Protein Amino Research Articles

Molecular Docking of Shallot (Allium ascalonicum) Active Compounds to Lanosterol Enzym 14-Alpha Demethylase and Squalene Monooxygenase for Antifungi Potential Activity

<p>Shallots <em>(Allium ascalonicum</em>) are one of the important horticultural export commodities in Indonesia, but the productivity of shallots has decreased due to the attack of pathogenic fungi. This study was aimed to determine the potential of active shallot compounds as ligands for inhibiting the activity of the enzyme lanosterol 14-alpha demethylase (ID: 4LXJ) and squalene monooxygenase (ID: 6C6R) enzymes which play an important role in the biosynthesis of ergosterol or fungal cell membranes. The molecular docking used the Autodock Vina (PyRx) program, an analysis of molecule interaction used PyMol, and Discovery Studio 2019 to analyze the types of bonds between molecules. Thirty-nine ligands from shallot compounds are docked to the anti-fungal target protein. The results showed ascalonicoside A1, ascalonicoside A2, ascalonicoside B, quercetin, isorhamnetin, quercetin di glucoside, quercetin tri glucoside, ethyl palmitate and benzyl salicylate have the potential to be anti-fungal to the enzyme lanosterol 14-alpha demethylase and squalene monooxygenase enzyme that responds to the synthesis of fungi cell wall. These ligand compounds bind to the target protein's amino acid residues with hydrogen and hydrophobic bonds. This research showed that shallot was the potential to be replicated as an anti-fungus for many purposes.</p>

Inhibitory effect of LSOPC on AGEs formation and sensory quality in cookies.

At the conclusion of the Maillard reaction (MR), free amino groups of proteins, amino acids, or lipids with the carboxyl groups of reducing sugars to form stable molecules known as advanced glycation end products (AGEs), which hasten aging and may potentially be the root cause of a number of chronic degenerative diseases. According to researches, lotus seedpod oligomeric procyanidins (LSOPC), a premium natural antioxidant produced from lotus waste, can be included in cookies to improve flavor and lower the risk of illnesses linked to AGEs. In this work, we used cookies without LSOPC as a control to examine the effects of adding various concentrations of LSOPC (0, 0.05, 0.1, 0.2, and 0.4%) on the AGEs formation and the sensory quality in cookies. The amounts of AGEs and N-ε-carboxymethyl lysine (CML) decreased with the increase of LSOPC concentration, indicating that the concentration of LSOPC was positively correlated with the ability to inhibit AGEs formation. It was also demonstrated that the amount of antioxidant capacity of the cookies increased significantly with the increase of LSOPC concentration. On the other hand, the chromaticity, texture, electronic nose, and other aspects of the cookies' sensory attributes were also evaluated. The color of the cookies deepened and the flavor varied as LSOPC added content increased. The sensory quality of the cookies was examined, and the findings indicated that LSOPC would somewhat improve that quality. These findings implied that AGEs formation could be decreased in cookies while also enhancing their sensory quality by adding LSOPC.

Targeting of colorectal cancer organoids with zoledronic acid conjugated to the anti-EGFR antibody cetuximab

BackgroundAntibody-drug conjugates (ADC) are essential therapeutic options to treat solid and hematological cancers. The anti-epidermal growth factor-receptor (EGFR) antibody cetuximab (Cet) is used for the therapy of colorectal carcinoma (CRC)....

Amine-Reactive BODIPY Dye: Spectral Properties and Application for Protein Labeling.

