munich

Human serum albumin

January 29, 2024
by

Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma; it constitutes about half of serum protein. It is produced in the liver. It is soluble in water, and it is monomeric.[citation needed]

Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains oncotic pressure, among other functions.

Albumin is synthesized in the liver as preproalbumin, which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi apparatus to produce the secreted albumin.

The reference range for albumin concentrations in serum is approximately 35–50 g/L (3.5–5.0 g/dL). It has a serum half-life of approximately 21 days. It has a molecular mass of 66.5 kDa.

The gene for albumin is located on chromosome 4 in locus 4q13.3 and mutations in this gene can result in anomalous proteins. The human albumin gene is 16,961 nucleotides long from the putative ‘cap’ site to the first poly(A) addition site. It is split into 15 exons that are symmetrically placed within the 3 domains thought to have arisen by triplication of a single primordial domain.

Human serum albumin (HSA) is a highly water-soluble globular monomeric plasma protein with a relative molecular weight of 67 KDa, consisting of 585 amino acid residues, one sulfhydryl group and 17 disulfide bridges. Among nanoparticulate carriers, HSA nanoparticles have long been the center of attention in the pharmaceutical industry due to their ability to bind to various drug molecules, great stability during storage and in vivo usage, no toxicity and antigenicity, biodegradability, reproducibility, scale up of the production process and a better control over release properties. In addition, significant amounts of drug can be incorporated into the particle matrix because of the large number of drug binding sites on the albumin molecule.

  • Kouchakzadeh H, Shojaosadati SA, Shokri F (September 2014). “Efficient loading and entrapment of tamoxifen in human serum albumin based nanoparticulate delivery system by a modified desolvation technique”. Chemical Engineering Research and Design. 92 (9): 1681–1692. doi:10.1016/j.cherd.2013.11.024.

Function

Measurement

Serum albumin is commonly measured by recording the change in absorbance upon binding to a dye such as bromocresol green or bromocresol purple.

From left to right solutions of 0.1 M HCl, 3 buffer solutions of pH 3.78, 3 of pH 4.00, 3 of pH 4.62 and NaOH 0.1 M after adding different amounts of bromocresol green (more in darker solutions)

Bromocresol green (BCG) is a dye of the triphenylmethane family (triarylmethane dyes). It belongs to a class of dyes called sulfonephthaleins. It is used as a pH indicator in applications such as growth mediums for microorganisms and titrations. In clinical practise, it is commonly used as a diagnostic technique. The most common use of bromocresol green is to measure serum albumin concentration within mammalian blood samples in possible cases of kidney failure and liver disease. In chemistry, bromocresol green is used in Thin-layer chromatography staining solutions to visualize acidic compounds. In aqueous solution, bromocresol green will ionize to give the monoanionic form (yellow), that further deprotonates at higher pH to give the dianionic form (blue), which is stabilized by resonance. The acid dissociation constant (pKa) of this reaction is 4.8. Tap water is sufficiently basic to give a solution of bromocresol green its characteristic blue-green color. The acid and basic forms of this dye have an isosbestic point in their UV-Visible spectrum, around 515 nm, indicate that the two forms interconvert directly without forming any other substance. An ethanol solution (0.04 wt%) of bromocresol green has been proposed for TLC staining and is suitable for visualisation of the compounds with functional groups whose pKa is below 5.0 (carboxylic acids, sulfonic acids, etc.). These appear as yellow spots on a light or dark blue background; no heating is necessary. Bromophenol blue solution can be used for the same purpose. The compound is synthesized by bromination of cresol purple (m-cresolsulfonphthalein).

Absorbance spectrum of bromocresol green at different pH values. The isosbestic point occurs where the acid and basic forms and mixtures thereof have the same absorbance

Uses

It is used as a pH indicator and as a tracking dye for DNA agarose gel electrophoresis. It can be used in its free acid form (light brown solid), or as a sodium salt (dark green solid). It is also an inhibitor of the prostaglandin E2 transport protein. ??? Additional applications include use in sol-gel matrices, the detection of ammonia, and the measurement of albumin in human plasma and serum. Bromocresol green may cause irritation. Skin and eye contact should be avoided.

