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Related Concept Videos

Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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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.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Acute Pancreatitis II: Pathophysiology01:21

Acute Pancreatitis II: Pathophysiology

The pathophysiology of acute pancreatitis centers on injury to pancreatic acinar cells, which initiates a cascade of harmful intracellular events.This injury leads to premature activation of trypsinogen to trypsin in the pancreas. Trypsin then activates other digestive enzymes, such as chymotrypsin, elastase, and phospholipase A2, which begin breaking down pancreatic tissue. The resulting autodigestion causes local inflammation, tissue swelling, hemorrhage, and fat necrosis.Injured acinar cells...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
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...

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Emerging functional roles of cathepsin E.

Nousheen Zaidi1, Clemens Hermann1, Timo Herrmann1

  • 1Medical and Natural Sciences Research Centre, University of Tubingen, Ob dem Himmelreich 7, 72074 Tubingen, Germany; Interfacultary Institute of Biochemistry, University of Tubingen, Germany.

Biochemical and Biophysical Research Communications
|October 22, 2008
PubMed
Summary

Cathepsin E, an aspartic protease, plays roles in various bodily processes. This review details its functions and links deficiency or overexpression to specific health conditions.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Cathepsin E is an intracellular aspartic protease.
  • It functions within the endolysosomal pathway.
  • Its precise physiological and pathological roles require further elucidation.

Purpose of the Study:

  • To review the known physiological functions of Cathepsin E.
  • To highlight conditions associated with Cathepsin E deficiency.
  • To discuss health implications of Cathepsin E overexpression.

Main Methods:

  • Literature review of research on Cathepsin E.
  • Analysis of studies investigating Cathepsin E's functional roles.
  • Compilation of data on Cathepsin E deficiency and overexpression phenotypes.

Main Results:

  • Cathepsin E is linked to diverse physiological processes.
  • Specific pathological conditions arise from Cathepsin E deficiency.
  • Altered Cathepsin E levels correlate with certain disease states.

Conclusions:

  • Cathepsin E is a significant protease with multifaceted roles.
  • Understanding Cathepsin E's function is crucial for diagnosing and treating related disorders.
  • Further research is needed to fully clarify its functional significance.