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Related Concept Videos

Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
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...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...

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Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
10:44

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

Published on: May 15, 2019

A multifunctional protease inhibitor to regulate endolysosomal function.

Sander I van Kasteren1, Ilana Berlin, Jeff D Colbert

  • 1Division of Cell Signalling and Immunology, College of Life Sciences, University of Dundee, U.K.

ACS Chemical Biology
|September 14, 2011
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel, highly soluble protease inhibitor by linking pepstatin A and cystatin C. This compound effectively targets key proteases within endosomes and lysosomes, impacting cellular processes.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Drug Discovery

Background:

  • Proteases are crucial drug targets, with endosomal proteases implicated in inflammation, cancer, and immunity.
  • Current inhibitors often lack solubility or specificity for multiple protease families.

Purpose of the Study:

  • To synthesize and characterize a novel multifunctional protease inhibitor targeting endosomal and lysosomal proteases.
  • To create a soluble inhibitor capable of suppressing multiple protease families within the endocytic pathway.

Main Methods:

  • Conjugation of pepstatin A to cystatin C to create a single inhibitor molecule.
  • Characterization of the synthesized cystatin-pepstatin inhibitor (CPI).
  • Assessment of CPI cellular uptake and its ability to modulate protease activity.

Main Results:

  • A highly soluble cystatin-pepstatin inhibitor (CPI) was successfully synthesized.
  • CPI effectively suppresses the activity of cathepsins D and E, papain-like cysteine proteases (PLCP), and asparagine endopeptidase (AEP).
  • CPI is cell-permeable and modulates cellular protease activity and biological responses.

Conclusions:

  • The novel CPI offers a promising strategy for generalized, targeted protease inhibition within the endocytic pathway.
  • CPI's ability to inhibit multiple protease families has implications for treating diseases involving these pathways.
  • This approach enables modulation of cellular protease activity and downstream biological effects.