Bromocresol purple (BCP) or 5′,5″-dibromo-o-cresolsulfophthalein, is a dye of the triphenylmethane family (triarylmethane dyes) and a pH indicator. It is colored yellow below pH 5.2, and violet above pH 6.8. In its cyclic sulfonate ester form, it has a pKa value of 6.3, and is usually prepared as a 0.04% aqueous solution. Bromocresol purple is used in medical laboratories to measure albumin. Use of BCP in this application may provide some advantage over older methods using bromocresol green. In microbiology, it is used for staining dead cells based on their acidity, and for the isolation and assaying of lactic acid bacteria. In photographic processing, it can be used as an additive to acid stop baths to indicate that the bath has reached neutral pH and needs to be replaced. Bromocresol purple milk solids glucose agar is used as a medium used to distinguish dermatophytes from bacteria and other organisms in cases of ringworm fungus (T. verrucosum) infestation in cattle and other animals.

pH Indicator

Similar to bromocresol green, the structure of bromocresol purple changes with pH. Changing the level of acidity causes a shift in the equilibrium between two different structures that have different colors. In near-neutral or alkaline solution, the chemical has a sulfonate structure that gives the solution a purple color. As the pH decreases, it converts to a sultone (cyclic sulfonic ester) that colors the solution yellow. In some microbiology tests, this change is used as an indicator of bacterial growth.

Categories: 

Reference ranges

The normal range of human serum albumin in adults (> 3 y.o.) is 3.5–5.0  g/dL (35–50 g/L). For children less than three years of age, the normal range is broader, 2.9–5.5 g/dL.

Low albumin (hypoalbuminemia) may be caused by liver disease, nephrotic syndrome, burns, protein-losing enteropathy, malabsorption, malnutrition, late pregnancy, artefact, genetic variations and malignancy.[citation needed]

High albumin (hyperalbuminemia) is almost always caused by dehydration. In some cases of retinol (Vitamin A) deficiency, the albumin level can be elevated to high-normal values (e.g., 4.9 g/dL) because retinol causes cells to swell with water. (This is also the reason too much Vitamin A is toxic.) This swelling also likely occurs during treatment with 13-cis retinoic acid (isotretinoin), a pharmaceutical for treating severe acne, amongst other conditions. In lab experiments it has been shown that all-trans retinoic acid down regulates human albumin production.

