Evaluation of Dry Fasting Effect during Ramadan on Protein Glycation in Saudi Individuals

Abstract

Introduction: The non-enzymatic protein glycation alters protein function and contributes to many biochemical disorders. The accumulation of advanced glycation end-products (AGEs) is associated with the complications of diabetes, kidney disease, metabolic disorders and degenerative diseases. 
 Objectives: This study was designed to measure the level of some glycated proteins such as glycated insulin and glycated hemoglobin in Saudi volunteers before and after dry fasting in Ramadan.
 Methods: Blood samples were collected twice; first sample (before) and second sample (after) dry fasting. The study included 45 Saudi male volunteers, whose ages ranged between23 and 52 years They were divided into four groups: healthy, type II diabetic patients, smokers, and obese individuals. Plasma glucose level and HbA1c were measured immediately using (Beckman coulter). Assessment of insulin resistance was determined using the equation of homeostasis model for insulin resistance (HOMA-IR). Plasma insulin level and glycated insulin % were assayed by TSQ Vantage Triple Stage Quadruple LC/MS Mass Spectrometer from Thermo Scientific.
 Results: Level of HbA1c, HOMA IR and glycated insulin in healthy, type II diabetic patients, smokers, and obese individuals showed significant decrease in the second sample. The level of HbA1c showed a significant decrease (p-value <0.0001) after dry fasting (5.69 ± 1.55 %), (6.14 ± 1.77%). The level of HOMA IR showed significant decrease (p-value <0.0001) after dry fasting (1.97 ± 1), (2.46 ± 1.28). The level of glycated insulin showed significant decrease (p-value <0.0001) after dry fasting (6.25 ± 2%), (7.71 ± 2.48%).
 Conclusion: Glucose, HbA1c, HOMA IR, and glycated insulin levels showed a significant decrease after dry fasting. Reduced protein glycation and formation of advanced glycation end products, can improve the clinical course of many medical disorders. More researches are needed to understand the molecular mechanisms behind glycation-induced clinical disorders and diseases, as well as to correlate these mechanisms to the diagnosis and prevention of lifestyle-related diseases.