–214.
  • Turk Z, Ljubic S, Turk NA, et al. Detection of autoantibodies against advanced glycation endproducts and AGE-immune complexes in serum of patients with diabetes mellitus. Clinica Chimica Acta. 2001;303:105–115.
  • Cornacoff JB, Hebert LA, Smead WL, et al. Primate erythrocyte-immune complex-clearing mechanism. J Clin Invest. 1983;71:236–247.
  • Velez MG, Bhalla V. The role of the immune system in the pathogenesis of diabetic nephropathy. J Nephrol Therapeutic. 2012;5:2161–2959.
  • Bhat S, Jagadeeshaprasad MG, Patil YR, et al. Proteomic insight reveals elevated levels of albumin in circulating immune complexes in diabetic plasma. Mol Cell Proteomics. 2016;15:2011–2020.
  • Ramasamy R, Yan SF, Schmidt AM. Receptor for AGE (RAGE): signaling mechanisms in the pathogenesis of diabetes and its complications. Ann NY Acad Sci. 2011;1243:88–102.
  • Schmidt AM, Hori O, Chen JX, et al. Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes. J Clin Invest. 1995;96:1395–1403.
  • Kislinger T, Fu C, Huber B, et al. N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J Biol Chem. 1994;274:31740–31749.
  • Huang JS, Guh JY, Chen HC, et al. Role of receptor for advanced glycation end-product (RAGE) and the JAK/STAT-signaling pathway in AGE-induced collagen production in NRK-49F cells. J Cell Biochem. 2001;81:102–113.
  • Arif B, Ashraf JM, Ahmad J, et al. Structural and immunological characterization of Amadori-rich human serum albumin: role in diabetes mellitus. Arch Biochem Biophys. 2012;522:17–25.
  • Barnaby OS, Wa C, Cerny RL, et al. Quantitative analysis of glycation sites on human serum albumin using 16 O/18 O-labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Clinica Chimica Acta. 2010;411:1102–1110.
  • Westwood ME, Thornalley PJ. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins. J Protein Chem. 1995;14:359–372.
  • Okabe N, Hashizume N. Drug binding properties of glycosylated human serum albumin as measured by fluorescence and circular dichroism. Biol Pharm Bull. 1994;17:16–21.
  • Howard MJ, Smales CM. NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification. J Biol Chem. 2005:22582–22589.
  • Lapolla A, Gerhardinger C, Baldo L, et al. A study on in vitro glycation processes by matrix-assisted laser desorption ionization mass spectrometry. Biochim Biophys Acta. 1993;1225:33–38.
  • Barnaby OS, Cerny RL, Clarke W, et al. Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI-TOF MS. Clinica Chimica Acta. 2011;412:1606–1615.
  • Zhang Q, Tang N, Brock JWC, et al. Enrichment and analysis of nonenzymatically glycated peptides: boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry. J Proteome Res. 2007;6:2323–2330.
  • Frolov A, Hoffmann P, Hoffmann R. Fragmentation behavior of glycated peptides derived from D-glucose, D-fructose and D-ribose in tandem mass spectrometry. J Mass Spectrom. 2006;41:1459–1469.
  • Lapolla A, Fedele D, Reitano R, et al. Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides. J Am Soc Mass Spectrom. 2004;15:496–509.
  • Ahmed N, Dobler D, Dean M, et al. Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J Biol Chem. 2005;280:5724–5732.
  • Gadgil HS, Bondarenko PV, Treuheit MJ, et al. Screening and sequencing of glycated proteins by neutral loss scan LC/MS/MS method. Anal Chem. 2007;79:5991–5999.
  • Frolov A, Hoffmann R. Identification and relative quantification of specific glycation sites in human serum albumin. Anal Bioanal Chem. 2010;397:2349–2356.
  • Stefanowicz P, Kijewska M, Kluczyk A, et al. Detection of glycation sites in proteins by high-resolution mass spectrometry combined with isotopic labeling. Anal Biochem. 2010;400:237–243.
  • Bhonsle HS, Korwar AM, Kote SS, et al. Low plasma albumin levels are associated with increased plasma protein glycation and HbA1c in diabetes. J Proteome Res. 2012;11:1391–1396.