Isotretinoin, also known as 13-cis-retinoic acid and sold under the brand name Accutane among others, is a medication primarily used to treat severe acne. It is also used to prevent certain skin cancers (squamous-cell carcinoma), and in the treatment of other cancers. It is used to treat harlequin-type ichthyosis, a usually lethal skin disease, and lamellar ichthyosis. It is a retinoid, meaning it is related to vitamin A, and is found in small quantities naturally in the body. Its isomer, tretinoin, is also an acne drug. The most common adverse effects are dry lips (cheilitis), dry and fragile skin, and an increased susceptibility to sunburn. Uncommon and rare side effects include muscle aches and pains (myalgias), and headaches. Isotretinoin is known to cause birth defects due to in-utero exposure because of the molecule’s close resemblance to retinoic acid, a natural vitamin A derivative that controls normal embryonic development. It is also associated with psychiatric side effects, most commonly depression but also, more rarely, psychosis and unusual behaviours. Other rare side effects include hyperostosis and premature epiphyseal closure, which have been reported to be persistent. Isotretinoin was patented in 1969 and approved for medical use in 1982. In 2021, it was the 264th most commonly prescribed medication in the United States, with more than 1 million prescriptions. In February 2002, Roche’s patents for isotretinoin expired, and there are now many other companies selling cheaper generic versions of the drug. On 29 June 2009, Roche Pharmaceuticals, the original creator and distributor of isotretinoin, officially discontinued both the manufacture and distribution of their Accutane brand in the United States due to what the company described as business reasons related to low market share (below 5%), coupled with the high cost of defending personal injury lawsuits brought by some people who took the drug. Roche USA continues to defend Accutane and claims to have treated over 13 million people since its introduction in 1982. F. Hoffmann-La Roche Ltd. apparently will continue to manufacture and distribute Roaccutane outside of the United States. Among others, actor James Marshall sued Roche over allegedly Accutane-related disease that resulted in removal of his colon. The jury, however, decided that James Marshall had a pre-existing bowel disease. Several trials over inflammatory bowel disease claims have been held in the United States, with many of them resulting in multimillion-dollar judgments against the makers of isotretinoin. As of 2017, it was marketed as a topical combination drug with erythromycin under the brand names Isotrex Eritromicina, Isotrexin, and Munderm. As of 2017, isotretinoin was marketed under many brand names worldwide: A-Cnotren, Absorica, Accuran, Accutane, Accutin, Acne Free, Acnecutan, Acnegen, Acnemin, Acneone, Acneral, Acnestar, Acnetane, Acnetin A, Acnetrait, Acnetrex, Acnogen, Acnotin, Acnotren, Acretin, Actaven, Acugen, Acutret, Acutrex, Ai Si Jie, Aisoskin, Aknal, Aknefug Iso, Aknenormin, Aknesil, Aknetrent, Amnesteem, Atlacne, Atretin, Axotret, Casius, Ciscutan, Claravis, Contracné, Curacne, Curacné, Curakne, Curatane, Cuticilin, Decutan, Dercutane, Effederm, Epuris, Eudyna, Farmacne, Flexresan, Flitrion, I-Ret, Inerta, Inflader, Inotrin, Isac, Isdiben, Isoacne, Isobest, Isocural, Isoderm, Isoface, IsoGalen, Isogeril, Isolve, Isoprotil, Isoriac, Isosupra, Isosupra Lidose, Isotane, Isotina, Isotinon, Isotren, Isotret, Isotretinoin, Isotretinoina, Isotretinoína, Isotretinoine, Isotretinoïne, Isotrétinoïne, Isotretinoinum, Isotrex, Isotrin, Isotroin, Izotek, Izotziaja, Lisacne, Locatret, Mayesta, Medinac, Myorisan, Neotrex, Netlook, Nimegen, Noitron, Noroseptan, Novacne, Oralne, Oraret, Oratane, Piplex, Policano, Procuta, Reducar, Retacnyl, Retin A, Roaccutan, Roaccutane, Roacnetan, Roacta, Roacutan, Rocne, Rocta, Sotret, Stiefotrex, Tai Er Si, Teweisi, Tretin, Tretinac, Tretinex, Tretiva, Tufacne, Zenatane, Zerocutan, Zonatian ME, and Zoretanin.

Pathology

Hypoalbuminemia

Hypoalbuminemia means low blood albumin levels.

This can be caused by:

In clinical medicine, hypoalbuminemia significantly correlates with a higher mortality rates in several conditions such as heart failure, post-surgery, COVID-19.

Hyperalbuminemia

Hyperalbuminemia is an increased concentration of albumin in the blood. Typically, this condition is due to dehydration. Hyperalbuminemia has also been associated with high protein diets.

Medical use

Human albumin solution (HSA) is available for medical use, usually at concentrations of 5–25%.

Human albumin is often used to replace lost fluid and help restore blood volume in trauma, burns and surgery patients. There is no strong medical evidence that albumin administration (compared to saline) saves lives for people who have hypovolaemia or for those who are critically ill due to burns or hypoalbuminaemia. It is also not known if there are people who are critically ill that may benefit from albumin. Therefore, the Cochrane Collaboration recommends that it should not be used, except in clinical trials.

