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Related Concept Videos

The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.

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Characterization of proADAMTS5 processing by proprotein convertases.

Jean-Michel Longpré1, Daniel R McCulloch, Bon-Hun Koo

  • 1Department of Pharmacology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Que. J1H 5N4, Canada.

The International Journal of Biochemistry & Cell Biology
|November 11, 2008
PubMed
Summary

The processing of proADAMTS5, crucial for arthritis, occurs extracellularly via furin and PC7. This unique mechanism regulates ADAMTS5 activity and may be significant for osteoarthritis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biomedical Research

Background:

  • ADAMTS5 (aggrecanase-2) is a metalloprotease involved in cartilage destruction in arthritis.
  • It is synthesized as an inactive zymogen, proADAMTS5, requiring propeptide excision for activation.

Purpose of the Study:

  • To characterize the propeptide excision mechanism of proADAMTS5.
  • To investigate the role of proprotein convertases, particularly furin, in ADAMTS5 activation.
  • To understand the implications of its unique processing for osteoarthritis.

Main Methods:

  • Utilized furin-deficient cells and a furin inhibitor to study proADAMTS5 processing.
  • Performed mutagenesis of basic residue sites within the propeptide.
  • Assessed ADAMTS5 activity using substrates aggrecan and versican.
  • Investigated intracellular versus extracellular processing using immunoprecipitation and secretion blockade.

Main Results:

  • ProADAMTS5 is processed by furin and PC7, with processing occurring after Arg(261).
  • Furin processing is essential for ADAMTS5 activity against aggrecan and versican.
  • Unlike other ADAMTS proteases, processed ADAMTS5 and its propeptide are exclusively found extracellularly.
  • Exogenous proADAMTS5 activation confirmed extracellular processing.

Conclusions:

  • ProADAMTS5 processing is a regulated step with unusual extracellular characteristics.
  • The distinct extracellular processing mechanism of ADAMTS5 may be critical in osteoarthritis pathogenesis.
  • Understanding this mechanism offers potential therapeutic targets for arthritis.