A boron-dipyrromethene (BODIPY) derivative reactive towards amino groups of proteins (NHS-Ph-BODIPY) was synthesized. Spectroscopic and photophysical properties of amine-reactive NHS-Ph-BODIPY and its non-reactive precursor (COOH-Ph-BODIPY) in a number of organic solvents were investigated. Both fluorescent dyes were characterized by green absorption (521-532 nm) and fluorescence (538-552 nm) and medium molar absorption coefficients (46,500-118,500 M-1·cm-1) and fluorescence quantum yields (0.32 - 0.73). Solvent polarizability and dipolarity were found to play a crucial role in solvent effects on COOH-Ph-BODIPY and NHS-Ph-BODIPY absorption and emission bands maxima. Quantum-chemical calculations were used to show why solvent polarizability and dipolarity are important as well as to understand how the nature of the substituent affects spectroscopic properties of the fluorescent dyes. NHS-Ph-BODIPY was used for fluorescent labeling of a number of proteins. Conjugation of NHS-Ph-BODIPY with bovine serum albumin (BSA) resulted in bathochromic shifts of absorption and emission bands and noticeable fluorescence quenching (about 1.5 times). It was demonstrated that the sensitivity of BSA detection with NHS-Ph-BODIPY was up to eight times higher than with Coomassie brilliant blue while the sensitivity of PII-like protein PotN (PotN) detection with NHS-Ph-BODIPY and Coomassie brilliant blue was almost the same. On the basis of the molecular docking results, the most probable binding sites of NHS-Ph-BODIPY in BSA and PotN and the corresponding binding free energies were estimated.

Low Level of Advanced Glycation End Products in Serum of Patients with Allergic Rhinitis and Chronic Epstein-Barr Virus Infection at Different Stages of Virus Persistence.

Advanced glycation end products (AGEs) are formed in a nonenzymatic reaction of the reducing sugars with amino groups of proteins, lipids, and nucleic acids of different tissues and body fluids. A relatively small number of studies have been conducted on the role of AGEs in allergic inflammation. In this study, patients with allergic rhinitis (AR) were examined for the presence of Epstein-Barr virus and the content of fluorescent and nonfluorescent AGEs. We have also determined the level of a unique epitope (AGE10) which was recently identified in human serum using monoclonal antibodies against synthetic melibiose-derived AGE (MAGE). The levels of AGE10 determined with an immunoenzymatic method revealed no significant difference in the patients' blood with intermittent AR and chronic EBV persistence in the active and latent phases. It has been shown that there is a statistically significantly smaller amount of AGEs and pentosidine in groups of patients, both with and without viremia, than in healthy subjects. In turn, higher levels of immune complexes than of AGE10 were detected in the groups of patients, in contrast to the control group, which had lower levels of complexes than AGE10 concentration. In patients with active infection, there is even more complexes than of noncomplexed AGE10 antigen. The lower level of AGE in allergic rhinitis patient sera may also be due, besides complexes, to allergic inflammation continuously activating the cells, which effectively remove glycation products from the body.

A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates

Chlorogenic acid (CGA) is an ester between caffeic and quinic acid. It is found in many foods and reacts with free amino groups in proteins at alkaline pH, leading to the formation of an undesirable green pigment in sunflower seed-derived ingredients. This paper presents the biochemical characterization and application of a highly active chlorogenic acid esterase from Lactobacillus helveticus. The enzyme is one of the most active CGA esterases known to date with a Km of 0.090 mM and a kcat of 82.1 s−1. The CGA esterase is easily expressed recombinantly in E. coli in large yields and is stable over a wide range of pH and temperatures. We characterized CGA esterase’s kinetic properties in sunflower meal and demonstrated that the enzyme completely hydrolyzes CGA in the meal. Finally, we showed that CGA esterase treatment of sunflower seed meal enables the production of pale brown sunflower protein isolates using alkaline extraction. This work will allow for more widespread use of sunflower-derived products in applications where neutrally-colored food products are desired.

The OSE complotype and its clinical potential.

