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Protein Glycosylation

Protein Glycosylation

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.
Glycosylation occurs in...

Proteoglycans

Proteoglycans

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,...

Oligosaccharide Assembly

Oligosaccharide Assembly

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.
Multiple sugar molecules that may or may...

Polyprotic Acids

Polyprotic Acids

Acids are classified by the number of protons per molecule that they can give up in a reaction. Acids such as HCl, HNO3, and HCN that contain one ionizable hydrogen atom in each molecule are called monoprotic acids. Their reactions with water are:

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Updated: Apr 7, 2026

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

Published on: April 11, 2014

Ascorbic acid and protein glycation in vitro.

Izabela Sadowska-Bartosz¹, Grzegorz Bartosz²

¹Department of Biochemistry and Cell Biology, University of Rzeszow, Zelwerowicza St. 4, PL 35-601 Rzeszow, Poland.

Chemico-Biological Interactions

|July 12, 2015

Summary

This summary is machine-generated.

Ascorbic acid (AA) acts as a proglycating agent in cell-free systems but an antiglycating agent when cellular recycling occurs. This dual role of vitamin C impacts protein modification and cellular health.

Keywords:

Antioxidant Ascorbic acid Bovine serum albumin Erythrocyte Glycation

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Area of Science:

Biochemistry
Cell Biology
Nutritional Science

Background:

Ascorbic acid (vitamin C) is a vital antioxidant with complex roles in cellular metabolism.
Glycation and glycoxidation are post-translational modifications implicated in aging and disease.
Cellular metabolic pathways can influence the biochemical activity of ascorbic acid.

Purpose of the Study:

To investigate the contrasting effects of ascorbic acid on protein glycation in vitro.
To determine if cell-dependent recycling influences ascorbic acid's role in glycoxidation and glycation.
To elucidate the dual proglycating and antiglycating properties of ascorbic acid.

Main Methods:

In vitro experiments using a cell-free system with bovine serum albumin (BSA) and glucose.
Incubation of erythrocytes with ascorbic acid under varying glucose concentrations.
Assessment of erythrocyte hemolysis, hemoglobin and membrane glycation, and enzyme activities (catalase, acetylcholinesterase).
Measurement of glutathione levels in erythrocytes.

Main Results:

In a cell-free system, ascorbic acid enhanced BSA glycoxidation and induced glycation.
Ascorbic acid did not affect erythrocyte hemolysis, hemoglobin glycation, or catalase inactivation.
Ascorbic acid protected acetylcholinesterase from high glucose-induced inactivation and enhanced glutathione loss.

Conclusions:

Ascorbic acid exhibits a dual role: proglycating in the absence of cellular recycling and antiglycating when metabolic recycling is present.
The cellular environment significantly modulates the biochemical effects of ascorbic acid on proteins and cellular components.
Understanding this duality is crucial for evaluating the physiological impact of ascorbic acid in health and disease.