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Related Concept Videos

Proteoglycans01:05

Proteoglycans

4.0K
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,...
4.0K
Protein Glycosylation01:25

Protein Glycosylation

7.2K
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...
7.2K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.0K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
7.0K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.0K
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...
3.0K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.5K
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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.5K
Regulated Protein Degradation02:58

Regulated Protein Degradation

7.6K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.6K

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Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments
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Proteolysis: a key post-translational modification regulating proteoglycans.

Timothy J Mead1, Sumit Bhutada1, Daniel R Martin1

  • 1Department of Biomedical Engineering, Cleveland Clinic Lerner Research Institute, Cleveland, Ohio.

American Journal of Physiology. Cell Physiology
|July 5, 2022
PubMed
Summary
This summary is machine-generated.

Proteolysis significantly impacts proteoglycan function and localization, influencing development and disease. Understanding proteoglycan proteolysis is crucial for biological insights and therapeutic strategies.

Keywords:
degradomicsmass spectrometrymetalloproteaseproteaseproteoglycans

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Proteoglycans are complex molecules with diverse roles in tissue mechanics, cell adhesion, and growth factor regulation.
  • Proteolysis, an irreversible post-translational modification, critically affects proteoglycan function, abundance, and localization.
  • Dysregulated proteoglycan proteolysis is implicated in diseases like osteoarthritis, cancer, and inflammation.

Purpose of the Study:

  • To review the actions of proteases on proteoglycans.
  • To illustrate the functional impact of proteolysis on proteoglycans with examples.
  • To discuss strategies for defining proteoglycan cleavage sites and enabling proteoglycanome-wide mapping.

Main Methods:

  • Literature review of protease actions on proteoglycans.
  • Analysis of genetic evidence linking proteolysis to development and disease.
  • Discussion of methods for identifying cleavage sites, including mass spectrometry-based proteomics.

Main Results:

  • Proteolysis is essential for proteoglycan maturation, extracellular matrix remodeling, and generating bioactive fragments (matrikines).
  • Proteolytic fragments of specific proteoglycans (e.g., perlecan, versican, aggrecan) exhibit independent biological activities.
  • Proteoglycan proteolysis is vital for embryonic development but its dysregulation contributes to various pathologies.

Conclusions:

  • Proteolysis is a key regulator of proteoglycan biology, impacting both normal development and disease pathogenesis.
  • Further investigation into proteoglycan proteolysis is needed to fully elucidate its functional significance.
  • Integrating classical methods with mass spectrometry offers a promising approach for comprehensive proteoglycanome-wide proteolytic mapping.