Advanced glycation endproducts induce changes in glucose consumption, lactate production, and ATP levels in SH-SY5Y neuroblastoma cells by a redox-sensitive mechanism. Advanced glycation endproducts (AGEs) accumulate on long-lived proteins, including beta-amyloid plaques in Alzheimer's disease. They are suggested to contribute to neuronal dysfunction and cell death. A recent study at Neuroimmunological Cell Biology Unit, Leipzig, Germany investigated the effects of a model AGE upon glucose metabolism and energy production in a neuroblastoma cell line. AGEs decrease cellular ATP levels and increase glucose consumption and lactate production. All of the AGE-induced metabolic changes can be attenuated by antioxidants such as (R+)-alpha-lipoic acid and 17beta-estradiol. These antioxidants may become useful drugs against (AGE-mediated) effects in neurodegeneration through their positive effects on cellular energy metabolism. Reaction of amino groups in protein with glucose leads to the formation of advanced glycation end products (AGE) through the early products such as Schiff base and Amadori rearrangement products. Recent immunological studies using anti-AGE antibody demonstrated the presence of AGE-modified proteins in several human tissues:(i) human lens (non-diabetic and non-cataractous), (ii) renal proximal tubules in patients with diabetic nephropathy and chronic renal failure, (iii) diabetic retina, (iv) peripheral nerves of diabetic neuropathy, (v) atherosclerotic lesions of arterial walls, (vi) b2-microglobulin forming anyloid fibrils in patients with hemodialysis-related amyloidosis, (vii) senile plaques of patients with Alzheimer disease, (viii) peritoneum of CAPD patients, (ix) skin elastin in actinic elastosis, and (x) ceroid/lipofusion deposits. These results suggest a potential role of AGE-modification in normal aging as well as age-enhanced disease processes.
Applications:
Suitable for use in ELISA. Other applications not tested.
Recommended Dilution:
ELISA: 1:1000
Optimal dilutions to be determined by the researcher.
Storage and Stability:
Lyophilized powder may be stored at 4 degrees C for short-term only. Reconstitute to nominal volume by adding sterile 40-50% glycerol and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.