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Related Concept Videos

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 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...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Assaying Proteasomal Degradation in a Cell-free System in Plants
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Published on: March 26, 2014

Wheat sprout extract induces changes on 20S proteasomes functionality.

M Amici1, L Bonfili, M Spina

  • 1University of Camerino, Department of Biology M.C.A., 62032 Camerino (MC), Italy.

Biochimie
|January 15, 2008
PubMed
Summary
This summary is machine-generated.

Wheat sprout extract inhibits 20S proteasome activity, impacting cancer cell function and pro-apoptotic protein expression. This study reveals wheat sprouts

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Wheat sprouts are rich in polyphenols with documented antioxidant properties.
  • Polyphenols, like epigallocatechin-3-gallate, can modulate 20S proteasome activity.
  • The 20S proteasome plays a crucial role in cellular protein degradation and homeostasis.

Purpose of the Study:

  • To investigate the impact of wheat sprout extracts on 20S proteasome functionality.
  • To identify and quantify polyphenols within wheat sprout extracts.
  • To assess the effects of wheat sprout extracts on proteasome activity in cancer cells.

Main Methods:

  • Polyphenolic content of wheat sprout extracts analyzed using Folin-Ciocalteau reagent and RP-HPLC.
  • Isolated 20S proteasomes treated with wheat sprout extract to assess enzyme activity (ChT-L, T-L, PGPH, BrAAP).
  • Human colon adenocarcinoma (Caco) cells treated with extract to evaluate proteasome activity and protein expression.

Main Results:

  • Wheat sprout extract gradually inhibited all tested 20S proteasome activities.
  • Low extract concentrations showed minor activation of specific proteasome components.
  • Extract treatment reduced beta-casein degradation and attenuated TPA-induced proteasome activation in Caco cells.
  • Wheat sprout extract affected pro-apoptotic protein expression levels.

Conclusions:

  • Wheat sprout extracts possess potent 20S proteasome inhibitory properties.
  • The extract modulates proteasome activity in both isolated enzymes and cancer cells.
  • Wheat sprout extract demonstrates potential as a modulator of cellular processes relevant to cancer therapy.