Cellular death, aging, and tissue damage trigger inflammation that leads to enzymatic and non-enzymatic lipid peroxidation of polyunsaturated fatty acids present on cellular membranes and lipoproteins. This results in the generation of highly reactive degradation products, such as malondialdehyde (MDA) and 4-hydroxynonenal (4-HNE), that covalently modify free amino groups of proteins and lipids in their vicinity. These newly generated neoepitopes represent a unique set of damage-associated molecular patterns (DAMPs) associated with oxidative stress termed oxidation-specific epitopes (OSEs). OSEs are enriched on oxidized lipoproteins, microvesicles, and dying cells, and can trigger sterile inflammation. Therefore, prompt recognition and removal of OSEs is required to maintain the homeostatic balance. This is partially achieved by various humoral components of the innate immune system, such as natural IgM antibodies, pentraxins and complement components that not only bind OSEs but in some cases modulate their pro-inflammatory potential. Natural IgM antibodies are potent complement activators, and 30% of them recognize OSEs such as oxidized phosphocholine (OxPC-), 4-HNE-, and MDA-epitopes. Furthermore, OxPC-epitopes can bind the complement-activating pentraxin C-reactive protein, while MDA-epitopes are bound by C1q, C3a, complement factor H (CFH), and complement factor H-related proteins 1, 3, 5 (FHR-1, FHR-3, FHR-5). In addition, CFH and FHR-3 are recruited to 2-(ω-carboxyethyl)pyrrole (CEP), and full-length CFH also possesses the ability to attenuate 4-HNE-induced oxidative stress. Consequently, alterations in the innate humoral defense against OSEs predispose to the development of diseases associated with oxidative stress, as shown for the prototypical OSE, MDA-epitopes. In this mini-review, we focus on the mechanisms of the accumulation of OSEs, the pathophysiological consequences, and the interactions between different OSEs and complement components. Additionally, we will discuss the clinical potential of genetic variants in OSE-recognizing complement proteins – the OSE complotype - in the risk estimation of diseases associated with oxidative stress.

Non-lysine ubiquitylation: Doing things differently.

The post-translational modification of proteins with ubiquitin plays a central role in nearly all aspects of eukaryotic biology. Historically, studies have focused on the conjugation of ubiquitin to lysine residues in substrates, but it is now clear that ubiquitylation can also occur on cysteine, serine, and threonine residues, as well as on the N-terminal amino group of proteins. Paradigm-shifting reports of non-proteinaceous substrates have further extended the reach of ubiquitylation beyond the proteome to include intracellular lipids and sugars. Additionally, results from bacteria have revealed novel ways to ubiquitylate (and deubiquitylate) substrates without the need for any of the enzymatic components of the canonical ubiquitylation cascade. Focusing mainly upon recent findings, this review aims to outline the current understanding of non-lysine ubiquitylation and speculate upon the molecular mechanisms and physiological importance of this non-canonical modification.

D-ribose-mediated glycation of fibrinogen: Role in the induction of adaptive immune response

A nonenzymatic reaction between reducing sugars and amino groups of proteins results in the formation of advanced glycation end products, which are linked to a number of chronic progressive diseases with macro- and microvascular complications. In this research, we sought to ascertain the immunological response to d-ibose-glycated fibrinogen. New Zealand White female rabbits were immunized with native and d-ribose-glycated (Rb-gly-Fb) fibrinogen and used for studying the immunological response. Serum from these rabbits analyzed using direct binding and competitive inhibition ELISA was found to contain a high titer of antibodies against Rb-gly-Fb; Rb-gly-Fb was much more immunogenic than its native form. The IgG against Rb-gly-Fb (Rb-gly-Fb-IgG) was highly specific against the immunogenic protein. Moreover, histopathology and immunofluorescence studies revealed the deposition of the Rb-gly-Fb-IgG immune complex in the glomerular basement membrane of the kidneys of immunized rabbits. Furthermore, immunization with Rb-gly-Fb increased the expression of genes encoding proinflammatory cytokines, tumour necrosis factor α, interleukin-6, interleukin-1β, and interferon-gamma, which is indicative of increased inflammation and the antigenic role of Rb-gly-Fb in provoking an immune response.

