Influence ofL-arginine on glucose mediated collagen cross link precursors in patients with diabetes mellitus

Lubec, Gert; Vierhapper, H; Bailey, Allen J.; Damjancic, P.; Fasching, Peter; Sims, TJ; Kampel, D.; Popow, Christian; Bartosch, Birke

doi:10.1007/bf00808093

Cited by 12 publications

(2 citation statements)

References 14 publications

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“…For this reason, a nucleophilic hydrazine compound, aminoguanidine (a guanidine group-containing primary amine), has been devised as a prophylactic blocker of the initial glycation reaction between MG and proteins and has been found to be effective in preventing both the formation of glucose-derived advanced nonenzymatic glycosylation products and the formation of collagen cross-links in vitro [2,8]. Along the same vein, a high dose of L-arginine, a guanidine group-containing dibasic amino acid, has also been suggested as a prophylactic blocker of the initial glycation reaction between MG and protein [9,12]. Although the formation of a blue fluorescent pyrimidine, argpyrimidine, derived from the reaction of MG and Larginine, has been identified, the question of whether or not any harmful by-products are derived from this glycation reaction has never been investigated.…”

Section: Discussionmentioning

confidence: 99%

Evidence that High-Dose <i>L</i>-Arginine May Be Inappropriate for Use by Diabetic Patients as a Prophylactic Blocker of Methylglyoxal Glycation

Tsai¹,

Pan²,

Lee³

et al. 2004

J Biomed Sci

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Previous reports have suggested that high-dose L-arginine could be used in diabetic patients as a prophylactic blocker for the initial glycation reaction of proteins by methylglyoxal (MG), a reactive dicarbonyl compound of glucose metabolism. Here, we present several lines of evidence to substantiate that this prophylactic intervention may be inappropriate and should be used with care. First, we demonstrated that when various concentrations of L-arginine (2.0–8.0 mM) were added to a fixed concentration of MG (1.56 µM) in a buffered lucigenin solution, dose-dependent generation of superoxide anion (O^–₂)-mediated ultraweak chemiluminescence (uwCL) occurs. The suppression of uwCL generation by exogenously added superoxide dismutase further substantiated that the interaction between MG and L-arginine generated O^–₂. This phenomenon can also be demonstrated in a serum-based system. Furthermore, when a fixed concentration of L-arginine (8.0 mM) was added exogenously to a group of sera obtained from either diabetic patients (n = 10) or their matched nondiabetic controls (n = 10), a marked discrepancy in the generation of O^–₂-mediated uwCL could be demonstrated (12,534 ± 3,147 vs. 950 ± 350 counts; p < 0.001). Taken together, this evidence demonstrates that the appropriateness of using high-dose L-arginine for prophylactic measures in diabetic patients may be questioned, because the inhibition of the glycation reaction between MG and proteins by high-dose L-arginine unexpectedly produces plethoric O^–₂ as a by-product, which may subsequently aggravate the preexisting oxidative stress status of diabetic patients.

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Section: Discussionmentioning

confidence: 99%

Evidence that High-Dose <i>L</i>-Arginine May Be Inappropriate for Use by Diabetic Patients as a Prophylactic Blocker of Methylglyoxal Glycation

Tsai¹,

Pan²,

Lee³

et al. 2004

J Biomed Sci

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“…As an increase in MG concentration in blood samples of diabetic patients correlates with the development of diabetic complications [28], high-dose L-arginine has been suggested as an agent to scavenge MG [25]. As an increase in MG concentration in blood samples of diabetic patients correlates with the development of diabetic complications [28], high-dose L-arginine has been suggested as an agent to scavenge MG [25].…”

Section: L-arginine As a Prophylactic Blocker Of Methylglyoxal In Diamentioning

confidence: 99%

Biomedical vignette

2004

J Biomed Sci

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L-Arginine inhibits in vitro nonenzymatic glycation and advanced glycosylated end product formation of human serum albumin

et al. 1996

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L-Arginine (Arg) has a structure similar to that of aminoguanidine (AG) and may inhibit glycation and advanced glycosylated end product (AGE) formation. Human serum albumin (HSA) (100mg/ml) was incubated for 2 weeks with glucose (200mM) at 37°C or with glucose and equimolar concentrations of Arg, N-α-acetyl Arg, or AG with or without 25mM diethylenetriaminepentaacetic acid (DTPA). In the absence of DTPA, electrospray ionization mass spectrometry showed a 70% reduction of covalently bound glucose in the presence of Arg and a 30% reduction with AG. Digestibility by trypsin of HSA incubated with glucose and Arg was similar to that of HSA incubated alone. This suggests less covalent modification of HSA in the presence of Arg as compared with the absence of Arg. When incubations contained DTPA, autoradiography showed less(14)C labeling of HSA subunits in the presence of Arg and AG. When theα-amino group of Arg was blocked with an acetyl group, labeling was similar to that of HSA incubated with glucose, suggesting involvement of theα-amino group in the inhibition. Fluorescence of HSA at ex370 and em440 was reduced with Arg, but AG was more effective than Arg. These results suggest that Arg, like AG, can inhibit glycation and AGE formation.

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Influence ofL-arginine on glucose mediated collagen cross link precursors in patients with diabetes mellitus

Cited by 12 publications

References 14 publications

Evidence that High-Dose <i>L</i>-Arginine May Be Inappropriate for Use by Diabetic Patients as a Prophylactic Blocker of Methylglyoxal Glycation

Evidence that High-Dose <i>L</i>-Arginine May Be Inappropriate for Use by Diabetic Patients as a Prophylactic Blocker of Methylglyoxal Glycation

Biomedical vignette

L-Arginine inhibits in vitro nonenzymatic glycation and advanced glycosylated end product formation of human serum albumin

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