In acoustic droplet vaporization (ADV), albumin is sometimes used as a surfactant. ADV has been proposed as a cancer treatment by means of occlusion therapy.

  • Lo AH, Kripfgans OD, Carson PL, Rothman ED, Fowlkes JB (May 2007). “Acoustic droplet vaporization threshold: effects of pulse duration and contrast agent”. IEEE Transactions on Ultrasonics, Ferroelectrics, and Frequency Control. 54 (5): 933–946. doi:10.1109/tuffc.2007.339. PMID 17523558. S2CID 11983041.

Acoustic droplet vaporization (ADV) is the process by which superheated liquid droplets are phase-transitioned into gas bubbles by means of ultrasound. Perfluorocarbons and halocarbons are often used for the dispersed medium, which forms the core of the droplet. The surfactant, which forms a stabilizing shell around the dispersive medium, is usually composed of albumin or lipids. There exist two main hypothesis that explain the mechanism by which ultrasound induces vaporization. One poses that the ultrasonic field interacts with the dispersed medium so as to cause vaporization in the bubble core. The other suggests that shockwaves from inertial cavitation, occurring near or within the droplet, cause the dispersed medium to vaporize.

See also

Human serum albumin may be used to potentially reverse drug/chemical toxicity by binding to free drug/agent.

  • Ascenzi P, Leboffe L, Toti D, Polticelli F, Trezza V (August 2018). “Fipronil recognition by the FA1 site of human serum albumin”. Journal of Molecular Recognition. 31 (8): e2713. doi:10.1002/jmr.2713. PMID 29656610. S2CID 4894574.

Human albumin may also be used in treatment of decompensated cirrhosis.

Human serum albumin has been used as a component of a frailty index.

Glycation

It has been known for a long time that human blood proteins like hemoglobin and serum albumin may undergo a slow non-enzymatic glycation, mainly by formation of a Schiff base between ε-amino groups of lysine (and sometimes arginine) residues and glucose molecules in blood (Maillard reaction). This reaction can be inhibited in the presence of antioxidant agents. Although this reaction may happen normally, elevated glycoalbumin is observed in diabetes mellitus.

Glycation has the potential to alter the biological structure and function of the serum albumin protein.

  • Mohamadi-Nejad A, Moosavi-Movahedi AA, Hakimelahi GH, Sheibani N (September 2002). “Thermodynamic analysis of human serum albumin interactions with glucose: insights into the diabetic range of glucose concentration”. The International Journal of Biochemistry & Cell Biology. 34 (9): 1115–1124. doi:10.1016/S1357-2725(02)00031-6. PMID 12009306.
  • Shaklai N, Garlick RL, Bunn HF (March 1984). “Nonenzymatic glycosylation of human serum albumin alters its conformation and function”. The Journal of Biological Chemistry. 259 (6): 3812–3817. doi:10.1016/S0021-9258(17)43168-1. PMID 6706980.
  • Mendez DL, Jensen RA, McElroy LA, Pena JM, Esquerra RM (December 2005). “The effect of non-enzymatic glycation on the unfolding of human serum albumin”. Archives of Biochemistry and Biophysics. 444 (2): 92–99. doi:10.1016/j.abb.2005.10.019. PMID 16309624.
  • Mohamadi-Nejada A, Moosavi-Movahedi AA, Safariana S, Naderi-Maneshc MH, Ranjbarc B, Farzamid B, Mostafavie H, Larijanif MB, Hakimelahi GH (July 2002). “The thermal analysis of nonezymatic glycosylation of human serum albumin: differential scanning calorimetry and circular dichroism studies”. Thermochimica Acta. 389 (1–2): 141–151. doi:10.1016/S0040-6031(02)00006-0.