  • Korwar AM, Vannuruswamy G, Jagadeeshaprasad MG, et al. Development of diagnostic fragment ion library for glycated peptides of human serum albumin: targeted quantification in prediabetic, diabetic, and microalbuminuria plasma by parallel reaction monitoring, SWATH, and MSE. Mol Cell Proteomics. 2015;14:2150–2159.
  • Brede C, Hop B, Jørgensen K, et al. Measurement of glycated albumin in serum and plasma by LC-MS/MS. Scand J Clin Lab Invest. 2016;76:195–201.
  • Soboleva A, Modzel M, Didio A, et al. Quantification of prospective type 2 diabetes mellitus biomarkers by stable isotope dilution with bi-labeled standard glycated peptides. Anal Methods. 2017;9:409–418.
  • Cohen RM, Franco RS, Khera PK, et al. Red cell life span heterogeneity in hematologically normal people is sufficient to alter HbA1c. Blood. 2008;112:4284–4291.
  • Cohen RM, Sacks DB. Comparing multiple measures of glycemia: how to transition from biomarker to diagnostic test? Clinical Chemistry. 2012;58:1615–1617.
  • Sacks DB. A1C versus glucose testing: a comparison. Diabetes Care. 2011;34:518–523.
  • Wright LA-C, Hirsch IB. The challenge of the use of glycemic biomarkers in diabetes: reflecting on hemoglobin A1C, 1, 5-anhydroglucitol, and the glycated proteins fructosamine and glycated albumin. Diabetes Spectrum. 2012;25:141–148.
  • Tylee TS, Trence DL. Glycemic variability: looking beyond the A1C. Diabetes Spectrum. 2012;25:149–153.
  • Bhonsle HS, Singh SK, Srivastava G, et al. Albumin competitively inhibits glycation of less abundant proteins. Protein Pept Lett. 2008;15:663–667.
  • Takahashi S, Uchino H, Shimizu T, et al. Comparison of glycated albumin (GA) and glycated hemoglobin (HbA1c) in type 2 diabetic patients: usefulness of GA for evaluation of short-term changes in glycemic control. Endocr J. 2007;54:139–144.
  • Armbruster DA. Fructosamine: structure, analysis, and clinical usefulness. Clinical Chemistry. 1987;33:2153–2163.
  • Rodriguez-Segade S, Lojo S, Camina MF, et al. Effects of various serum proteins on quantification of fructosamine. Clinical Chemistry. 1989;35:134–138.
  • Koga M, Kasayama S. Clinical impact of glycated albumin as another glycemic control marker. Endocr J. 2010;57:751–762.
  • Paroni R, Ceriotti F, Galanello R, et al. Performance characteristics and clinical utility of an enzymatic method for the measurement of glycated albumin in plasma. Clin Biochem. 2007;40:1398–1405.
  • Kouzuma T, Usami T, Yamakoshi M, et al. An enzymatic method for the measurement of glycated albumin in biological samples. Clinica Chimica Acta. 2002;324:61–71.
  • Sumner AE, Duong MT, Aldana PC, et al. A1C combined with glycated albumin improves detection of prediabetes in Africans: the Africans in America study. Diabetes Care. 2016;39:271–277.
  • Chujo K, Shima K, Tada H, et al. Indicators for blood glucose control in diabetics with end-stage chronic renal disease: GHb vs. glycated albumin (GA). J Med Investig. 2006;53:223–228.
  • Inaba M, Okuno S, Kumeda Y, et al. Glycated albumin is a better glycemic indicator than glycated hemoglobin values in hemodialysis patients with diabetes: effect of anemia and erythropoietin injection. J Am Soc Nephrol. 2007;18:896–903.
  • Wang N, Xu Z, Han P, et al. Glycated albumin and ratio of glycated albumin to glycated hemoglobin are good indicators of diabetic nephropathy in type 2 diabetes mellitus. Diabetes Metab Res Rev. 2017;33:e2843. [Epub 2016 Sep 26].
