Involvement of disulfide bonds in the condensed structure of facultative heterochromatin and implications on cellular differentiation and aging.
In the previous contribution to this debate, the age-associated disulfide bonding between chromatin proteins was suggested as the primary event leading to cellular aging. Evidence is now presented that S-S bond formation in chromatin may be a programmed event. The possible role of SH oxidating random events in the accumulation of S-S bonds in chromatin with age are also pointed out. Finally, the possible slowing down of the aging process with the sulfhydryl protecting-disulfide reducing agents is discussed together with some supporting experimental results.
D000328:Adult; D000375:Aging; D002454:Cell Differentiation; D002478:Cells, Cultured / Q000187:drug effects; D002610:Cheek; D004229:Dithiothreitol / Q000494:pharmacology; D005260:Female; D006570:Heterochromatin; D006801:Humans; D008623:Mercaptoethanol / Q000494:pharmacology; D009061:Mouth Mucosa / Q000648:ultrastructure
D006570:Heterochromatin; D008623:Mercaptoethanol; D004229:Dithiothreitol