Moreover, the glycation can result in the formation of Advanced Glycation End-Products (AGE), which result in abnormal biological effects. Accumulation of AGEs leads to tissue damage via alteration of the structures and functions of tissue proteins, stimulation of cellular responses, through receptors specific for AGE-proteins, and generation of reactive oxygen intermediates. AGEs also react with DNA, thus causing mutations and DNA transposition. Thermal processing of proteins and carbohydrates brings major changes in allergenicity. AGEs are antigenic and represent many of the important neoantigens found in cooked or stored foods. They also interfere with the normal product of nitric oxide in cells.

Although there are several lysine and arginine residues in the serum albumin structure, very few of them can take part in the glycation reaction.

Oxidation

The albumin is the predominant protein in most body fluids, its Cys34 represents the largest fraction of free thiols within the body. The albumin Cys34 thiol exists in both reduced and oxidized forms. In plasma of healthy young adults, 70–80% of total HSA contains the free sulfhydryl group of Cys34 in a reduced form or mercaptoalbumin (HSA-SH). However, in pathological states characterized by oxidative stress such as kidney disease, liver disease and diabetes the oxidized form, or non-mercaptoalbumin (HNA), could predominate. The albumin thiol reacts with radical hydroxyl (.OH), hydrogen peroxide (H2O2) and the reactive nitrogen species as peroxynitrite (ONOO.), and have been shown to oxidize Cys34 to sulfenic acid derivate (HSA-SOH), it can be recycled to mercapto-albumin; however at high concentrations of reactive species leads to the irreversible oxidation to sulfinic (HSA-SO2H) or sulfonic acid (HSA-SO3H) affecting its structure. Presence of reactive oxygen species (ROS), can induce irreversible structural damage and alter protein activities.[citation needed]

Loss via kidneys

In the healthy kidney, albumin’s size and negative electric charge exclude it from excretion in the glomerulus. This is not always the case, as in some diseases including diabetic nephropathy, which can sometimes be a complication of uncontrolled or of longer term diabetes in which proteins can cross the glomerulus. The lost albumin can be detected by a simple urine test. Depending on the amount of albumin lost, a patient may have normal renal function, microalbuminuria, or albuminuria.

Interactions

Human serum albumin has been shown to interact with FCGRT.

The neonatal fragment crystallizable (Fc) receptor (also FcRn, IgG receptor FcRn large subunit p51, or Brambell receptor) is a protein that in humans is encoded by the FCGRTgene. It is an IgG Fc receptor which is similar in structure to the MHC class I molecule and also associates with beta-2-microglobulin. In rodents, FcRn was originally identified as the receptor that transports maternal immunoglobulin G (IgG) from mother to neonatal offspring via mother’s milk, leading to its name as the neonatal Fc receptor. In humans, FcRn is present in the placenta where it transports mother’s IgG to the growing fetus. FcRn has also been shown to play a role in regulating IgG and serum albumin turnover. Neonatal Fc receptor expression is up-regulated by the proinflammatory cytokine, TNF, and down-regulated by IFN-γ.

It might also interact with a yet-unidentified albondin (gp60), a certain pair of gp18/gp30, and some other proteins like:

In medicine and pharmacology, albondin (gp60) is a cell receptor that binds serum albumin. It seems to be expressed on endothelial cells and binding induces endocytosis. Not much is known about this protein, except for its approximate molecular mass of 60 kDa.