The effects of conjugation of walnut protein isolate with polyphenols on protein solubility, antioxidant activity, and emulsifying properties

Alkaline-extracted walnut protein isolate (AWPI) shows poor solubility in aqueous solutions, resulting in relatively low emulsion capacity. This work investigated the influence of ellagic acid (EA) or epigallocatechin-3-gallate (EGCG) conjugation on the solubility and emulsifying properties of AWPI. The increase in polyphenol content and decrease in free amino and thiol groups of walnut proteins confirmed successful conjugation. AWPI polyphenol conjugates showed significantly reduced surface hydrophobicity, greatly enhanced surface charge, and consequently improved solubility. Circular dichroism (CD) results indicated that the polyphenol-conjugated AWPI contained relatively higher α-helical and lower β-sheet contents than AWPI. The antioxidant capacity of the polyphenol-conjugated AWPI was significantly enhanced. Additionally, polyphenol conjugation resulted in decreased mean particle sizes and increased surface charges of the walnut protein-covered oil droplets. The emulsions stabilized by AWPI-polyphenol conjugates were relatively more stable over a range of pH values (7.0–11.0) and thermal treatments (25 °C–90 °C). Moreover, they exhibited greater storage stability than those stabilized by unmodified AWPI.

Chromatographic separation of glycated peptide isomers derived from glucose and fructose

Amino groups in proteins can react with aldehyde groups in aldoses or keto groups in ketoses, e.g., d-glucose and d-fructose, yielding Schiff bases that rearrange to more stable Amadori and Heyns products, respectively. Analytical strategies to identify and quantify each glycation product in the presence of the corresponding isomer are challenged by similar physicochemical properties, impeding chromatographic separations, and by identical masses including very similar fragmentation patterns in tandem mass spectrometry. Thus, we studied the separation of seven peptide families, each consisting of unmodified, glucated, and fructated 15mer to 22mer peptides using reversed-phase (RP) and hydrophilic interaction chromatography (HILIC). In RP-HPLC using acidic acetonitrile gradients, unglycated peptides eluted ~ 0.1 to 0.8 min after the corresponding glycated peptides with four of seven peptides being baseline separated. Isomeric glucated and fructated peptides typically coeluted, although two late-eluting peptides were partially separated. Neutral eluents (pH 7.2) improved the chromatographic resolution (Rs), especially in the presence of phosphate, providing good and often even baseline separations for six of the seven isomeric glycated peptide pairs with fructated peptides eluting earlier (Rs = 0.7 to 1.5). Some glucated and unmodified peptides coeluted, but they can be distinguished by mass spectrometry. HILIC separated glycated and unmodified peptides well, whereas glucated and fructated peptides typically coeluted. In conclusion, HILIC efficiently separated unmodified and the corresponding glycated peptides, while isomeric Amadori and Heyns peptides were best separated by RP-HPLC using phosphate buffered eluents.

Blood and faecal biomarkers to assess dietary energy, protein and amino acid efficiency of utilization by growing and finishing pigs

BackgroundDiet evaluation and optimization is a slow and expensive process and it is not possible to do it at a farm level. This study aimed to use the blood serum metabolite (BSM) and faecal volatile fatty acid (VFA) profiles as potential biomarkers to identify changes in protein, amino acid and energy dietary content in growing and finishing pig diets at farm level.ResultsTwo studies were conducted. The first study (S1) included 20 pens of 11 pigs (87.0 ± 4.10 kg; 18 weeks old) assigned to 5 diets: control (C1), high or low crude protein (HP1 and LP1, respectively), and high or low net energy (HE1 and LE1, respectively). The second study (S2) included 28 pens of 11 pigs (41.3 ± 2.60 kg; 12 weeks old) assigned to 7 diets: control (C2), high or low crude protein (HP2 and LP2, respectively), high or low amino acid (HA2 and LA2, respectively), and high or low net energy (HE2 and LE2, respectively). Pigs were followed for 10 (S1) and 20 (S2) days, and blood and faecal samples were collected at 20 (S1) and 14 (S2) weeks of age. Data were analysed using general linear models and receiver operating characteristic curve analysis. Urea nitrogen showed the best results as a biomarker. Urea nitrogen was higher in pigs fed high protein diets, HP1 (13.6 ± 0.95 mg/dL) and HP2 (11.6 ± 0.61), compared to those fed low protein diets, LP1 (6.0 ± 0.95) and LP2 (5.2 ± 0.61; P < 0.001), showing good discrimination ability (Area under the curve (AUC) = 98.4 and 100%, respectively). These differences were not observed between diets LA2 (6.5 ± 0.61) and HA2 (8.7 ± 0.61; P > 0.05; AUC = 71.9%), which were formulated based on the ideal protein profile but with no excess of protein. Creatinine, triglycerides, branched-chain fatty acids, albumin, propionic acid, and cholesterol showed differences between at least 2 diets but only in one of the studies.ConclusionsUrea nitrogen showed high accuracy to detect excess of crude protein in growing and finishing pig diets. Other biomarkers like BCFA showed promising results and need to be further studied.

