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Literature summary for 2.3.1.48 extracted from

  • Kadiyala, C.S.; Zheng, L.; Du, Y.; Yohannes, E.; Kao, H.Y.; Miyagi, M.; Kern, T.S.
    Acetylation of retinal histones in diabetes increases inflammatory proteins: effects of minocycline and manipulation of histone acetyltransferase (HAT) and histone deacetylase (HDAC) (2012), J. Biol. Chem., 287, 25869-25880.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine histone acetylation is significantly increased in retinas from diabetic rats, and this acetylation is inhibited in diabetics treated with minocycline. Both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300, or activators of histone deacetylase, such as theophylline and resveratrol, and are increased by the histone deacetylase inhibitor, suberolylanilide hydroxamic acid. Hyperglycemia causes acetylation of retinal histones and probably other proteins and the acetylation contributes to the hyperglycemia-induced upregulation of proinflammatory proteins and thereby to the development of diabetic retinopathy Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
garcinol both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300 Rattus norvegicus
additional information both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
retina
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Rattus norvegicus
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