See also

References

  1. GRCh38: Ensembl release 89: ENSG00000163631 – Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000029368 – Ensembl, May 2017
  3. “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. “Harmonisation of Reference Intervals” (PDF). pathologyharmony.co.uk. Pathology Harmony. Archived from the original (PDF) on 2 August 2013. Retrieved 23 June 2013.
  6. “Hypoalbuminemia: Background, Pathophysiology, Etiology”. Medscape Reference. 2019-11-10. Retrieved 2019-12-22.
  7. Kouchakzadeh H, Shojaosadati SA, Shokri F (September 2014). “Efficient loading and entrapment of tamoxifen in human serum albumin based nanoparticulate delivery system by a modified desolvation technique”. Chemical Engineering Research and Design. 92 (9): 1681–1692. doi:10.1016/j.cherd.2013.11.024.
  8. di Masi A, Leboffe L, Polticelli F, Tonon F, Zennaro C, Caterino M, et al. (September 2018). “Human Serum Albumin Is an Essential Component of the Host Defense Mechanism Against Clostridium difficile Intoxication”. The Journal of Infectious Diseases. 218 (9): 1424–1435. doi:10.1093/infdis/jiy338. PMID 29868851.
  9. “Albumin: analyte monograph” (PDF). Association for Clinical Biochemistry and Laboratory Medicine. Archived from the original (PDF) on 13 November 2012. Retrieved 23 June 2013.
  10. “Normal Ranges for Common Laboratory Tests”. Archived from the original on 2013-01-14. Retrieved 2007-12-06. Rush University
  11. Pasantes-Morales H, Wright CE, Gaull GE (December 1984). “Protective effect of taurine, zinc and tocopherol on retinol-induced damage in human lymphoblastoid cells”. The Journal of Nutrition. 114 (12): 2256–2261. doi:10.1093/jn/114.12.2256. PMID 6502269.
  12. Masaki T, Matsuura T, Ohkawa K, Miyamura T, Okazaki I, Watanabe T, Suzuki T (July 2006). “All-trans retinoic acid down-regulates human albumin gene expression through the induction of C/EBPbeta-LIP”. The Biochemical Journal. 397 (2): 345–353. doi:10.1042/BJ20051863. PMC 1513275. PMID 16608438.
  13. Anderson DM (2000). Dorland’s illustrated medical dictionary (29th ed.). Philadelphia [u.a.]: Saunders. p. 860. ISBN 978-0721682617.
  14. Zerbato V, Sanson G, De Luca M, Di Bella S, di Masi A, Caironi P, et al. (2022-04-20). “The Impact of Serum Albumin Levels on COVID-19 Mortality”. Infectious Disease Reports. 14 (3): 278–286. doi:10.3390/idr14030034. ISSN 2036-7449. PMC 9149867. PMID 35645213.
  15. Green P, Woglom AE, Genereux P, Daneault B, Paradis JM, Schnell S, et al. (September 2012). “The impact of frailty status on survival after transcatheter aortic valve replacement in older adults with severe aortic stenosis: a single-center experience”. JACC. Cardiovascular Interventions. 5 (9): 974–981. doi:10.1016/j.jcin.2012.06.011. PMC 3717525. PMID 22995885.
  16. Uthamalingam S, Kandala J, Daley M, Patvardhan E, Capodilupo R, Moore SA, Januzzi JL (December 2010). “Serum albumin and mortality in acutely decompensated heart failure”. American Heart Journal. 160 (6): 1149–1155. doi:10.1016/j.ahj.2010.09.004. PMID 21146671.
  17. Xu R, Hao M, Zhou W, Liu M, Wei Y, Xu J, Zhang W (August 2022). “Preoperative hypoalbuminemia in patients undergoing cardiac surgery: a meta-analysis”. Surgery Today. 53 (8): 861–872. doi:10.1007/s00595-022-02566-9. PMID 35933630. S2CID 251369303.
  18. Zerbato V, Sanson G, De Luca M, Di Bella S, di Masi A, Caironi P, et al. (April 2022). “The Impact of Serum Albumin Levels on COVID-19 Mortality”. Infectious Disease Reports. 14 (3): 278–286. doi:10.3390/idr14030034. PMC 9149867. PMID 35645213.