The effect of dietary protein level and amino acid supplementation on the Nile tilapia (Oreochromis niloticus) nursering performance under biofloc system conditions at a cold suboptimal water temperature

The effect of dietary protein level and amino acid supplementation on the Nile tilapia (Oreochromis niloticus) nursering performance under biofloc system conditions at a cold suboptimal water temperature

Nanomechanical and Nonlinear Optical Properties of Glycated Dental Collagen

Nonenzymatic glycation is a multistep, slow reaction between reducing sugars and free amino groups of long-lived proteins, which affects the structural and mechanical properties of collagen-rich tissues via accumulation of advanced glycation end products (AGEs). Dental collagen is exposed to glycation as part of the natural aging process. However, in case of chronically high blood glucose, the process can be accelerated, resulting in premature stiffening of dentin, leading to tooth fragility. The molecular mechanisms whereby collagen glycation evokes the loss of mechanical stability in teeth are currently unknown. In this study, we used 2-photon and atomic force microscopies to correlate structural and mechanical changes in dental collagen induced by in vitro glycation. Young tooth samples were demineralized and cut longitudinally into 30-µm sections, then artificially glycated in 0.5 M ribose solution for 10 wk. Two-photon microscopy analysis showed that both the autofluorescence and second harmonic–generated (SHG) signal intensities of glycated samples were significantly greater than those of the controls. Regarding the structural alteration of individual collagen fibers, a remarkable increase could be measured in fiber length of ribose-treated sections. Furthermore, nanoindentation of intertubular dentin regions revealed significantly higher stiffness in the ribose-treated samples, which points at a significant accumulation of AGEs. Thus, collagen glycation occurring during sustained exposure to reducing sugars leads to profound structural and mechanical changes in dentin. Besides the numerous oral complications associated with type 2 diabetes, the premature structural and mechanical deterioration of dentin may also play an important role in dental pathology.

Receptor of advanced glycation end product (RAGE) polymorphism and oxidative status in Hashimoto’s thyroiditis in Egyptian female patients: case control study

BackgroundHashimoto's thyroiditis is the most widespread autoimmune illness targeting a specific organ. "Redox homeostasis" is achieved when the production of Reactive Oxygen Species and their elimination are in balance. Advanced glycation end products (AGEs) are formed when glucose and/or α-oxaloaldehydes react non-enzymatically with the amino groups of lipids, proteins, and DNA. Nowadays, many studies are concerned with AGEs, the polymorphisms of their receptors, and their association with increased risk of HT. However, few studies investigated the role of receptors of advanced glycation end product (RAGE) SNP in Egyptian females.ObjectiveThe goals of this investigation were to ascertain whether oxidative stress plasma malondialdehyde (MDA) and total antioxidant capacity (TAC) were associated with HT, in addition, to assess the association of RAGE polymorphisms (− 374 T > A and the − 429 T > C and Gly82Ser) with HT.Subject and methods.Our case–control study has 80 patients enrolled who have newly been diagnosed with HT and 80 age and sex-matched healthy female controls. Each participant underwent a thorough medical history, physical examination, and laboratory investigations, which included Genotyping of RAGE Gly82Ser, − 374 T > A and − 429 T > C using polymerase chain reaction-restriction fragment length polymorphisms (PCR–RFLP).ResultsChi-square revealed a significant association regarding the distribution of RAGE (− 374 T < C) genotypes TT and CC between patients and control (P = 0.04). Non-significant associations regarding the distribution of Gly82Ser genotypes Gly/Gly, Gly/Ser, Ser/Ser were found between patients and control (P = 0.5), and non-significant associations related to − 429 T > C gene polymorphism were revealed. In addition, patients with HT had higher MDA and lower TCA compared with controls.ConclusionThe elevated MDA and decreased TAC as an antioxidant may be one of several risk factors associated with the prevalence of HT in individuals with the − 429 T > C RAGE mutation polymorphism that is associated with an increased risk of HT in Egyptian females.

