Glycated albumin (GA) and inflammation: role of GA as a potential marker of inflammation

Roohk, H. Vernon; Zaidi, Asad R.; Patel, Dhaval

doi:10.1007/s00011-017-1089-4

Cited by 24 publications

(20 citation statements)

References 49 publications

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“…Aside from blocking the IgG-FcRn interactions, there is also premise that hindering albumin binding to FcRn might also be beneficial, although the evidence for a pathological role of albumin is more ambiguous. For instance, abnormal levels of glycated albumin, observed in diabetic patients, have been associated with disease pathogenesis and tissue inflammation (287–289). Further, albumin as a carrier protein associates with many hormones, ions, metabolites and drugs, and can extend their in vivo half-life.…”

Section: Fcrn-based Therapeuticsmentioning

confidence: 99%

The Neonatal Fc Receptor (FcRn): A Misnomer?

et al. 2019

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Antibodies are essential components of an adaptive immune response. Immunoglobulin G (IgG) is the most common type of antibody found in circulation and extracellular fluids. Although IgG alone can directly protect the body from infection through the activities of its antigen binding region, the majority of IgG immune functions are mediated via proteins and receptors expressed by specialized cell subsets that bind to the fragment crystallizable (Fc) region of IgG. Fc gamma (γ) receptors (FcγR) belong to a broad family of proteins that presently include classical membrane-bound surface receptors as well as atypical intracellular receptors and cytoplasmic glycoproteins. Among the atypical FcγRs, the neonatal Fc receptor (FcRn) has increasingly gained notoriety given its intimate influence on IgG biology and its ability to also bind to albumin. FcRn functions as a recycling or transcytosis receptor that is responsible for maintaining IgG and albumin in the circulation, and bidirectionally transporting these two ligands across polarized cellular barriers. More recently, it has been appreciated that FcRn acts as an immune receptor by interacting with and facilitating antigen presentation of peptides derived from IgG immune complexes (IC). Here we review FcRn biology and focus on newer advances including how emerging FcRn-targeted therapies may affect the immune responses to IgG and IgG IC.

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Section: Fcrn-based Therapeuticsmentioning

confidence: 99%

The Neonatal Fc Receptor (FcRn): A Misnomer?

et al. 2019

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“…Serum GA can reflect short-term (2–3 weeks) mean glycemic levels [ 13 – 18 ], and the measurement of GA levels has distinctive advantages in patients with newly diagnosed DM, marked glycemic excursion, treatment adjustment, and stress [ 19 ]. Recent studies have focused on the role of GA as a direct pathological harmful factor in the development of vascular complications in DM [ 14 , 20 ]. Additionally, GA cannot only predict the development but also indicate the severity of DM complications [ 21 – 24 ].…”

Section: Discussionmentioning

confidence: 99%

“…Day et al [ 27 ] reported that the glycation reaction of GA progressed approximately 10 times faster than that of HbA 1c in a Sprague–Dawley rat model of DM. This is believed to be because when the elevated blood glucose level decreases, an unstable product of early HbA 1c through the Amadori reaction is reversibly dissociated to hemoglobin and glucose [ 28 ], whereas unstable GA produced from albumin and glucose rapidly goes through the irreversible reaction, and stable GA is produced [ 14 ]. Further studies are needed to fully elucidate the underlying mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Postload Glycated Albumin as an Alternate Measure for Diabetes Screening in a Chinese Population

Tang

et al. 2018

Journal of Diabetes Research

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In previous epidemiological screening in China, glycated albumin (GA) was mostly detected during the fasting state. This strict restriction causes some problems with diabetes screening. It is unclear if GA could help improve the efficiency of screening for diabetes for subjects who are not in the fasting state. The present study analyzed the differences between fasting and postload (30, 60, 120, and 180 min) GA levels. A total of 691 participants were enrolled in the present study. The Bland-Altman difference plots revealed that 95.4, 94.8, 93.6, and 93.9% of data points were within the limits of agreement for each time point. The receiver operating characteristic curve showed that the areas under the curve (AUC) for baseline GA and postload GA for every time point were 0.822 (95% CI 0.791–0.849), 0.821 (95% CI 0.790–0.848), 0.833 (95% CI 0.803–0.860), 0.840 (95% CI 0.811–0.867), and 0.840 (95% CI 0.810–0.867), with sensitivities of 67.5, 68.1, 69.3, 71.6, and 69.3%, respectively. There was no difference between the baseline and postload GA levels in either AUC or sensitivity (all p > 0.05). In conclusion, postload serum GA levels were in good agreement with those at baseline, and thus, it may be reasonable to employ nonfasting measurements of GA levels for diabetes screening.

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“…When talking about proteins with a slow turnover rate, attention should turn to collagen and other Extracellular Matrix components such as laminin and elastin, to the predominant eye lens protein α-crystallin [14], cartilage [15], and also to some plasma proteins such as hemoglobin [1]. However, even though long-lived proteins are more susceptible to glycation, those with a shorter half-life can also be important when dealing with inflammatory effects of AGEs, and the perfect example for this is glycated albumin, which is known to be involved in inflammatory processes leading to renal damage [16,17,18,19].…”

Section: Advanced Glycation End-products Origin Structure and Mamentioning

confidence: 99%

The Modern Western Diet Rich in Advanced Glycation End-Products (AGEs): An Overview of Its Impact on Obesity and Early Progression of Renal Pathology

et al. 2019

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Advanced glycation end-products (AGEs) are an assorted group of molecules formed through covalent bonds between a reduced sugar and a free amino group of proteins, lipids, and nucleic acids. Glycation alters their structure and function, leading to impaired cell function. They can be originated by physiological processes, when not counterbalanced by detoxification mechanisms, or derive from exogenous sources such as food, cigarette smoke, and air pollution. Their accumulation increases inflammation and oxidative stress through the activation of various mechanisms mainly triggered by binding to their receptors (RAGE). So far, the pathogenic role of AGEs has been evidenced in inflammatory and chronic diseases such as chronic kidney disease, cardiovascular disease, and diabetic nephropathy. This review focuses on the AGE-induced kidney damage, by describing the molecular players involved and investigating its link to the excess of body weight and visceral fat, hallmarks of obesity. Research regarding interventions to reduce AGE accumulation has been of great interest and a nutraceutical approach that would help fighting chronic diseases could be a very useful tool for patients’ everyday lives.

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Glycated albumin (GA) and inflammation: role of GA as a potential marker of inflammation

Cited by 24 publications

References 49 publications

The Neonatal Fc Receptor (FcRn): A Misnomer?

The Neonatal Fc Receptor (FcRn): A Misnomer?

Postload Glycated Albumin as an Alternate Measure for Diabetes Screening in a Chinese Population

The Modern Western Diet Rich in Advanced Glycation End-Products (AGEs): An Overview of Its Impact on Obesity and Early Progression of Renal Pathology

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