Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human monocytic THP-1 cells induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts

Abordo, Evelyn A.; Westwood, Marie; Thornalley, Paul J.

doi:10.1016/0165-2478(96)02601-6

Cited by 39 publications

(16 citation statements)

References 32 publications

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“…Wound healing is a multifactorial process involving inflammation, tissue remodeling, and restoration of healthy tissue. AGE are shown to regulate a variety of inflammatory cell responses and growth-promoting events, which to a certain extent occur normally during wound healing (5,29 -32 which could in turn impair normal cellular functions and wound tissue remodeling (5,(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33). Thus, diabetic H-AGE-fed mice healed slowly with thicker scars and with a persistent, nonresolving inflammatory infiltrate.…”

Section: Discussionmentioning

confidence: 99%

Adverse Effects of Dietary Glycotoxins on Wound Healing in Genetically Diabetic Mice

et al. 2003

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Advanced glycoxidation end products (AGEs) are implicated in delayed diabetic wound healing. To test the role of diet-derived AGE on the rate of wound healing, we placed female db/db (؉/؉) (n ‫؍‬ 55, 12 weeks old) and age-matched control db/db (؉/؊) mice (n ‫؍‬ 45) on two diets that differed only in AGE content (high [H-AGE] versus low [L-AGE] ratio, 5:1) for 3 months. Full-thickness skin wounds (1 cm) were examined histologically and for wound closure. Serum 24-h urine and skin samples were monitored for N ⑀ -carboxymethyl-lysine and methylglyoxal derivatives by enzyme-linked immunosorbent assays. L-AGE-fed mice displayed more rapid wound closure at days 7 and 14 (P < 0.005) and were closed completely by day 21 compared with H-AGE nonhealed wounds. Serum AGE levels increased by 53% in H-AGE mice and decreased by 7.8% in L-AGE mice (P < 0.04) from baseline. L-AGE mice wounds exhibited lower skin AGE deposits, increased epithelialization, angiogenesis, inflammation, granulation tissue deposition, and enhanced collagen organization up to day 21, compared with H-AGE mice. Reepithelialization was the dominant mode of wound closure in H-AGE mice compared with wound contraction that prevailed in L-AGE mice. Thus, increased diet-derived AGE intake may be a significant retardant of wound closure in diabetic mice; dietary AGE restriction may improve impaired diabetic wound healing. Diabetes 52:2805-2813, 2003 W ound healing is impaired in diabetes and constitutes a major cause for increased morbidity and mortality in patients with diabetes (1). The majority of nonhealing wounds often lead to amputation. The percentage of amputees increases with age as do the direct costs of their care, rehabilitation, and lost productivity (2) The exact cellular and molecular mechanisms underlying the pathogenesis of this complication are not fully elucidated (3,4). However, a number of hyperglycemiadependent factors have been identified, including the progressive accumulation of advanced glycation end products (AGEs) (5).Two well characterized compounds, N ⑀ -carboxymethyllysine (CML) and methylglyoxal (MG), derivatives of glucoseprotein or glucose-lipid interactions, serve as markers for AGE in a wide range of disorders related to diabetes, renal failure, and aging (6 -8). According to recent observations, AGEs can be introduced in the body by exogenous sources such as diet and possibly in amounts that exceed those caused by hyperglycemia alone. A direct correlation is shown between the amount of AGEs consumed and that found in the circulation (9,10). In vitro data show that food-derived AGEs, which include CML and MG derivatives, can mimic the actions of endogenously formed AGEs and can induce intracellular oxidative stress and inflammatory cell activation, in a manner reversible by antioxidants or anti-AGE agents (11). Animal studies have revealed a significant contribution to the total AGE pool and related pro-oxidant or proinflammatory processes by dietary AGE intake, including tissue damage; this seems to be preventable by restric...

