Hyperlipidemia and Tissue Contents of Nε-(Carboxymethyl)lysine in Streptozotocin Diabetes

1997 ◽  
pp. 132-139
Author(s):  
T. Niwa ◽  
T. Katsuzaki ◽  
N. Tatemichi ◽  
Y. Takei
Keyword(s):  
Streptozotocin Diabetes ◽  
Carboxymethyl Lysine ◽  
Tissue Contents

Studies on streptozotocin diabetes

Diabetes ◽  
1976 ◽  
Vol 25 (7) ◽  
pp. 595-603 ◽  
Author(s):  
O. P. Ganda ◽  
A. A. Rossini ◽  
A. A. Like
Keyword(s):  
Streptozotocin Diabetes

Intracellular enzymes of collagen biosynthesis in rat kidney in streptozotocin diabetes

Diabetes ◽  
1976 ◽  
Vol 25 (11) ◽  
pp. 1066-1070 ◽  
Author(s):  
J. Risteli ◽  
V. A. Koivisto ◽  
H. K. Akerblom ◽  
K. I. Kivirikko
Keyword(s):  
Rat Kidney ◽  
Streptozotocin Diabetes ◽  
Collagen Biosynthesis ◽  
Intracellular Enzymes

Methylglyoxal in diabetes: link to treatment, glycaemic control and biomarkers of complications

2014 ◽  
Vol 42 (2) ◽  
pp. 450-456 ◽  
Author(s):  
Paul J. Beisswenger
Keyword(s):  
Glycaemic Control ◽  
Diabetic Complications ◽  
Predictive Biomarkers ◽  
Complication Rates ◽  
Specific Chemical ◽  
End Products ◽  
Carboxymethyl Lysine ◽  
Genetic And Environmental Factors ◽  
Novel Concept ◽  
The Cost

Diabetic complications are major health problems worldwide, with the cost of caring for diabetes rising to US$245 billion in 2012 in the U.S.A. alone. It is widely recognized that non-enzymatic glycation in diabetes is a major cause of damage and dysfunction of key vascular cells. MG (methylglyoxal) is directly toxic to tissues, and is a major precursor of AGEs (advanced glycation end-products). Various propensities to diabetic complications are seen among individuals with diabetes, with accelerated rates occurring in some individuals with modest hyperglycaemia, while others never progress in spite of poor glycaemic control over many years. Since production and detoxification of MG is ultimately controlled by enzymatic mechanisms, both genetic and environmental factors could regulate tissue glycation and potentially account for these variable complication rates. Activation of pathways that determine MG levels occurs in susceptible patients, indicting an important role in pathogenesis. MG leads to formation of specific AGEs, which are likely to predict propensity to diabetic complications. We have shown recently that three specific plasma AGE biomarkers [MG-H1 (MG-derived hydroimidazolones), CEL (Nε-carboxyethyl-lysine) and CML (Nε-carboxymethyl-lysine)] predict biopsy-documented fast DN (diabetic nephropathy) progression. Since two of the predictive biomarkers are MG end-products, these outcomes support a role for MG in the development of DN. Our studies on MG and its end-products have also shown anti-complication effects of the drug metformin, which binds and inactivates MG, thus reducing MG-related AGEs. We have also shown that reducing post-meal glucose decreases MG levels, as well as levels of MG-related AGEs. Our clinical outcome studies have been based on the novel concept that the unique glycation products that we can measure reflect the activity of specific chemical pathways that are selectively activated by hyperglycaemia in patients that are inherently more susceptible to diabetic complications, and can be used to solve other diabetes-related medical questions.

Age-dependent accumulation of N.epsilon.-(carboxymethyl)lysine and N.epsilon.-(carboxymethyl)hydroxylysine in human skin collagen

Biochemistry ◽  
1991 ◽  
Vol 30 (5) ◽  
pp. 1205-1210 ◽  
Author(s):  
John A. Dunn ◽  
David R. McCance ◽  
Suzanne R. Thorpe ◽  
Timothy J. Lyons ◽  
John W. Baynes
Keyword(s):  
Human Skin ◽  
Skin Collagen ◽  
Age Dependent ◽  
Carboxymethyl Lysine

scholarly journals Development of Capture Assays for Different Modifications of Human Low-Density Lipoprotein

2005 ◽  
Vol 12 (1) ◽  
pp. 68-75 ◽  
Author(s):  
Gabriel Virella ◽  
M. Brooks Derrick ◽  
Virginia Pate ◽  
Charlyne Chassereau ◽  
Suzanne R. Thorpe ◽  
...  
Keyword(s):  
Oxidized Ldl ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Gas Chromatography Mass Spectrometry ◽  
Low Density ◽  
Modified Ldl ◽  
Capture Assay ◽  
Carboxymethyl Lysine

ABSTRACT Antibodies to malondialdehyde (MDA)-modified low-density lipoprotein (LDL), copper-oxidized LDL (oxLDL), N ε(carboxymethyl) lysine (CML)-modified LDL, and advanced glycosylation end product (AGE)-modified LDL were obtained by immunization of rabbits with in vitro-modified human LDL preparations. After absorption of apolipoprotein B (ApoB) antibodies, we obtained antibodies specific for each modified lipoprotein with unique patterns of reactivity. MDA-LDL antibodies reacted strongly with MDA-LDL and also with oxLDL. CML-LDL antibodies reacted strongly with CML-LDL and also AGE-LDL. oxLDL antibodies reacted with oxLDL but not with MDA-LDL, and AGE-LDL antibodies reacted with AGE-LDL but not with CML-LDL. Capture assays were set with each antiserum, and we tested their ability to capture ApoB-containing lipoproteins isolated from precipitated immune complexes (IC) and from the supernatants remaining after IC precipitation (free lipoproteins). All antibodies captured lipoproteins contained in IC more effectively than free lipoproteins. Analysis of lipoproteins in IC by gas chromatography-mass spectrometry showed that they contained MDA-LDL and CML-LDL in significantly higher concentrations than free lipoproteins. A significant correlation (r = 0.706, P < 0.019) was obtained between the MDA concentrations determined by chemical analysis and by the capture assay of lipoproteins present in IC. In conclusion, we have developed capture assays for different LDL modifications in human ApoB/E lipoprotein-rich fractions isolated from precipitated IC. This approach obviates the interference of IC in previously reported modified LDL assays and allows determination of the degree of modification of LDL with greater accuracy.

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