Recent advances in histone glycation: emerging role in diabetes and cancer

Ever increasing information on genome and proteome has offered fascinating details and new opportunities to understand the molecular biology. It is now known that histone proteins surrounding the DNA play a crucial role in the chromatin structure and function. Histones undergo a plethora of posttranslational enzymatic modifications that influence nucleosome dynamics and affect DNA activity. Earlier research offered insights into the enzymatic modifications of histones; however, attention has been diverted to histone modifications induced by by-products of metabolism without enzymatic engagement in the last decade. Nonenzymatic modifications of histones are believed to be crucial for epigenetic landscape, cellular fate and for role in human diseases. Glycation of histone proteins constitutes the major nonenzymatic modifications of nuclear proteins that have implications in diabetes and cancer. It has emerged that glycation damages nuclear proteins, modifies amino acids of histones at crucial locations, generates adducts affecting histone chromatin interaction, develops neo-epitopes inducing specific immune response and impacts cell function. Presence of circulating antibodies against glycated histone proteins in diabetes and cancer has shown immunological implications with diagnostic relevance. These crucial details make histone glycation an attractive focus for investigators. This review article, therefore, makes an attempt to exclusively summarize the recent research in histone glycation, its impact on structural integrity of chromatin and elaborates on its role in diabetes and cancer. The work offers insights for future scientists who investigate the link between metabolism, biomolecular structures, glycobiology, histone-DNA interactions in relation to diseases in humans.

Automated summary

Recent research has highlighted the importance of glycation as a major nonenzymatic modification of histone proteins, impacting epigenetic landscape, cellular fate, and human diseases such as diabetes and cancer. Glycation damages nuclear proteins, modifies amino acids of histones at crucial locations, affects histone chromatin interaction, induces specific immune response, and impacts cell function. Circulating antibodies against glycated histone proteins in diabetes and cancer suggest immunological implications with diagnostic relevance. These crucial details make histone glycation an attractive focus for investigators studying the link between metabolism, biomolecular structures, glycobiology, histone-DNA interactions, and diseases in humans.