Keluwih (Artocarpus camansi Blanco): Potential utilization as foodstuff and its bioactivity

Artocarpus camansi (AC) has been long used by Indonesian local people as food and traditional medicine. This study aims to explain the relationship between the use of AC as a food ingredient and traditional medicine and its bioactivity. The method used in writing this article is a literature study on various scientific articles published online at Google Scholar using AC, uses AC, and AC bioactivities. The results obtained were synthesized so as to be able to explain the botany, utilization and bioactivity of AC in a comprehensive manner. The fruits of AC have been used as a vegetable ingredient, baby food and has the potential to be developed as an economic commodity. The use of AC as a food ingredient is related to its nutritional content. The seeds of AC are rich in protein carbohydrates, amino acids, fats and minerals (phosphorus, potassium, sodium, iron, copper). As a traditional medicine, AC is used to treat dysentery, malaria, related to its bioactivity as an anti-microbial, anti-malarial, anti-diabetic-mellitus, anti-cancer. The flavonoids of AC extract associated with antimalarial and anti-cancer activity, while -sitosterol propionate was associated with anti-diabetes mellitus activity. AC is very potential to be developed as an alternative food ingredient as well as anti-diabetes mellitus.

L-theanine protects rat kidney from D-galactose-induced injury via inhibition of the AGEs/RAGE signaling pathway

As the irreversible products of the non-enzymatic reduction of sugars and the amino groups of proteins or peptides, advanced glycation end products (AGEs) are metabolized and excreted via the kidneys. However, if AGEs are not metabolized, they are deposited in the kidneys and bind to AGE receptors (RAGE), which can induce various pathological changes, including oxidative stress, apoptosis, and inflammation. This study used the D-galactose (DG)-induced rat model to explore the potential role and mechanism of L-theanine in inhibiting AGEs/RAGE-related signaling pathways in renal tissues. L-theanine increased the activities of glutathione peroxidase (GSH-Px) and total antioxidant capacity (T-AOC) while downregulating the contents of malondialdehyde (MDA) and AGEs in renal tissues induced by DG (P < 0.05). By inhibiting the upregulation of RAGE protein expression attributed to AGEs accumulation (P < 0.05), L-theanine downregulated phosphorylated nuclear factor (p–NF–κB (p65)), Bax, and cleaved-caspase-3 expression and increased Bcl-2 protein expression (P < 0.05), thereby alleviating the oxidative stress damage and reducing the inflammation and cell injury induced by DG. In addition, the Congo red staining section of renal tissue also showed that the natural product L-theanine can protect against AGEs-induced renal damage in DG-induced rat model.

Experience of application of an alternative source of protein for feeding of broiler chickens

