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Related Concept Videos

Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Proteoglycans01:05

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Transducer Mechanism: Enzyme-Linked Receptors01:27

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Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Specific O-GlcNAc modification at Ser-615 modulates eNOS function.

Kulwant S Aulak1, Jarrod W Barnes1, Liping Tian1

  • 1Inflammation and Immunity, Lerner Research Institute. Cleveland Clinic, OH, USA.

Redox Biology
|September 1, 2020
PubMed
Summary
This summary is machine-generated.

Glucose dysregulation increases O-GlcNAc modification on eNOS in pulmonary arterial hypertension (PAH), impairing nitric oxide production. This novel mechanism involves O-GlcNAc modification of Ser-615, reducing eNOS activity and causing endothelial dysfunction.

Keywords:
Endothelial nitric oxide synthetaseNitric oxideO-GlcNAc modificationPulmonary arterial hypertension

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Area of Science:

  • Cardiovascular Biology
  • Metabolic Disease Research
  • Pulmonary Hypertension Pathophysiology

Background:

  • Idiopathic pulmonary arterial hypertension (IPAH) involves vascular proliferation and nitric oxide (NO) deficiency.
  • Endothelial nitric oxide synthase (eNOS) dysfunction contributes to reduced NO production in IPAH.
  • Glucose dysregulation is linked to increased O-GlcNAc modification in IPAH, but its effect on eNOS is unknown.

Purpose of the Study:

  • To investigate the link between O-GlcNAc modification and eNOS function in pulmonary arterial hypertension (PAH).
  • To identify novel regulatory mechanisms of eNOS under conditions of glucose dysregulation.

Main Methods:

  • Analysis of eNOS O-GlcNAc modification in PAH.
  • Functional characterization of eNOS Ser-615 residue.
  • Assessment of eNOS activity and Ser-1177 phosphorylation.

Main Results:

  • Increased O-GlcNAc modification on eNOS was observed in PAH.
  • Ser-615 was identified as a novel O-GlcNAc modification site on eNOS, leading to reduced eNOS dimerization.
  • O-GlcNAc modification of Ser-615 negatively regulates eNOS activity by inhibiting Ser-1177 phosphorylation.

Conclusions:

  • A novel regulatory mechanism of eNOS is identified, where O-GlcNAc modification of Ser-615 reduces eNOS activity.
  • This mechanism contributes to endothelial dysfunction in PAH under conditions of glucose dysregulation.
  • Targeting O-GlcNAc modification may offer a therapeutic strategy for PAH associated with metabolic disturbances.