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Section: Discussionmentioning

confidence: 99%

Adverse Effects of Dietary Glycotoxins on Wound Healing in Genetically Diabetic Mice

et al. 2003

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“…Pro-inflammatory cytokines (IL- 6, TNF-α), as well as endotoxins via TLR4, participate in the development of IR by stimulating hepatic glucose production [86] and altering insulin signalling [87]. These cytokines activate numerous kinases that inhibit insulin signal transduction [88-91].…”

Section: Why Does Glycaemia Finally Increase During Acute Injury?mentioning

confidence: 99%

Bench-to-bedside review: Glucose and stress conditions in the intensive care unit

2010

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The physiological response to blood glucose elevation is the pancreatic release of insulin, which blocks hepatic glucose production and release, and stimulates glucose uptake and storage in insulin-dependent tissues. When this first regulatory level is overwhelmed (that is, by exogenous glucose supplementation), persistent hyperglycaemia occurs with intricate consequences related to the glucose acting as a metabolic substrate and as an intracellular mediator. It is thus very important to unravel the glucose metabolic pathways that come into play during stress as well as the consequences of these on cellular functions. During acute injuries, activation of serial hormonal and humoral responses inducing hyperglycaemia is called the 'stress response'. Central activation of the nervous system and of the neuroendocrine axes is involved, releasing hormones that in most cases act to worsen the hyperglycaemia. These hormones in turn induce profound modifications of the inflammatory response, such as cytokine and mediator profiles. The hallmarks of stress-induced hyperglycaemia include 'insulin resistance' associated with an increase in hepatic glucose output and insufficient release of insulin with regard to glycaemia. Although both acute and chronic hyperglycaemia may induce deleterious effects on cells and organs, the initial acute endogenous hyperglycaemia appears to be adaptive. This acute hyperglycaemia participates in the maintenance of an adequate inflammatory response and consequently should not be treated aggressively. Hyperglycaemia induced by an exogenous glucose supply may, in turn, amplify the inflammatory response such that it becomes a disproportionate response. Since chronic exposure to glucose metabolites, as encountered in diabetes, induces adverse effects, the proper roles of these metabolites during acute conditions need further elucidation.

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“…A few MG-derived modifications have been defined chemically. Binding of MG-modified proteins to receptors on macrophages (37) and monocytic (THP-1) cells can induce cytokines such as interleukin-1␤ (38) and monocyte-macrophage colony-stimulating factor (39). We reported formation of an MG-derived lysine-lysine cross-link in proteins and showed that it could be formed in vivo (40).…”

mentioning

confidence: 94%

Immunological Evidence for Methylglyoxal-derived Modifications in vivo

Shamsi¹,

Partal²,

Sady³

et al. 1998

Journal of Biological Chemistry

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The Maillard reaction, a non-enzymatic reaction of ketones and aldehydes with amino groups of proteins, contributes to the aging of proteins and to complications associated with diabetes. Methylglyoxal (MG) is a 2-oxoaldehyde derived from glycolytic intermediates and produced during the Maillard reaction. We reported previously the formation of a lysine-lysine protein crosslinking structure (imidazolysine) and a fluorescent arginine modification (argpyrimidine) from the Maillard reaction of MG. Here we show that rabbit antibodies to MG-modified ribonuclease A identify proteins modified by the Maillard reaction of glucose, fructose, ribose, glyceraldehyde, glyoxal, ascorbate, and ascorbate oxidation products (dehydroascorbate, 2,3-diketogulonate, L-xylosone, and L-threose) in addition to those modified by MG. The antibody recognized imidazolysine and argpyrimidine and a glyoxal-derived lysine-lysine cross-link. It did not react with N⑀-carboxymethyllysine. Incubations with amino acids revealed strongest reactivity with N␣-tbutoxycarbonylarginine and MG, and we identified argpyrimidine as one of the epitopes from this incubation mixture. Serum proteins from human diabetics reacted more strongly with the antibody than those from normal individuals, and the levels correlated with glycemic control. Collagen from human corneas contained MG-derived modifications, with those from older subjects containing higher levels of modified proteins than those from younger ones. An immunoaffinity-purified antibody showed higher reactivity with old corneas than with younger ones and localized the antigens primarily within the stromal region of the cornea. These results confirm reported MG-derived modifications in tissue proteins and show that dicarbonyl-mediated protein modification occurs during Maillard reactions in vivo.

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Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human monocytic THP-1 cells induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts

Cited by 39 publications

References 32 publications

Adverse Effects of Dietary Glycotoxins on Wound Healing in Genetically Diabetic Mice

Adverse Effects of Dietary Glycotoxins on Wound Healing in Genetically Diabetic Mice

Bench-to-bedside review: Glucose and stress conditions in the intensive care unit

Immunological Evidence for Methylglyoxal-derived Modifications in vivo

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