Proteins are obligated components of cells of any living organism that perform vital functions: catalytic, regulatory, transport, bioenergetic, protective against infections and other stress factors, structural, spare, etc. The purpose of the work was to evaluate the effect of the feed additive „Feed bioprotein“ in the form of powder on the main economic indicators characterizing the efficiency of broiler chickens rearing. „Feed bioprotein“ is a high-protein feed additive and is a biomass of inactivated methanassimilating bacteria Methylococcus capsulatus. The high content of protein and essential amino acids in the composition of this feed additive allows it to be introduced into the feed including for broiler chickens to replace other high-protein components such as fish and meat and bone meal, soy and sunflower meal. When conducting a production experiment on broiler chickens in the cross Ross 308, feed which was used to feed the poultry of the experimental groups, in which a feed additive was introduced, both in the minimum and maximum dosage recommended by the manufacturer for this species of animals. Broiler chickens of the control group have been received feed prepared according to a standard recipe. At the end of the 41 day rearing cycle in the experimental groups, the average daily gain in live weight exceeded the results of the control group by 2,6–5,1 %, feed conversion was by 2,3–3,4 % higher, and poultry livability was by 2 abs.% higher than in the control group. At the same time, higher rates have been observed in the group where the feed additive “Feed bioprotein” was used in the maximum dosage.

Proteins in human body fluids contain in vivo antigen analog of the melibiose-derived glycation product: MAGE

Melibiose-derived AGE (MAGE) is an advanced glycation end-product formed in vitro in anhydrous conditions on proteins and protein-free amino acids during glycation with melibiose. Our previous studies revealed the presence of MAGE antigen in the human body and tissues of several other species, including muscles, fat, extracellular matrix, and blood. MAGE is also antigenic and induces generation of anti-MAGE antibody. The aim of this paper was to identify the proteins modified by MAGE present in human body fluids, such as serum, plasma, and peritoneal fluids. The protein-bound MAGE formed in vivo has been isolated from human blood using affinity chromatography on the resin with an immobilized anti-MAGE monoclonal antibody. Using mass spectrometry and immunochemistry it has been established that MAGE epitope is present on several human blood proteins including serum albumin, IgG, and IgA. In serum of diabetic patients, mainly the albumin and IgG were modified by MAGE, while in healthy subjects IgG and IgA carried this modification, suggesting the novel AGE can impact protein structure, contribute to auto-immunogenicity, and affect function of immunoglobulins. Some proteins in peritoneal fluid from cancer patients modified with MAGE were also observed and it indicates a potential role of MAGE in cancer.

Are Inflamed Periodontal Tissues Endogenous Source of Advanced Glycation End-Products (AGEs) in Individuals with and without Diabetes Mellitus? A Systematic Review.

Advanced glycation end-products (AGEs) are heterogeneous compounds formed when excess sugars condense with the amino groups of nucleic acids and proteins. Increased AGEs are associated with insulin resistance and poor glycemic control. Recently, inflamed periodontal tissues and certain oral bacteria were observed to increase the local and systemic AGE levels in both normoglycemic and hyperglycemic individuals. Although hyperglycemia induced AGE and its effect on the periodontal tissues is known, periodontitis as an endogenous source of AGE formation is not well explored. Hence, this systematic review is aimed to explore, for the first time, whether inflamed periodontal tissues and periodontal pathogens have the capacity to modulate AGE levels in individuals with or without T2DM and how this affects the glycemic load. Six electronic databases were searched using the following keywords: (Periodontitis OR Periodontal disease OR Periodontal Inflammation) AND (Diabetes mellitus OR Hyperglycemia OR Insulin resistance) AND Advanced glycation end products. The results yielded 1140 articles, of which 13 articles were included for the review. The results showed that the mean AGE levels in gingival crevicular fluid was higher in individuals with diabetes mellitus and periodontitis (521.9 pg/mL) compared to healthy individuals with periodontitis (234.84 pg/mL). The serum AGE levels in normoglycemic subjects having periodontitis was higher compared to those without periodontitis (15.91 ng/mL vs. 6.60 ng/mL). Tannerella forsythia, a common gram-negative anaerobe periodontal pathogen in the oral biofilm, was observed to produce methylglyoxal (precursor of AGE) in the gingival tissues. Increased AGE deposition and activate of AGE receptors was noted in the presence of periodontitis in both normoglycemic and hyperglycemic individuals. Hence, it can be concluded that periodontitis can modulate the local and systemic levels of AGE levels even in absence of hyperglycemia. This explains the bidirectional relationship between periodontitis and development of prediabetes, incident diabetes, poor glycemic control, and insulin resistance.