  • Umayahara Y, Fujita Y, Watanabe H, et al. Association of glycated albumin to HbA1c ratio with diabetic retinopathy but not diabetic nephropathy in patients with type 2 diabetes. Clin Biochem. 2016;60:30390–30393.
  • Song SO, Kim KJ, Lee B-W, et al. Serum glycated albumin predicts the progression of carotid arterial atherosclerosis. Atherosclerosis. 2012;225:450–455.
  • Furusyo N, Koga T, Ai M, et al. Plasma glycated albumin level and atherosclerosis: results from the Kyushu and Okinawa Population Study (KOPS). Int J Cardiol. 2013;167:2066–2072.
  • Wang N, Guo C, Han P, et al. Glycated albumin indicates peripheral diabetic neuropathy. Acta Diabetol. 2016;53:973–979.
  • Selvin E, Rawlings AM, Grams M, et al. Fructosamine and glycated albumin for risk stratification and prediction of incident diabetes and microvascular complications: a prospective cohort analysis of the Atherosclerosis Risk in Communities (ARIC) study. Lancet Diabetes Endocrinol. 2014;2:279–288.
  • Hashimoto K, Noguchi S, Morimoto Y, et al. A1C but not serum glycated albumin is elevated in late pregnancy owing to iron deficiency. Diabetes Care. 2008;31:1945–1948.
  • Hashimoto K, Osugi T, Noguchi S, et al. A1C but not serum glycated albumin is elevated because of iron deficiency in late pregnancy in diabetic women. Diabetes Care. 2008;33:509–511.
  • Flaim KE, Hutson SM, Lloyd CE, et al. Direct effect of insulin on albumin gene expression in primary cultures of rat hepatocytes. Am J Physiology-Endocrinology Metabolism. 1985;249:E447–E53.
  • Jefferson LS, Liao WS, Peavy DE, et al. Diabetes-induced alterations in liver protein synthesis. Changes in the relative abundance of mRNAs for albumin and other plasma proteins. J Biol Chem. 1983;258:1369–1375.
  • Nicholson JP, Wolmarans MR, Park GR. The role of albumin in critical illness. Br J Anaesth. 2000;85:599–610.
  • Merlot AM, Kalinowski DS, Richardson DR. Unraveling the mysteries of serum albumin-more than just a serum protein. Front Physiol. 2014;5:299.
  • Stehle G, Sinn H, Wunder A, et al. Plasma protein (albumin) catabolism by the tumor itself–implications for tumor metabolism and the genesis of cachexia. Crit Rev Oncol Hematol. 1997;26:77–100.
  • Viswanathan V, Snehalatha C, Kumutha R, et al. Serum albumin levels in different stages of type 2 diabetic nephropathy patients. Indian J Nephrol. 2004;14:89–92.
  • Rodríguez-Segade S, Rodríguez J, Mayan D, et al. Plasma albumin concentration is a predictor of HbA1c among type 2 diabetic patients, independently of fasting plasma glucose and fructosamine. Diabetes Care. 2005;28:437–439.
  • Jellinge ME, Henriksen DP, Hallas P, et al. Hypoalbuminemia is a strong predictor of 30-day all-cause mortality in acutely admitted medical patients: a prospective, observational, cohort study. PLoS One. 2014;9:e105983.
  • Nathan DM, McGee P, Steffes MW, et al. Relationship of glycated albumin to blood glucose and glycated hemoglobin (HbA1C) values and to retinopathy, nephropathy and cardiovascular outcomes in the DCCT/EDIC study. Diabetes. 2014;63:282–289.
  • Tiwari S, Bothale M, Hasan I, et al. Association between serum albumin and glycated hemoglobin in Asian Indian subjects. Indian J Endocrinol Metab. 2014;19:52–55.
  • Jagadeeshaprasad MG, Batkulwar KB, Meshram NN, et al. Targeted quantification of N-1-(carboxymethyl) valine and N-1-(carboxyethyl) valine peptides of β-hemoglobin for better diagnostics in diabetes. Clin Proteomics. 2016;13:7.
  • Sviridov D, Drake SK, Hortin GL. Reactivity of urinary albumin (microalbumin) assays with fragmented or modified albumin. Clinical Chemistry. 2008;54:61–68.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.