In vitro Yb,Er:Glass laser hydroacoustic processing of human cataract eye lens: influence of pulse structure on removal efficiency

2019 ◽  
Author(s):  
Andrey V. Belikov ◽  
Sergey V. Gagarsky ◽  
Andrey N. Sergeev ◽  
Sergey N. Smirnov ◽  
Alexey M. Zagorulko
Keyword(s):  
Removal Efficiency ◽  
Eye Lens ◽  
Pulse Structure

In-vitro Prevention of Cataract by Ginseng on Isolated Goat Eye Lens

2012 ◽  
Vol 2 (2) ◽  
pp. 40-43
Author(s):  
Nithya S ◽  
Sumadhuri Anbu ◽  
Sumithra M
Keyword(s):  
Eye Lens

In vitro uptake of ascorbic acid by the guinea pig eye lens

1970 ◽  
Vol 9 (2) ◽  
pp. 175-180 ◽  
Author(s):  
R.E. Hughes ◽  
R.J. Hurley
Keyword(s):  
Ascorbic Acid ◽  
Guinea Pig ◽  
Eye Lens ◽  
In Vitro Uptake

In vivo, Ex Vivo, and In Vitro Approaches to Study Intermediate Filaments in the Eye Lens

2016 ◽  
pp. 581-611 ◽  
Author(s):  
Miguel Jarrin ◽  
Laura Young ◽  
Weiju Wu ◽  
John M. Girkin ◽  
Roy A. Quinlan
Keyword(s):  
Intermediate Filaments ◽  
Ex Vivo ◽  
Eye Lens ◽  
Approaches To Study

Ellagic acid, a new antiglycating agent: its inhibition of Nϵ-(carboxymethyl)lysine

2012 ◽  
Vol 442 (1) ◽  
pp. 221-230 ◽  
Author(s):  
Puppala Muthenna ◽  
Chandrasekhar Akileshwari ◽  
G. Bhanuprakash Reddy
Keyword(s):  
Ellagic Acid ◽  
Ex Vivo ◽  
Total Soluble Protein ◽  
Eye Lens ◽  
Glycation End Products ◽  
Carboxymethyl Lysine ◽  
And Function ◽  
Age Inhibition

Non-enzymatic glycation is a complex series of reactions between reducing sugars and amino groups of proteins. Accumulation of AGEs (advanced glycation end-products) due to non-enzymatic glycation has been related to several diseases associated with aging and diabetes. The formation of AGEs is accelerated in hyperglycaemic conditions, which alters the structure and function of long-lived proteins, thereby contributing to long-term diabetic complications. The present study describes AGE inhibition and the mechanism of action of a new antiglycating agent, EA (ellagic acid), a flavonoid present in many dietary sources. Inhibition of AGE formation by EA was demonstrated with different proteins, namely eye lens TSP (total soluble protein), Hb (haemoglobin), lysozyme and BSA, using different glycating agents such as fructose, ribose and methylglyoxal by a set of complementary methods. These results suggest that the antiglycating action of EA seems to involve, apart from inhibition of a few fluorescent AGEs, predominantly inhibition of CEL [Nϵ-(carboxyethyl)lysine] through scavenging of the dicarbonyl compounds. Furthermore, MALDI–TOF-MS (matrix-assisted laser-desorption ionisation–time-of-flight MS) analysis confirms inhibition of the formation of CEL on lysozyme on in vitro glycation by EA. Prevention of glycation-mediated β-sheet formation in Hb and lysozyme by EA confirm its antiglycating ability. Inhibition of glycosylated Hb formation in human blood under ex vivo high-glucose conditions signifies the physiological antiglycating potential of EA. We have also determined the effectiveness of EA against loss of eye lens transparency through inhibition of AGEs in the lens organ culture system. These findings establish the antiglycating potential of EA and its in vivo utility in controlling AGE-mediated diabetic pathologies.

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