O-GlcNAc, proteinski vezan višefunkcijski mehanizam u staničnoj signalizaciji te njegova uloga u patogenezi šećerne bolesti, stresa i zloćudnih bolesti

Translated title of the contribution: Protein-associated O-GlcNAc, a multifunctional mechanism in cell signaling and its role in the pathogenesis of diabetes, stress and malignant diseases

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Growing evidence suggests that hexosamine biosynthesis pathway (HBP) plays a significant role in the modulation of intracellular signaling transduction pathways. Its end product, UDP-GlcNAc is a substrate for the addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to Ser/Thr residues. This process regulates a wide range of proteins usually by interfering with phosphorylation. O-GlcNAc is a dynamic posttranslational modification, which is essential in normal mammalian cellular function; however, its main significance has been revealed in pathological processes. Since HBP requires glucose, high glucose intake considerably increases the flux through HBP and also increases the ratio of O-GlcNAc-associated proteins. This has an impact on various cellular functions, involving either the traditionally recognized detrimental effects in diabetes and diabetic complications or, as found recently, O-GlcNAc might be beneficial in ischemia/reperfusion injuries. In this review we summarize the current findings in O-GlcNAc research concerning its participation in signaling pathways and cellular processes. We also focus on the impact of O-GlcNAc in diseases such as diabetes, inflammation, development of malignancies or hypoxia-induced injuriers.

Original languageUndefined/Unknown
Pages (from-to)162-177
Number of pages16
JournalBiochemia Medica
Volume17
Issue number2
Publication statusPublished - 2007

Fingerprint

Cell signaling
Hexosamines
Biosynthesis
Medical problems
Diabetes Complications
Glucose
Phosphorylation
Proteins
Uridine Diphosphate
Acetylglucosamine
Pathologic Processes
Post Translational Protein Processing
Reperfusion Injury
Modulation
Fluxes
Inflammation
Substrates
Research
Neoplasms

Keywords

  • Ca
  • Diabetes
  • Malignancy
  • O-GlcNAc
  • Stress response

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, medical

Cite this

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title = "O-GlcNAc, proteinski vezan višefunkcijski mehanizam u staničnoj signalizaciji te njegova uloga u patogenezi šećerne bolesti, stresa i zloćudnih bolesti",
abstract = "Growing evidence suggests that hexosamine biosynthesis pathway (HBP) plays a significant role in the modulation of intracellular signaling transduction pathways. Its end product, UDP-GlcNAc is a substrate for the addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to Ser/Thr residues. This process regulates a wide range of proteins usually by interfering with phosphorylation. O-GlcNAc is a dynamic posttranslational modification, which is essential in normal mammalian cellular function; however, its main significance has been revealed in pathological processes. Since HBP requires glucose, high glucose intake considerably increases the flux through HBP and also increases the ratio of O-GlcNAc-associated proteins. This has an impact on various cellular functions, involving either the traditionally recognized detrimental effects in diabetes and diabetic complications or, as found recently, O-GlcNAc might be beneficial in ischemia/reperfusion injuries. In this review we summarize the current findings in O-GlcNAc research concerning its participation in signaling pathways and cellular processes. We also focus on the impact of O-GlcNAc in diseases such as diabetes, inflammation, development of malignancies or hypoxia-induced injuriers.",
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author = "T. Nagy and A. Miseta and G. Kov{\'a}cs",
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AU - Nagy, T.

AU - Miseta, A.

AU - Kovács, G.

PY - 2007

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AB - Growing evidence suggests that hexosamine biosynthesis pathway (HBP) plays a significant role in the modulation of intracellular signaling transduction pathways. Its end product, UDP-GlcNAc is a substrate for the addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to Ser/Thr residues. This process regulates a wide range of proteins usually by interfering with phosphorylation. O-GlcNAc is a dynamic posttranslational modification, which is essential in normal mammalian cellular function; however, its main significance has been revealed in pathological processes. Since HBP requires glucose, high glucose intake considerably increases the flux through HBP and also increases the ratio of O-GlcNAc-associated proteins. This has an impact on various cellular functions, involving either the traditionally recognized detrimental effects in diabetes and diabetic complications or, as found recently, O-GlcNAc might be beneficial in ischemia/reperfusion injuries. In this review we summarize the current findings in O-GlcNAc research concerning its participation in signaling pathways and cellular processes. We also focus on the impact of O-GlcNAc in diseases such as diabetes, inflammation, development of malignancies or hypoxia-induced injuriers.

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