  19. Busher JT (1990). “Chapter 101: Serum Albumin and Globulin”. In Walker HK, Hall WD, Hurst JW (eds.). Clinical methods : the history, physical, and laboratory examinations (3rd ed.). Boston: Butterworths. ISBN 978-0409900774. PMID 21250048.
  20. Mutlu EA, Keshavarzian A, Mutlu GM (June 2006). “Hyperalbuminemia and elevated transaminases associated with high-protein diet”. Scandinavian Journal of Gastroenterology. 41 (6): 759–760. doi:10.1080/00365520500442625. PMID 16716979. S2CID 21264934.
  21. Roberts I, Blackhall K, Alderson P, Bunn F, Schierhout G (November 2011). “Human albumin solution for resuscitation and volume expansion in critically ill patients”. The Cochrane Database of Systematic Reviews. 2011 (11): CD001208. doi:10.1002/14651858.CD001208.pub4. hdl:2299/5243. PMC 7055200. PMID 22071799.
  22. Yu YT, Liu J, Hu B, Wang RL, Yang XH, Shang XL, et al. (July 2021). “Expert consensus on the use of human serum albumin in critically ill patients”. Chinese Medical Journal. 134 (14): 1639–1654. doi:10.1097/CM9.0000000000001661. PMC 8318641. PMID 34397592.
  23. Lo AH, Kripfgans OD, Carson PL, Rothman ED, Fowlkes JB (May 2007). “Acoustic droplet vaporization threshold: effects of pulse duration and contrast agent”. IEEE Transactions on Ultrasonics, Ferroelectrics, and Frequency Control. 54 (5): 933–946. doi:10.1109/tuffc.2007.339. PMID 17523558. S2CID 11983041.
  24. Ascenzi P, Leboffe L, Toti D, Polticelli F, Trezza V (August 2018). “Fipronil recognition by the FA1 site of human serum albumin”. Journal of Molecular Recognition. 31 (8): e2713. doi:10.1002/jmr.2713. PMID 29656610. S2CID 4894574.
  25. Caraceni P, Riggio O, Angeli P, Alessandria C, Neri S, Foschi FG, et al. (June 2018). “Long-term albumin administration in decompensated cirrhosis (ANSWER): an open-label randomised trial”. Lancet. 391 (10138): 2417–2429. doi:10.1016/S0140-6736(18)30840-7. hdl:2108/208667. PMID 29861076. S2CID 44120418.
  26. Rahbar S (October 1968). “An abnormal hemoglobin in red cells of diabetics”. Clinica Chimica Acta; International Journal of Clinical Chemistry. 22 (2): 296–298. doi:10.1016/0009-8981(68)90372-0. PMID 5687098.
  27. Day JF, Thorpe SR, Baynes JW (February 1979). “Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum”. The Journal of Biological Chemistry. 254 (3): 595–597. doi:10.1016/S0021-9258(17)37845-6. PMID 762083.
  28. Iberg N, Flückiger R (October 1986). “Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites”. The Journal of Biological Chemistry. 261 (29): 13542–13545. doi:10.1016/S0021-9258(18)67052-8. PMID 3759977.
  29. Jakus V, Hrnciarová M, Cársky J, Krahulec B, Rietbrock N (1999). “Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity”. Life Sciences. 65 (18–19): 1991–1993. doi:10.1016/S0024-3205(99)00462-2. PMID 10576452.
  30. Mohamadi-Nejad A, Moosavi-Movahedi AA, Hakimelahi GH, Sheibani N (September 2002). “Thermodynamic analysis of human serum albumin interactions with glucose: insights into the diabetic range of glucose concentration”. The International Journal of Biochemistry & Cell Biology. 34 (9): 1115–1124. doi:10.1016/S1357-2725(02)00031-6. PMID 12009306.
  31. Shaklai N, Garlick RL, Bunn HF (March 1984). “Nonenzymatic glycosylation of human serum albumin alters its conformation and function”. The Journal of Biological Chemistry. 259 (6): 3812–3817. doi:10.1016/S0021-9258(17)43168-1. PMID 6706980.
  32. Mendez DL, Jensen RA, McElroy LA, Pena JM, Esquerra RM (December 2005). “The effect of non-enzymatic glycation on the unfolding of human serum albumin”. Archives of Biochemistry and Biophysics. 444 (2): 92–99. doi:10.1016/j.abb.2005.10.019. PMID 16309624.
