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Asian Journal of Research in Medical and Pharmaceutical Sciences, 2457-0745,Vol.: 3, Issue.: 4

Review Article

Advanced Glycation Endproducts, (AGEs): Formation, Complication and Pharmacological Evaluation to Its Inhibition

 

Mohammad Nadeem Khan1* and Ragini Gothawal2

1SOS in Biotechnology, Bastar University, Jagdalpur (C.G.) 494001, India.

2Department of Biotechnology and Bio-informatics centre, Barkatullah University, Bhopal-462001, India.

Article Information

Editor(s):

(1) Aurora Martinez Romero, Professor, Department of Clinical Biochemistry, Juarez University, Durango, Mexico.

(2) Alex Xiucheng Fan, Professor, Department of Biochemistry and Molecular Biology, University of Florida, USA.

(3) John Yahya I. Elshimali, Professor,  Department of Pathology and Oncology, UCLA School of Medicine, Charles R. Drew University of Medicine and Science, California, USA.

(4) BuLang Gao, Professor, Department of Medical Research, Shijiazhuang First Hospital, Hebei Medical University, China and Department of Radiology, Shanghai Jiaotong University Renji Hospital, China.

Reviewers:

(1) Mohsen Kerkeni, Unviversity of Monastir, Tunisia.

(2) Ismail Kucukkurt, Afyon Kocatepe University, Turkey.

(3) Fernanda Maria Machado Maia, Universidade Estadual do Ceará, Brasil.

Complete Peer review History: http://www.sciencedomain.org/review-history/25081

Abstracts

Glycation commonly known as non-enzymatic glycosylation is the result of sugar molecules binding with a protein or lipid molecule without controlling the action of an enzyme. During the process of glycation, early stage glycation compounds are formed first, which subsequently rearrange into final advanced glycation end products (AGEs) structures through a series of very complex chemical reactions and formed methylglyoxal-lysine dimer, glyoxallysine dimer and the deoxyglucosone-lysine dimer . AGEs are involved in many age related diseases such as type–II (diabetic mellitus), cardiovascular disease (the endothelial cell, collagen, fibrinogen are damaged), Alzheimer diseases (amyloid protein are side product of the reaction progressing to AGEs), Cancer (acryl-amide and other side product are related), peripheral neuropathy (the myelin is attached), and other sensory losses such as deafness (due to demyelination), and blindness (mostly due to micro-vascular damage in the retina), this span of diseases is the result of very root level at which glycation interfere with molecular and cellular functioning throughout the body. Pharmacologically influence the process of non-enzymatic glycation and AGE product formation Inhibit the formation of AGEs are purported to have therapeutic potentials in patients with hyperglycemia and age-related diseases. The redox process is believed to play an important role in AGEs formation The best cross-link inhibitors currently available are carnosine, aminoguanidine, metformin and acarbose, whereas others are now becoming available. No cross-link breakers are commercially obtainable as yet, but these will be marketed within 2-3 years. Soon after, combinations of inhibitors and breakers are due to follow.

Keywords :

AGEs; MOLD; GOLD; Amadori reaction; NEG; CML (carboxyl methyl lysine); β-amyloid.

Full Article - PDF    Page 1-18 Article Metrics

DOI : 10.9734/AJRIMPS/2018/40927

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