  33. Mohamadi-Nejada A, Moosavi-Movahedi AA, Safariana S, Naderi-Maneshc MH, Ranjbarc B, Farzamid B, Mostafavie H, Larijanif MB, Hakimelahi GH (July 2002). “The thermal analysis of nonezymatic glycosylation of human serum albumin: differential scanning calorimetry and circular dichroism studies”. Thermochimica Acta. 389 (1–2): 141–151. doi:10.1016/S0040-6031(02)00006-0.
  34. Kańska U, Boratyński J (2002). “Thermal glycation of proteins by D-glucose and D-fructose”. Archivum Immunologiae et Therapiae Experimentalis. 50 (1): 61–66. PMID 11916310.
  35. Rojas A, Romay S, González D, Herrera B, Delgado R, Otero K (February 2000). “Regulation of endothelial nitric oxide synthase expression by albumin-derived advanced glycosylation end products”. Circulation Research. 86 (3): E50–E54. doi:10.1161/01.RES.86.3.e50. PMID 10679490.
  36. Garlick RL, Mazer JS (May 1983). “The principal site of nonenzymatic glycosylation of human serum albumin in vivo”. The Journal of Biological Chemistry. 258 (10): 6142–6146. doi:10.1016/S0021-9258(18)32384-6. PMID 6853480.
  37. Kawakami A, Kubota K, Yamada N, Tagami U, Takehana K, Sonaka I, et al. (July 2006). “Identification and characterization of oxidized human serum albumin. A slight structural change impairs its ligand-binding and antioxidant functions”. The FEBS Journal. 273 (14): 3346–3357. doi:10.1111/j.1742-4658.2006.05341.x. PMID 16857017. S2CID 12844381.
  38. Turell L, Carballal S, Botti H, Radi R, Alvarez B (April 2009). “Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment”. Brazilian Journal of Medical and Biological Research = Revista Brasileira de Pesquisas Medicas e Biologicas. 42 (4): 305–311. doi:10.1590/s0100-879×2009000400001. PMID 19330257.
  39. Rosas-Díaz M, Camarillo-Cadena M, Hernández-Arana A, Ramón-Gallegos E, Medina-Navarro R (June 2015). “Antioxidant capacity and structural changes of human serum albumin from patients in advanced stages of diabetic nephropathy and the effect of the dialysis”. Molecular and Cellular Biochemistry. 404 (1–2): 193–201. doi:10.1007/s11010-015-2378-2. PMID 25758354. S2CID 6718332.
  40. Watanabe H, Imafuku T, Otagiri M, Maruyama T (2017). “Clinical Implications Associated With the Posttranslational Modification-Induced Functional Impairment of Albumin in Oxidative”. Journal of Pharmaceutical Sciences. 106 (9): 2195–2203. doi:10.1016/j.xphs.2017.03.002. PMID 28302542.
  41. Matsuyama Y, Terawaki H, Terada T, Era S (August 2009). “Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease”. Clinical and Experimental Nephrology. 13 (4): 308–315. doi:10.1007/s10157-009-0161-y. PMID 19363646. S2CID 20886185.
  42. “Microalbumin Urine Test”. WebMD.
  43. Chaudhury C, Mehnaz S, Robinson JM, Hayton WL, Pearl DK, Roopenian DC, Anderson CL (February 2003). “The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan”. The Journal of Experimental Medicine. 197 (3): 315–322. doi:10.1084/jem.20021829. PMC 2193842. PMID 12566415.
  44. Merlot AM, Kalinowski DS, Richardson DR (2014). “Unraveling the mysteries of serum albumin-more than just a serum protein”. Frontiers in Physiology. 5: 299. doi:10.3389/fphys.2014.00299. PMC 4129365. PMID 25161624.

Further reading

External links

Globular proteins
Acute-phase proteins

Categories: 

Tags:

Leave a Reply

Your email address will not be published. Required fields are marked *

This site uses Akismet to reduce spam. Learn how your comment data is processed.